Standard Treatment Remains the Recommended Approach for Patients with Bone Sarcoma Who Underwent Unplanned Surgery: Report from the Japanese Musculoskeletal Oncology Group

Background: The results of operations are not planned for bone sarcomas has not often discussed. However, it is important to recognize patterns, treatment, and clinical outcome of the operation was not planned for patients with bone sarcomas. The aim of this multicenter study to characterize the clinical outcome of patients with bone sarcoma who undergo planned operations.

Patients and methods: Data from 43 patients with bone sarcoma who undergo planned operations between 2006 and 2017 was obtained from 23 hospitals in Japan. These included 18 cases of osteosarcoma, Ewing sarcoma of 9, 8 of chondrosarcoma, and 6 undifferentiated pleomorphic sarcoma. The study involved 28 men and 15 women, with an average age of 46 years. The duration of the average follow-up was 59 months.

Results: The main primary tumor sites are the femur (n = 19), spine (n = 6), pelvis (n = 5), the tibia (n = 3), and humerus (n = 3). Diagnosis principal is benign bone tumors (n = 24), trauma (n = 7), bone metastases (n = 5), osteomyelitis (n = 4), degeneration (n = 2), and unknown (n = 1). As unplanned surgery, curettage, with or without bone graft, performed in 26 patients; Internal fixation is done at 7; spine surgery at 5; arthroplasty in 4; and arthroscopy in one.

Thirty-eight patients received standard treatments extra. Thirty-four patients underwent surgical resection of the tumor, including amputation (n = 10), and the remaining 4 receive radiotherapy or carbon ion radiotherapy for the treatment of additional standards. Level 5-year disease-specific survival (DSS) in patients with osteosarcoma, Ewing sarcoma, and chondrosarcoma was 65.5%, 58.3% and 72.9%, respectively. Twelve patients (27.9%) developed local recurrence (LR); among a total of 43 patients studied, the level of 5-year DSS was significantly worse for those who develop LR compared with those who did not (p = 0.03). 5-year DSS levels in patients with and without LR was 44% and 73.8%, respectively.

Conclusions: We recommend that patients undergoing surgery underwent unplanned given standard treatment, including the option to amputation because here, LR proved to be a risk factor for decreased DSS.

The Pathogenesis and Prevention Port-Site Metastasis in Gynecologic Oncology

Port-site metastases (PSM) is a specific and challenging complications of laparoscopic gynecologic oncology procedures. Research has shown that PSM is associated with morbidity and poor results. The exact pathogenesis of PSM in gynecological patients is not clear. Some precautions of PSM has been discussed in the relevant literature, and novel approaches to prevent this complication rarely keep up. In this review, we summarize the potential mechanisms of PSM and discuss the controversy and benefits of measures proposed prevention of PSM in gynecologic oncology.

We conducted a literature search using Medline database to identify studies of the pathogenesis and prevention of laparoscopic PSM. The hypothesis of the pathogenesis PSM at the center of the body’s immune response, pneumoperitoneum, contamination of wounds and surgical methods. convincing evidence of effective prevention of PSM after laparoscopic surgery is less. traditional preventive measures such as irrigation and tumor manipulation must be taken individually.

CO2 insufflation Hyperthermic and humidified CO2 leads to better outcomes in patients with malignant tumors who underwent laparoscopic procedures with the CO2 pneumoperitoneum than normal. Port-resection site showed no advantage in survival and outcome in the event of more injuries. PSM prevention plays an important part in the overall care of patients with gynecological malignancies who underwent laparoscopic procedures.

 Standard Treatment Remains the Recommended Approach for Patients with Bone Sarcoma Who Underwent Unplanned Surgery: Report from the Japanese Musculoskeletal Oncology Group
Standard Treatment Remains the Recommended Approach for Patients with Bone Sarcoma Who Underwent Unplanned Surgery: Report from the Japanese Musculoskeletal Oncology Group

End of the decision on the limitation of treatment in patients with cancer: an empirical analysis of the end-of-life practice of hematology and oncology unit at a university hospital in Germany

Background: The decision to limit treatment (DLTs) were essential to protect patients from overtreatment but it is one of the most ethically challenging situations in the practice of oncology. Ethics Policy Planning in Advance Care and Treatment study Limiting (EPAL), we examined how often DLT preceded the death of the patient and how early they were determined before (T1) and after (T2) the implementation of ethics policies intrainstitutional in DLT.

Methods: This prospective quantitative recruited 1,134 patients with hematology / oncology neoplasia within a period of 2 × 6 months at the Hospital of the University of Munich, Germany. Information on admission, discharge, diagnosis, age, DLT, date and place of death, and the time span between the initial determination of the DLT and the death of a patient are recorded using a standard form.

