NRP1 Human
Neuropilin-1 isoform a, NRP1, BDCA4, CD304, NP1, NRP, VEGF165R, Vascular endothelial cell growth factor 165 receptor.
Greater than 90.0% as determined by SDS-PAGE.
Description
NRP1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 843 amino acids (22-856a.a.) and having a molecular mass of 94.8kDa. (Molecular size on SDS-PAGE will appear at approximately 100-150kDa).
NRP1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Product Specs
Neuropilin-1 isoform a, NRP1, BDCA4, CD304, NP1, NRP, VEGF165R, Vascular endothelial cell growth factor 165 receptor.
FRNDKCGDTI KIESPGYLTS PGYPHSYHPS EKCEWLIQAP DPYQRIMINF NPHFDLEDRD CKYDYVEVFD GENENGHFRG KFCGKIAPPP VVSSGPFLFI KFVSDYETHG AGFSIRYEIF KRGPECSQNY TTPSGVIKSP GFPEKYPNSL ECTYIVFAPK MSEIILEFES FDLEPDSNPP
GGMFCRYDRL EIWDGFPDVG PHIGRYCGQK TPGRIRSSSG ILSMVFYTDS AIAKEGFSAN YSVLQSSVSE DFKCMEALGM ESGEIHSDQI TASSQYSTNW SAERSRLNYP ENGWTPGEDS YREWIQVDLG LLRFVTAVGT QGAISKETKK KYYVKTYKID VSSNGEDWIT IKEGNKPVLF
QGNTNPTDVV VAVFPKPLIT RFVRIKPATW ETGISMRFEV YGCKITDYPC SGMLGMVSGL ISDSQITSSN QGDRNWMPEN IRLVTSRSGW ALPPAPHSYI NEWLQIDLGE EKIVRGIIIQ GGKHRENKVF MRKFKIGYSN NGSDWKMIMD DSKRKAKSFE GNNNYDTPEL RTFPALSTRF
IRIYPERATH GGLGLRMELL GCEVEAPTAG PTTPNGNLVD ECDDDQANCH SGTGDDFQLT GGTTVLATEK PTVIDSTIQS EFPTYGFNCE FGWGSHKTFC HWEHDNHVQL KWSVLTSKTG PIQDHTGDGN FIYSQADENQ KGKVARLVSP VVYSQNSAHC MTFWYHMSGS HVGTLRVKLR
YQKPEEYDQL VWMAIGHQGD HWKEGRVLLH KSLKLYQVIF EGEIGKGNLG GIAVDDISIN NHISQEDCAK PADLDKKNPE IKIDETGSTP GYEGEGEGDK NISRKPGNVL KTLDPLEHHH HHH.
Product Science Overview
Neuropilin 1 is composed of several distinct domains:
- a1 and a2 domains: These are CUB (complement-binding) domains that are involved in binding to semaphorins.
- b1 and b2 domains: These are coagulation factor V/VIII homology domains that bind to VEGF.
- c domain: This is a MAM (meprin, A5 protein, and receptor protein-tyrosine phosphatase mu) domain that is involved in protein-protein interactions.
- Transmembrane domain: This anchors the protein to the cell membrane.
- Cytoplasmic domain: This is involved in intracellular signaling.
Neuropilin 1 is known to form complexes with other receptors, such as VEGF receptors, to mediate its effects on angiogenesis and cell migration. It is also involved in the immune response by modulating the activity of T cells and dendritic cells .
Recombinant human Neuropilin 1 is produced using various expression systems, including mammalian cells, insect cells, and bacterial cells. The recombinant protein is often tagged with a His-tag or Fc-tag to facilitate purification and detection. It is used in various research applications, including studies on angiogenesis, cancer, and neurobiology.
The recombinant protein is typically purified to high purity (>95%) and tested for bioactivity using functional assays, such as binding to VEGF in an enzyme-linked immunosorbent assay (ELISA) .
Neuropilin 1 is widely studied in the context of cancer research due to its role in promoting tumor growth and metastasis. It is also a target for therapeutic interventions aimed at inhibiting angiogenesis. Additionally, Neuropilin 1 is studied in neurobiology for its role in axon guidance and neuronal development.
In immunology, Neuropilin 1 is investigated for its role in modulating the immune response, particularly in the context of autoimmune diseases and transplant rejection.
