rev:   July 10, 2003

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Human Cytokine/Growth Factor/Chemokines Sample Spec sheets (subject to change without notice):


see below 4 new sVEGFR receptors

see also new Elisa kits for  sVEGFR1 (total), sVEFFR1(free), VEGF-A


Recombinant Human (sVEGFR2) sKDR D1-7

Description: Recombinat Human soluble Endothelial Growth Factor Receptor-2 (sKDRd1-7) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein consists of all 7 extracellular domains, which contain all the information necessary for high affinity ligand binding. The receptor monomers have a mass of approximately 116 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. 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 signaling 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 occuring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.

Source:                                  Insect cells

Molecular Weight:                116 kDa

Specific Activity:                   1 x 105 units/mg

Purity:                        > 95% (SDS-PAGE; HPLC)

Endotoxin level:                    < 0.1 ng/ug of sKDR

Stabilizer:                              none

Buffer:                                   none

Formulation:                          lyophilized


Biological Activity:  The activity of rh sVEGFR-2 was determined by its ability to abolish the binding of iodinated VEGF to solid surfaces or cell surfaces. The ED50 for this effect is typically 10.0 ng/ml.

Reconstitution: The lyophilized human sKDR is soluble in water and most aqueous buffers, The lyophilized powder dshould be reconstituted in water to a concentration of 100 ng/ml. 

Stability: The material is stable for greater than six months at -20° C to -70° C. After the first thawing it is recommended to aliquote the material, because repeated freeze-thaw cycles will decrease the activity. Store at 4°C not longer than 2 days.

Usage:
Human sKDR is offered for research use. Not for drug use. Not for human use.

Catalogue number:    RDI-S01001               Size:    5 µg

Lot number :  001-001                                  Units/vial:       5 x 102

Price:  $188.00  $156.00/3+              Range:          0.1-10.0 ng/ml

Catalogue number:    RDI-S01002                  Size: 50 µg

Lot number :  002-001                                  Units/vial:       5 x 103

Price:  $438.00   $375.00/vial 5+       Range:           0.1-10.0 ng/ml

Literature: [Röckl et al., 1998, Exp Cell Res, 241: 161-170].

Distributed by:RDI Division of Fitzgerald Industries Intl  Pleasant Hill Road  Concord MA 01742-3049

USA

(978) 371-6446 or (800) 370-2222  fax (973) 584-0210    http://www.researchd.com


Recombinant Human (sVEGFR-2-FC Chimera) sKDR-Fc chimera

Description: Recombinat Human soluble Endothelial Growth Factor Receptor-2 (sKDRd1-7) was fused with the Fc of human IgG. The soluble receptor protein consists of all 7 extracellular domains, which contain all the information necessary for high affinity ligand binding. The receptor monomers have a mass of approximately 160kDa.

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. 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 signaling 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 occuring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.

Source:                     Insect cells

Molecular Weight:    160kda

Subunit:                    glycosylated dimer

Purity:                       > 90% (SDS-PAGE; HPLC)

Endotoxin level:       < 0.1 ng/ug of sKDR

Stabilizer:                 none

Buffer:                      PBS;pH7.4

Formulation:             lyophilized

Biological Activity: The activity of rh sKDR-FC was determined by its ability to inhibit the VEGF-dependent proliferation of human umbilical vein endothelial cells. The ED50 for for this effect is typically 10.0-30 ng/ml.

Reconstitution: The lyophilized human sKDR-Fc is soluble in water and most aqueous buffers, The lyophilized powder dshould be reconstituted in water or PBS to a concentration of not less than 100ug/ml.

Stability: The material is stable for greater than six months at -20° C to -70° C. After the first thawing it is recommended to aliquote the material, because repeated freeze-thaw cycles will decrease the activity. Store at 4°C not longer than 2 days.

Usage: Human sKDR-Fc is offered for research use. Not for drug use. Not for human use.

Catalogue number:   RDI-S01005  or RDI-SFC-007     Size: 50 µg

Lot number : S10-005.1.2                

Price: $500.00      $438.00/5+   $406.00/vial 10+   Bulk on request

Range: 0.1-10.0 ng/ml


Recombinant Human sVEGFR-1D1-5

Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1D1-5 (sVEGFR-1D1-5) 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.

Source:                                  Insect cells

Molecular Weight:                70.0 kDa

Specific activity:                    1 x 105 units/mg          

Purity:                        > 95% by SDS-PAGE and HPLC analyses

Endotoxin level:                    < 0.1 ng per mg of VEGFR-1

Stabilizer:                              none

Buffer:                                   Acetic acid; pH 7.2

Formulation:                          lyophilized

Biological Activity:  The activity of rh sVEGFR-1 was determined by its ability to abolish the binding of iodinated VEGF to solid surfaces or cell surfaces. The ED50 for this effect is typically 10 ng/ml. In a 13 day CAM-assay sVEGFR-1 is able to inhibit VEGF stimulated sprouting of capillaries at 30 pM.

Reconstitution: The lyophilized human sVEGFR-1 is soluble in water and most aqueous buffers, The lyophilized powder dshould be reconstituted in water to a concentration of 100 ng/ml.  

Stability: The material is stable for greater than six months at -20° C to -70° C. After the first thawing it is recommended to aliquote the material, because repeated freeze-thaw cycles will decrease the activity. Store at 4°C not longer than 2 days.

Usage: Human sVEGFR-1 is offered for research use. Not for drug use. Not for human use.

Catalogue number:    RDI-S01011   Size:    5 µg

Lot number :              011-001                                   Units/Vial:     5 x 102

Price:  $188.00  $156.00/3+  Range:           0.1-10 ng/ml

Catalogue number:    S01-012          Size:    20 µg

Lot number :              012-001                      Units/Vial:      2 x 103

Price:  $312.00 $250.00/3+   Range:           0.1-10 ng/ml

Literature: [Röckl et al., 1998, Exp Cell Res, 241: 161-170].

 

(978) 371-6446 or (800) 370-2222  fax (973) 584-0210    http://www.researchd.com


Recombinant Human sVEGFR-1D1-6

Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1D1-6 (sVEGFR-1D1-6) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 6 extracellular domains, which contain all the information necessary for high affinity ligand binding. The receptor monomers have a mass of approximately 97 kDa containing 661 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 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.

Source:                                  Insect cells

Molecular Weight:                97 kDa

Specific activity:                    1 x 105 units/mg          

Purity:                        > 95% by SDS-PAGE and HPLC analyses

Endotoxin level:        < 0.1 ng per mg of VEGFR-1

Stabilizer:                              none

Buffer:                                   none

Formulation:                          lyophilized