Results: Overall, 21% (n = 236) of the 1,134 patients, DLT was made. After the implementation of the policy, the proportion of reduction (26% T1 / T2 16%). However, the decision was more comprehensive, including more frequent combinations of ‘Do Not Resuscitate’ and ‘no intensive care unit’ (44% T1 / T2 64%). The median time between the determination of DLT and the patient’s death is equally short with 6 days in regular wards (each T1 / T2) and 10.5 / 9 (T1 / T2) days in the palliative care unit. For patients with solid tumors, DLTs made earlier in both routine and palliative care units than the deceased with hematologic neoplasia.

Mouse FLT-4/VEGFR-3 Control/blocking peptide #1

FLT41-P 100 ug
EUR 196.8

Rabbit anti VEGFR-1/Flt-1 (human)

102-PA20S 100ug
EUR 240

Mouse anti VEGFR-1/Flt-1 (#EWC) (human)

101-M24 100ug
EUR 297.6

Mouse anti VEGFR-1/Flt-1 (#EIC) (human)

101-M26 100ug
EUR 297.6

Mouse anti VEGFR-1/Flt-1 (#EWF) (human)

101-M28 100ug
EUR 297.6

Mouse anti VEGFR-1/Flt-1 (#EWI) (human)

101-M30 100ug
EUR 297.6

Mouse anti VEGFR-3/Flt-4 (#1) (human)

101-M36 100ug
EUR 297.6

Mouse Anti-Human VEGFR-1/Flt-1

MBS690002-01mg 0.1mg
EUR 430

Mouse Anti-Human VEGFR-1/Flt-1

MBS690002-5x01mg 5x0.1mg
EUR 1645

Mouse Anti-Human VEGFR-1/Flt-1

MBS690109-005mg 0.05mg
EUR 450

Mouse Anti-Human VEGFR-1/Flt-1

MBS690109-5x005mg 5x0.05mg
EUR 1725

Mouse Anti-Human VEGFR-1/Flt-1

MBS690355-01mg 0.1mg
EUR 450

Mouse Anti-Human VEGFR-1/Flt-1

MBS690355-5x01mg 5x0.1mg
EUR 1725

Mouse Anti-Human VEGFR-1/Flt-1

MBS690361-01mg 0.1mg
EUR 450

Mouse Anti-Human VEGFR-1/Flt-1

MBS690361-5x01mg 5x0.1mg
EUR 1725

Mouse Anti-Human VEGFR-1/Flt-1

MBS690384-005mg 0.05mg
EUR 430

Mouse Anti-Human VEGFR-1/Flt-1

MBS690384-5x005mg 5x0.05mg
EUR 1645

Mouse Anti-Human VEGFR-1/Flt-1

MBS690483-005mg 0.05mg
EUR 430

Mouse Anti-Human VEGFR-1/Flt-1

MBS690483-5x005mg 5x0.05mg
EUR 1645

Mouse Anti-Human VEGFR-1/Flt-1

MBS690832-01mg 0.1mg
EUR 430

Mouse Anti-Human VEGFR-1/Flt-1

MBS690832-5x01mg 5x0.1mg
EUR 1645

Anti-Human VEGFR-1/Flt-1 Antibody

101-MBi24 50 µg
EUR 246.75
Description: Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA.

Anti-Human VEGFR-1/Flt-1 Antibody

101-MBi30 50 µg
EUR 189
Description: Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA.

Anti-Human VEGFR-1/Flt-1 Antibody

102-PA20 200 µg
EUR 173.25
Description: Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA.

Anti-Human VEGFR-1/Flt-1 Antibody

102-PABi20 50 µg
EUR 157.5
Description: Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA.

anti- VEGFR-1/FLT-1 antibody

FNab09393 100µg
EUR 606.3
Description: Antibody raised against VEGFR-1/FLT-1

Mouse anti VEGFR-1/Flt-1-Biotin (#EWF) (human)

