Human Flt-1/VEGFR-1 (D7)-FC Chimera, soluble recombinant Protein

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Product Overview, Sizes and Prices

 

Protein

Synonyms: soluble vascular endothelial growth factor receptor-1, soluble FLT1, soluble VEGFR-1

Source: Insect cells

Purity: ≥ 90 % (SDS-PAGE, silver stained)

Physical state: Lyophilized

Manufacturer:  Active Bioscience

Article No. Size Price  
1399.952.010 10 µg 90 €
1399.952.050 50 µg 235 €

Please inquire for other vial sizes and custom vialing.

 

 

Product Details

Synonyms

soluble vascular endothelial growth factor receptor-1, soluble FLT1, soluble VEGFR-1

 

Description of Human Flt-1/VEGFR-1 (D7)-FC Chimera, soluble

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.

 

Biological Activity

The activity of sVEGFR-1/Fc was determined by its ability to inhibit the VEGF-dependent proliferation of human umbilical vein endothelial cells.

 

Reconstitution

The lyophilized sVEGFR-1/Fc should be reconstituted in water to a concentration not lower than 50µg/ml.

 

Amino Acid Sequence

SKLKDPELSL KGTQHIMQAG QTLHLQCRGE AAHKWSLPEM VSKESERLSI TKSACGRNGK QFCSTLTLNT AQANHTGFYS CKYLAVPTSK KKETESAIYI FISDTGRPFV EMYSEIPEII HMTEGRELVI PCRVTSPNIT VTLKKFPLDT LIPDGKRIIW DSRKGFIISN ATYKEIGLLT CEATVNGHLY KTNYLTHRQT NTIIDVQIST PRPVKLLRGH TLVLNCTATT PLNTRVQMTW SYPDEKNKRA SVRRRIDQSN SHANIFYSVL TIDKMQNKDK GLYTCRVRSG PSFKSVNTSV HIYDKAFITV KHRKQQVLET VAGKRSYRLS MKVKAFPSPE VVWLKDGLPA TEKSARYLTR GYSLIIKDVT EEDAGNYTIL LSIKQSNVFK NLTATLIVNV KPQIYEKAVS SFPDPALYPL GSRQILTCTA YGIPQPTIKW FWHPCNHNHS EARCDFCSNN EESFILDADS NMGNRIESIT QRMAIIEGKN KMASTLVVAD SRISGIYICI ASNKVGTVGR NISFYITDVP NGFHVNLEKM PTEGEDLKLS CTVNKFLYRD VTWILLRTVN NRTMHYSISK QKMAITKEHS ITLNLTIMNV SLQDSGTYAC RARNVYTGEE ILQKKEITIR DQEAPYLLRN LSDHTVAISS STTLDCHANG VPEPQITWFK NNHKIQQEPG IILGPGSSTL FIERVTEEDE GVYHCKATNQ KGSVESSAYL TVQGTRSDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SREEMTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPMLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGK

 

 

 

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