101-MBi28 50ug
EUR 297.6

Human VEGFR-1/Flt-1 (D5), soluble

MBS691664-002mg 0.02mg
EUR 380

Human VEGFR-1/Flt-1 (D5), soluble

MBS691664-5x002mg 5x0.02mg
EUR 1410

Human VEGFR-1/Flt-1 (D5), soluble

MBS691669-0005mg 0.005mg
EUR 265

Human VEGFR-1/Flt-1 (D5), soluble

MBS691669-5x0005mg 5x0.005mg
EUR 890

Human VEGFR-1/Flt-1 (D3), soluble

MBS691717-002mg 0.02mg
EUR 450

Human VEGFR-1/Flt-1 (D3), soluble

MBS691717-5x002mg 5x0.02mg
EUR 1725

Human VEGFR-1/Flt-1 (D4), soluble

MBS691847-0005mg 0.005mg
EUR 310

Human VEGFR-1/Flt-1 (D4), soluble

MBS691847-5x0005mg 5x0.005mg
EUR 1110

Human VEGFR-1/Flt-1 (D3), soluble

MBS692000-0005mg 0.005mg
EUR 310

Human VEGFR-1/Flt-1 (D3), soluble

MBS692000-5x0005mg 5x0.005mg
EUR 1110

Human VEGFR-1/Flt-1 (D4), soluble

MBS692119-002mg 0.02mg
EUR 450

Human VEGFR-1/Flt-1 (D4), soluble

MBS692119-5x002mg 5x0.02mg
EUR 1725

Human VEGFR-1/Flt-1 (native), soluble

MBS691505-0005mg 0.005mg
EUR 265

Human VEGFR-1/Flt-1 (native), soluble

MBS691505-5x0005mg 5x0.005mg
EUR 890

Human VEGFR-1/Flt-1 (native), soluble

MBS691991-002mg 0.02mg
EUR 380

Human VEGFR-1/Flt-1 (native), soluble

MBS691991-5x002mg 5x0.02mg
EUR 1410

Mouse anti VEGFR-3/Flt-4-Biotin (#1) (human)

101-MBi36 50ug
EUR 297.6

VEGFR-1 / FLT-1 Antibody

abx239393-100ug 100 ug
EUR 577.2

VEGFR-1/FLT-1 antibody

E39-09393 100ug/100ul
EUR 225
Description: Available in various conjugation types.

VEGFR-1/FLT-1 antibody

CAF50629-100ug 100ug
EUR 312

Anti-Mouse VEGFR-1/Flt-1 Antibody

103-M31 100 µg
EUR 399
Description: Vascular Endothelial Growth Factor (VEGF or VEGF-A) family members are major mediators of vasculogenesis and angiogenesis. Specifically, biological activities attributed to VEGFs include: mitogenic activity on endothelial cells, increased permeability of endothelial cells to proteins, stimulation of monocyte migration across endothelial cells and angiogenic activity. Three VEGF family receptors have been described: Flt-1 (fms-like tyrosine kinase) also known as VEGF R1, KDR (kinase-insert domain-containing receptor) also known as Flk-1 and VEGF R2, and Flt-4 also known as VEGF R3. The three receptors contain seven extracellular immunoglobulin-like domains and share substantial sequence homology. In addition, neuropilin-1, a neuronal receptor, also acts as a co-receptor for VEGF when expressed on vascular endothelial cells, endothelial cell progenitors and monocytes. VEGF R1 is expressed primarily on endothelial cells but is also found on human peripheral blood monocytes. Through its endothelial mitogenic and hyperpermeability activities, VEGF influences a variety of immune functions related to wound healing and blood protein traffic across endothelial barriers.

Recombinant Human FLT-1/VEGFR-1 Protein

RP01137 50μg
EUR 308.75

Recombinant Human FLT-1/VEGFR-1 Protein

RP02099 100μg
EUR 205.47

Human VEGFR-1/Flt-1 (D3)-His, soluble

MBS692528-005mg 0.05mg
EUR 725

Human VEGFR-1/Flt-1 (D3)-His, soluble

MBS692528-5x005mg 5x0.05mg
EUR 2965

Rabbit anti VEGFR-3/Flt-4 (human)

102-PA22AG 50ug
EUR 240

Rabbit anti VEGFR-3/Flt-4 (human)

102-PA22S 100ug
EUR 240

Anti-Human VEGFR-3/FLT-4 (#1) Antibody

MBS4158541-01mg 0.1mg
EUR 920

Anti-Human VEGFR-3/FLT-4 (#1) Antibody

MBS4158541-5x01mg 5x0.1mg
EUR 3880

Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble

MBS691483-005mg 0.05mg
EUR 395

Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble

MBS691483-5x005mg 5x0.05mg
EUR 1490

Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble

MBS691782-001mg 0.01mg
EUR 245

Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble

MBS691782-5x001mg 5x0.01mg
EUR 805

Active Recombinant Human FLT-1/VEGFR-1 Protein

RP01188 5 μg
EUR 32.5

Biotinylated Recombinant Human FLT-1/VEGFR-1 Protein

RP02100 500μg
EUR 2843.75

Anti-Human VEGFR-l/Flt-1 (#EWC) Antibody

MBS4158536-01mg 0.1mg
EUR 920

Anti-Human VEGFR-l/Flt-1 (#EWC) Antibody

MBS4158536-5x01mg 5x0.1mg
EUR 3880

Anti-Human VEGFR-l/Flt-1 (#EIC) Antibody

MBS4158537-01mg 0.1mg
EUR 920

Anti-Human VEGFR-l/Flt-1 (#EIC) Antibody

MBS4158537-5x01mg 5x0.1mg
EUR 3880

Anti-Human VEGFR-l/Flt-1 (#EWF) Antibody

MBS4158538-01mg 0.1mg
EUR 920

Anti-Human VEGFR-l/Flt-1 (#EWF) Antibody

MBS4158538-5x01mg 5x0.1mg
EUR 3880

Human VEGFR-1/Flt-1 (D5), soluble Recombinant Protein

S01-011 5 µg
EUR 73.5
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-5 (sVEGFR-1(D5)) is a 70 kDa protein. The baculovirus generated, recombinant human sVEGFR-1 is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 5 extracellular domains, which contain all the information necessary for high affinity ligand binding. The receptor monomers have a mass of approximately 70 kDa. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (D5), soluble Recombinant Protein

S01-012 20 µg
EUR 157.5
Description: Recombinat human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-5 (sVEGFR-1(D5)) is a 70 kDa protein containing amino acid residues. The baculovirus generated, recombinant human sVEGFR-1 is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 5 extracellular domains, which contain all the information necessary for high affinity ligand binding. The receptor monomers have a mass of approximately 70 kDa. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVE supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (D4), soluble Recombinant Protein

S01-013 5 µg
EUR 103.95
Description: Recombinant Human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-4 (sVEGFR-1(D4)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 4 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 55 kDa containing 457 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (D4), soluble Recombinant Protein

S01-014 20 µg
EUR 199.5
Description: Recombinant Human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-4 (sVEGFR-1(D4)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 4 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 55 kDa containing 457 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (D3), soluble Recombinant Protein

S01-015 5 µg
EUR 103.95
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-3 (sVEGFR-1(D3)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 3 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 45 kDa containing 352 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (D3), soluble Recombinant Protein

S01-016 20 µg
EUR 199.5
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-3 (sVEGFR-1(D3)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 3 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 45 kDa containing 352 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (native), soluble Recombinant Protein

S01-009 5 µg
EUR 73.5
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1) is the naturally occurring form and was cloned from total RNA of human umbilical vein endothelial cells. The recombinant mature sVEGFR-1 is a glycosylated monomeric protein with a mass of approximately 96 kDa. The soluble receptor precursor protein consists of the first 6 extracellular domains (Met1-His688) containing the unique 31 amino acids residues at the C-terminus. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly, a naturally occurring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (native), soluble Recombinant Protein

S01-010 20 µg
EUR 157.5
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1) is the naturally occurring form and was cloned from total RNA of human umbilical vein endothelial cells. The recombinant mature sVEGFR-1 is a glycosylated monomeric protein with a mass of approximately 96 kDa. The soluble receptor protein consists of the first 6 extracellular domains (Met1-His688) containing the unique 31 amino acids residues at the C-terminus. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly, a naturally occurring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis binding VEGF with the same affinity as the full-length receptor.

Anti-Inflammatory Peptide 1

004-01 200 μg
EUR 27

Anti-Mouse VEGFR-2/Flk-1 (Peptide), soluble Antibody

103-PA19S 100 µg
EUR 126
Description: The antibody recognizes solely the endogenous soluble form of mouse vascular endothelial growth factor receptor 2, alos known as CD309, VEGFR2, KDR, protein tyrosine kinase receptor flk-1, and fetal liver kinase-1. The endogenous soluble mouse esFlk-1 generated by alternative splicing consists of the first 6 Ig-like loops followed by the unique C-terminal end: GMEASLGDRIAMP. Flk-1 is a member of the tyrosine protein kinase family, sub-family CSF-1/PDGF, that contains a single pass transmembrane receptor with a protein kinase domain and seven immunoglobulin-like domains in the extracellular region. Flk-1 is expressed at high levels in adult heart, lung, kidney, brain, and skeletal muscle; other tissues express at lower levels. Flk-1 is a receptor for VEGF-A or fully processed VEGF-C; ligand binding plays a key role in vascular development and vascular permeability.

Rabbit Anti-human FLT-1/VEGFR-1 IgG #1, aff pure

FLT11-A 100 ul
EUR 578.4

Rabbit Anti-Mouse VEGFR-2 Flk-1 (Peptide), soluble

103-PA19 100ug
EUR 240

Defensin I / Human Neutrophil Peptide-1 (HNP-1) (Human)

072-17 100 μg
EUR 370.44

Anti-Hu/Mo VEGFR-1/Flt-1, Antagonistic Antibody

mV1004.1m-h-m 100 µg
EUR 645.75
Description: Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The antibody will bind near the ligand binding site of the receptor and has antagonistic activity by blocking the binding of natural ligands.

RFamide-Related Peptide 1 (RFRP-1) (Human)

048-42 500 μg
EUR 177.12

Human VEGFR-1/Flt-1 (D3)-His, soluble Recombinant Protein

S01-080 50 µg
EUR 378
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-3 (sVEGFR-1(D3)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 3 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 45 kDa containing 352 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

VEGFR-KDR/Flk-1 Antagonist Peptide

H-5896.0001 1.0mg
EUR 691.2
Description: Sum Formula: C77H99N23O18S; CAS# [492444-99-2] net

VEGFR-KDR/Flk-1 Antagonist Peptide

H-5896.0005 5.0mg
EUR 2648.4
Description: Sum Formula: C77H99N23O18S; CAS# [492444-99-2] net

Human VEGFR-3/FLT-4, soluble

MBS691602-001mg 0.01mg
EUR 310

Human VEGFR-3/FLT-4, soluble

MBS691602-5x001mg 5x0.01mg
EUR 1110

Human VEGFR-3/FLT-4, soluble

MBS691970-005mg 0.05mg
EUR 465

Human VEGFR-3/FLT-4, soluble

MBS691970-5x005mg 5x0.05mg
EUR 1805

Human VEGFR-3/FLT-4, soluble

MBS692181-0005mg 0.005mg
EUR 250

Human VEGFR-3/FLT-4, soluble

MBS692181-5x0005mg 5x0.005mg
EUR 835

[Tyr0]-RFamide-Related Peptide 1 (RFRP-1) (Human)

048-43 200 μg
EUR 177.12

Anti-Human VEGFR-l/Flt-1 (#EWF) Biotin Antibody

MBS4158553-005mg 0.05mg
EUR 920

Anti-Human VEGFR-l/Flt-1 (#EWF) Biotin Antibody

MBS4158553-5x005mg 5x0.05mg
EUR 3880

Anti-Human VEGFR-3/FLT-4 (CL 1) Biotin Antibody

MBS4158555-005mg 0.05mg
EUR 920

Anti-Human VEGFR-3/FLT-4 (CL 1) Biotin Antibody

MBS4158555-5x005mg 5x0.05mg
EUR 3880

Nesfatin-1-Like Peptide (NLP) (Human)

009-83 100 μg
EUR 469.8

Peptide YY (PYY) (1-36)-Gly (Human)

059-07 100 μg
EUR 295.92

Mouse Anti-Human VEGFR-3/FLT-4

MBS690017-01mg 0.1mg
EUR 450

Mouse Anti-Human VEGFR-3/FLT-4

MBS690017-5x01mg 5x0.1mg
EUR 1725

Mouse Anti-Human VEGFR-3/FLT-4

MBS690153-01mg 0.1mg
EUR 450

Mouse Anti-Human VEGFR-3/FLT-4

MBS690153-5x01mg 5x0.1mg
EUR 1725

Mouse Anti-Human VEGFR-3/FLT-4

MBS690532-005mg 0.05mg
EUR 450

Mouse Anti-Human VEGFR-3/FLT-4

MBS690532-5x005mg 5x0.05mg
EUR 1725

Anti-Human VEGFR-3/FLT-4 Antibody

101-M37 100 µg
EUR 199.5
Description: VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk 1) and VEGFR-3 (FLT-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domains and kinase insert domains in their intracellular regions. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. These receptors play essential roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The VEGFR-3 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 24 aa residue signal peptide. Mature VEGFR-3 is composed of a 751 aa residue extracellular domain, a 22 aa residue transmembrane domain and a 482 aa residue cytoplasmic domain. Both VEGF-C and VEGF-D have been shown to bind and activate VEGF R3 (Flt-4). The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stage of development. It is important for lymphangiogenesis.

Anti-Human VEGFR-3/FLT-4 Antibody

101-M38 100 µg
EUR 399
Description: Receptor tyrosine Kinase VEGFR-3, also known as FLT4, together with VEGFR1 (Flt1) and VEGFR2 (KDR/Flk-1), are the receptors for vascular endothelial growth factors (VEGF). The VEGFR family belongs to the class II subfamily of receptor tyrosine kinases (RTKs), containing a large extracellular region which is composed of seven Ig-like domains (D1–D7), a single transmembrane (TM) helix and cytoplasmic region with a tyrosine kinase activity. In VEGFR-3, the fifth Ig homology domain is proteolytically cleaved which results in polypeptides which remain linked by two disulfide bonds. VEGFR-3 is widely expressed on all endothelial cells in early embryogenesis, while, in adult tissues, VEGFR-3 expression disappears from the vascular endothelial cells and is observed only on the lymphatic endothelium. VEGF-C and VEGF-D activation of VEGFR-3 plays an important role in the formation of the lymphatic vessel system.

Anti-Human VEGFR-3/FLT-4 Antibody

101-M870 100 µg
EUR 399
Description: Receptor tyrosine Kinase VEGFR-3, also known as FLT4, together with VEGFR1 (Flt1) and VEGFR2 (KDR/Flk-1), are the receptors for vascular endothelial growth factors (VEGF). The VEGFR family belongs to the class II subfamily of receptor tyrosine kinases (RTKs), containing a large extracellular region which is composed of seven Ig-like domains (D1–D7), a single transmembrane (TM) helix and cytoplasmic region with a tyrosine kinase activity. In VEGFR-3, the fifth Ig homology domain is proteolytically cleaved which results in polypeptides which remain linked by two disulfide bonds. VEGFR-3 is widely expressed on all endothelial cells in early embryogenesis, while, in adult tissues, VEGFR-3 expression disappears from the vascular endothelial cells and is observed only on the lymphatic endothelium. VEGF-C and VEGF-D activation of VEGFR-3 plays an important role in the formation of the lymphatic vessel system.

Anti-Human VEGFR-3/FLT-4 Antibody

102-PA22 200 µg
EUR 147
Description: Receptor tyrosine Kinase VEGFR-3, also known as FLT4, together with VEGFR1 (FIT1) and VEGFR2 (KDR/Flk-1), are the receptors for vascular endothelial growth factors (VEGF). The VEGFR family belongs to the class II subfamily of receptor tyrosine kinases (RTKs), containing a large extracellular region which is composed of seven Ig-like domains (D1–D7), a single transmembrane (TM) helix and cytoplasmic region with a tyrosine kinase activity. In VEGFR-3, the fifth Ig homology domain is proteolytically cleaved which results in polypeptides remain linked by two disulfide bonds. VEGFR-3 is widely expressed on all endothelia cells in early embryogenesis, while, in adult tissues, VEGFR-3 expression disappears from the vascular endothelial cells and is observed only on the lymphatic endothelium. VEGF-C and VEGF-D activation of VEGFR-3 plays an important role in the formation of the lymphatic vessel system.

Anti-Human VEGFR-3/FLT-4 Antibody

102-PABi22 50 µg
EUR 157.5
Description: Receptor tyrosine Kinase VEGFR-3, also known as FLT4, together with VEGFR1 (FIT1) and VEGFR2 (KDR/Flk-1), are the receptors for vascular endothelial growth factors (VEGF). The VEGFR family belongs to the class II subfamily of receptor tyrosine kinases (RTKs), containing a large extracellular region which is composed of seven Ig-like domains (D1–D7), a single transmembrane (TM) helix and cytoplasmic region with a tyrosine kinase activity. In VEGFR-3, the fifth Ig homology domain is proteolytically cleaved which results in polypeptides remain linked by two disulfide bonds. VEGFR-3 is widely expressed on all endothelia cells in early embryogenesis, while, in adult tissues, VEGFR-3 expression disappears from the vascular endothelial cells and is observed only on the lymphatic endothelium. VEGF-C and VEGF-D activation of VEGFR-3 plays an important role in the formation of the lymphatic vessel system.

Rabbit Anti-Human VEGFR-2/KDR (Peptide), soluble

102-PA19 100ug
EUR 240

Anti-Human VEGFR-2/KDR (Peptide), soluble Antibody

102-PA19S 100 µg
EUR 126
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis.

GnRH Associated Peptide (GAP) (1-13) / GnRH Precursor Peptide (14-26) (Human)

029-03 500 μg
EUR 114.48

GnRH Associated Peptide (GAP) (1-24) / GnRH Precursor Peptide (14-37) (Human)

029-04 100 μg
EUR 114.48

GnRH Associated Peptide (GAP) (1-53) / GnRH Precursor Peptide (14-66) (Human)

029-05 20 μg
EUR 267.84

Mouse Monoclonal Anti-human FLT-1/VEGFR-1 IgG, aff pure

FLT12-M 100 ug
EUR 578.4

Mouse Monoclonal Anti-human FLT-1/VEGFR-1 IgG, aff pure

FLT14-M 100 ug
EUR 578.4

TCAP-1 / Teneurin C-terminal Associated Peptide-1 (Human)

020-16 100 μg
EUR 317.52

SHLP1 / Small Humanin-Like Peptide 1 (Human)

018-75 100 μg
EUR 263.52

RFamide-Related Peptide 1 (RFRP-1) (Human) - FAM Labeled

FG-048-42A 1 nmol
EUR 336.96

Gastrin Releasing Peptide (GRP) (1-16) (Human)

027-08 1 mg
EUR 177.12

Gastrin Releasing Peptide (GRP) (1-17) (Human)

027-42 200 μg
EUR 189

prepro-Endothelin-1 (ET-1) Like Peptide (109-130) amide (Human)

023-11 100 μg
EUR 355.32

Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble Recombinant Protein

SFC-005 10 µg
EUR 57.75
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1(D7)) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-1(D7)/Fc is a disulfide-linked homodimeric protein. The sVEGFR-1(D7)/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.

Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble Recombinant Protein

SFC-006 50 µg
EUR 168
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1(D7)) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-1(D7)/Fc is a disulfide-linked homodimeric protein. The sVEGFR-1(D7)/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.

RFamide-Related Peptide 1 (RFRP-1) (Human) - Rhodamine Labeled

FR-048-42 1 nmol
EUR 336.96

Human VEGFR-3/FLT-4 ELISA (total)

MBS691467-0096mg 0.096mg
EUR 815

Human VEGFR-3/FLT-4 ELISA (total)

MBS691467-5x0096mg 5x0.096mg
EUR 3625

Mouse FLK-1/VEGFR-2 control/blocking peptide # 1

FLK11-P 100 ug
EUR 196.8

Human VEGFR-3 / Flt-4 GENLISA ELISA

KBH0215 1 x 96 wells
EUR 286

Neuroendocrine Regulatory Peptide 1 (NERP-1) / prepro-VGF (281-306) (Human) - Antibody

H-076-89 100 μl
EUR 336.96

Nesfatin-1-Like Peptide(NLP) (Human) - RIA Kit

RK-009-83 125 tubes
EUR 980.64

Bone Forming Peptide 1 (BFP-1) (Human, Rat, Mouse, Bovine, Feline)

080-57 100ug
EUR 196.56

Recombinant Human VEGFR-3/FLT-4 Protein

RP01797 100μg
EUR 42.51

[Tyr0]-RFamide-Related Peptide 1 (RFRP-1) (Human) - I-125 Labeled

T-048-43 10 μCi
EUR 1145.88

[Biotinyl-Gln1]-TCAP-1 / Teneurin C-terminal Associated Peptide-1 (Human)

B-020-16 20 μg
EUR 336.96

Neuroendocrine Regulatory Peptide 1 (NERP-1) / prepro-VGF (281-306) (Human)

076-89 100 μg
EUR 214.92

Rat Anti-Mouse VEGFR-3/FLT-4

MBS690799-01mg 0.1mg
EUR 450

Rat Anti-Mouse VEGFR-3/FLT-4

MBS690799-5x01mg 5x0.1mg
EUR 1725

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (AP)

MBS6443139-01mL 0.1mL
EUR 950

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (AP)

MBS6443139-5x01mL 5x0.1mL
EUR 4120

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (APC)

MBS6443140-01mL 0.1mL
EUR 950

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (APC)

MBS6443140-5x01mL 5x0.1mL
EUR 4120

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (HRP)

MBS6443143-01mL 0.1mL
EUR 950

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (HRP)

MBS6443143-5x01mL 5x0.1mL
EUR 4120

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (PE)

MBS6443149-01mL 0.1mL
EUR 950

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (PE)

MBS6443149-5x01mL 5x0.1mL
EUR 4120

Rabbit Anti-Mouse FLT-1/VEGFR-1 (279-299aa) IgG, aff pure

FLT15-A 100 ul
EUR 578.4

Anti-Mouse VEGFR-3/FLT-4 Antibody

103-M36 100 µg
EUR 246.75
Description: VEGFR-3, also known as FLT4, is a member of the Tyr protein kinase family. The extracellular portion of VEGFR-3 contains 7 immunoglobulin (Ig)-like domains and the cytoplasmic portion contains a protein kinase domain. FLT4 regulates angiogenesis and lymphangiogenesis, its ligands are VEGF-C and D and its binding is mediated by the 2nd and 3rd Ig-like domains of FLT4. During fetal development VEGFR-3 is expressed on endothelial cells, however, in the adult mice, the vascular endothelial cells lose VEGFR-3 expression, but the lymphatic endothelium expresses it constitutively. In addition, VEGFR-3 expression can be induced in tumors with active angiogenesis.

Anti-Mouse VEGFR-3/FLT-4 Antibody

103-M38 100 µg
EUR 399
Description: Receptor tyrosine kinase VEGFR-3, also known as Flt-4, together with VEGFR-1 (Flt-1) and VEGFR-2 (KDR/Flk-1), are the receptors for vascular endothelial growth factors (VEGF). The VEGFR family belongs to the class II subfamily of receptor tyrosine kinases (RTKs), containing a large extracellular region which is composed of seven Ig-like domains (D1–D7), a single transmembrane (TM) helix and cytoplasmic region with a tyrosine kinase activity. In VEGFR-3, the fifth Ig homology domain is proteolytically cleaved which results in polypeptides remaining linked by two disulfide bonds. VEGFR-3 is widely expressed on all endothelial cells in early embryogenesis, while, in adult tissues, VEGFR-3 expression disappears from the vascular endothelial cells and is observed only on the lymphatic endothelium. VEGF-C and VEGF-D activation of VEGFR-3 plays an important role in the formation of the lymphatic vessel system.

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (FITC)

MBS6443142-01mL 0.1mL
EUR 950

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (FITC)

MBS6443142-5x01mL 5x0.1mL
EUR 4120

VEGFR-3/Flt-4

JP27779 96
EUR 611

VEGFR-3/FLT-4

MBS692733-01mg 0.1mg
EUR 725

VEGFR-3/FLT-4

MBS692733-5x01mg 5x0.1mg
EUR 2965

[Tyr0]-Neuroendocrine Regulatory Peptide 1 (NERP-1) (Human) - I-125 Labeled

T-076-93 10 μCi
EUR 1145.88

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (Biotin)

MBS6443141-01mL 0.1mL
EUR 950

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (Biotin)

MBS6443141-5x01mL 5x0.1mL
EUR 4120

FLT1 (FLT, FLT-1, VEGFR1, VEGFR-1, Vascular Endothelial Growth Factor Receptor 1) (AP)

MBS6417421-01mL 0.1mL
EUR 950

FLT1 (FLT, FLT-1, VEGFR1, VEGFR-1, Vascular Endothelial Growth Factor Receptor 1) (AP)

MBS6417421-5x01mL 5x0.1mL
EUR 4120

FLT1 (FLT, FLT-1, VEGFR1, VEGFR-1, Vascular Endothelial Growth Factor Receptor 1) (APC)

MBS6417422-01mL 0.1mL
EUR 950

FLT1 (FLT, FLT-1, VEGFR1, VEGFR-1, Vascular Endothelial Growth Factor Receptor 1) (APC)

MBS6417422-5x01mL 5x0.1mL
EUR 4120

FLT1 (FLT, FLT-1, VEGFR1, VEGFR-1, Vascular Endothelial Growth Factor Receptor 1) (HRP)

MBS6417425-01mL 0.1mL
EUR 950

FLT1 (FLT, FLT-1, VEGFR1, VEGFR-1, Vascular Endothelial Growth Factor Receptor 1) (HRP)

MBS6417425-5x01mL 5x0.1mL
EUR 4120

FLT1 (FLT, FLT-1, VEGFR1, VEGFR-1, Vascular Endothelial Growth Factor Receptor 1) (PE)

MBS6417431-01mL 0.1mL
EUR 950

FLT1 (FLT, FLT-1, VEGFR1, VEGFR-1, Vascular Endothelial Growth Factor Receptor 1) (PE)

MBS6417431-5x01mL 5x0.1mL
EUR 4120

FLT1 (FLT, FLT-1, VEGFR1, VEGFR-1, Vascular Endothelial Growth Factor Receptor 1) (FITC)

MBS6417424-01mL 0.1mL
EUR 950

FLT1 (FLT, FLT-1, VEGFR1, VEGFR-1, Vascular Endothelial Growth Factor Receptor 1) (FITC)

MBS6417424-5x01mL 5x0.1mL
EUR 4120

Neuroendocrine Regulatory Peptide 1 (NERP-1) / prepro-VGF (281-306) (Human) - Purified IgG Antibody

G-076-89 100 μg
EUR 370.44

FLT1 (FLT, FLT-1, VEGFR1, VEGFR-1, Vascular Endothelial Growth Factor Receptor 1) (Biotin)

MBS6417423-01mL 0.1mL
EUR 950

FLT1 (FLT, FLT-1, VEGFR1, VEGFR-1, Vascular Endothelial Growth Factor Receptor 1) (Biotin)

MBS6417423-5x01mL 5x0.1mL
EUR 4120

Human VEGFR-3/FLT-4/Fc Chimera, soluble

SFC-010 50ug
EUR 378

Human VEGFR-3/FLT-4/Fc Chimera, soluble

MBS691672-005mg 0.05mg
EUR 430

Human VEGFR-3/FLT-4/Fc Chimera, soluble

MBS691672-5x005mg 5x0.05mg
EUR 1645

Human VEGFR-3/FLT-4/Fc Chimera, soluble

MBS691800-001mg 0.01mg
EUR 265

Human VEGFR-3/FLT-4/Fc Chimera, soluble

MBS691800-5x001mg 5x0.01mg
EUR 890

NGR Peptide 1

025-74 200 μg
EUR 184.68

Peptide YY (PYY) (Human) - Antibody

H-059-01 100 μl
EUR 469.8

Conclusions: Our results show that the ethics policy in DLT be sensitive to the limitations of treatment in terms of frequency and extension but did not have a significant impact on the time DLT. Since patients with hematological malignancies tend to undergo intensive therapy more frequently during their final days than patients with solid tumors, particular attention should be given to this group. To support the timely discussion, we suggest that the concept of advance care planning.

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