Cynomolgus Neuropilin-1 Protein 5093

$240.00 – $800.00

Summary

Expression: HEK293
Pure: Yes (HPLC)
Amino Acid Range: Phe22-Pro644

SKU: 5093parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	XP_005564992
express system	HEK293
product tag	C-His
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
background	Neuropilin 1 (NRP1) is a transmembrane glycoprotein that acts as a co-receptor for a number of extracellular ligands including class III/IV semaphorins, certain isoforms of vascular endothelial growth factor and transforming growth factor beta.
molecular weight	The protein has a predicted MW of 71.01 kDa. Due to glycosylation, the protein migrates to 80-100 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Cynomolgus Neuropilin-1 Protein 5093

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
Neuropilin 1 (NRP1) is a transmembrane glycoprotein that acts as a co-receptor for a number of extracellular ligands including class III/IV semaphorins, certain isoforms of vascular endothelial growth factor and transforming growth factor beta.
Protein names Neuropilin-1 (Vascular endothelial cell growth factor 165 receptor) (CD antigen CD304)
Protein family Neuropilin family
Mass 103134Da
Function Cell-surface receptor involved in the development of the cardiovascular system, in angiogenesis, in the formation of certain neuronal circuits and in organogenesis outside the nervous system. Mediates the chemorepulsant activity of semaphorins (PubMed:10688880, PubMed:9288753, PubMed:9529250). Recognizes a C-end rule (CendR) motif R/KXXR/K on its ligands which causes cellular internalization and vascular leakage (PubMed:19805273). It binds to semaphorin 3A, the PLGF-2 isoform of PGF, the VEGF165 isoform of VEGFA and VEGFB (PubMed:10688880, PubMed:19805273, PubMed:9288753, PubMed:9529250). Coexpression with KDR results in increased VEGF165 binding to KDR as well as increased chemotaxis. Regulates VEGF-induced angiogenesis. Binding to VEGFA initiates a signaling pathway needed for motor neuron axon guidance and cell body migration, including for the caudal migration of facial motor neurons from rhombomere 4 to rhombomere 6 during embryonic development (By similarity). Regulates mitochondrial iron transport via interaction with ABCB8/MITOSUR (PubMed:30623799). {ECO:0000250\|UniProtKB:P97333, ECO:0000269\|PubMed:10688880, ECO:0000269\|PubMed:19805273, ECO:0000269\|PubMed:30623799, ECO:0000269\|PubMed:9288753, ECO:0000269\|PubMed:9529250}.; (Microbial infection) Acts as a host factor for human coronavirus SARS-CoV-2 infection. Recognizes and binds to CendR motif RRAR on SARS-CoV-2 spike protein S1 which enhances SARS-CoV-2 infection. {ECO:0000269\|PubMed:33082293, ECO:0000269\|PubMed:33082294}.; [Isoform 2]: Binds VEGF-165 and may inhibit its binding to cells (PubMed:10748121, PubMed:26503042). May induce apoptosis by sequestering VEGF-165 (PubMed:10748121). May bind as well various members of the semaphorin family. Its expression has an averse effect on blood vessel number and integrity. {ECO:0000269\|PubMed:10748121, ECO:0000269\|PubMed:26503042}.
Subellular location [Isoform 2]: Secreted {ECO:0000269\|PubMed:10688880}.; Mitochondrion membrane {ECO:0000305\|PubMed:30623799}; Single-pass type I membrane protein {ECO:0000255}. Cell membrane {ECO:0000269\|PubMed:30623799}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269\|PubMed:30623799}.
Tissues [Isoform 1]: The expression of isoforms 1 and 2 does not seem to overlap. Expressed in olfactory epithelium (at protein level) (PubMed:33082293). Expressed in fibroblasts (at protein level) (PubMed:36213313). Expressed by the blood vessels of different tissues. In the developing embryo it is found predominantly in the nervous system. In adult tissues, it is highly expressed in heart and placenta; moderately in lung, liver, skeletal muscle, kidney and pancreas; and low in adult brain (PubMed:10688880, PubMed:9529250). Expressed in the central nervous system, including olfactory related regions such as the olfactory tubercles and paraolfactory gyri (PubMed:33082293). {ECO:0000269\|PubMed:10688880, ECO:0000269\|PubMed:33082293, ECO:0000269\|PubMed:36213313, ECO:0000269\|PubMed:9529250}.; [Isoform 2]: The expression of isoforms 1 and 2 does not seem to overlap. Found in liver hepatocytes, kidney distal and proximal tubules. {ECO:0000269\|PubMed:10688880}.
Structure Homodimer, and heterodimer with NRP2 (PubMed:17989695). Interacts with FER (By similarity). Interacts with PLXNB1 (PubMed:10520995). Interacts with VEGFA (PubMed:19805273, PubMed:26503042). Interacts with ABCB8/MITOSUR in mitochondria (PubMed:30623799). {ECO:0000250\|UniProtKB:P97333, ECO:0000269\|PubMed:10520995, ECO:0000269\|PubMed:17989695, ECO:0000269\|PubMed:19805273, ECO:0000269\|PubMed:26503042, ECO:0000269\|PubMed:30623799}.; (Microbial infection) Interacts with SARS coronavirus-2/SARS-CoV-2 spike protein S1 (via the CendR motif RRAR). {ECO:0000269\|PubMed:33082294}.
Domain The tandem CUB domains mediate binding to semaphorin, while the tandem F5/8 domains are resp
Target Relevance information above includes information from UniProt accession: O14786
The UniProt Consortium

Data

The purity of Cynomolgus Neuropilin-1 is greater than 95% as determined by SEC-HPLC.

SDS-PAGE gel of Cynomolgus Neuropilin-1 Protein

Cynomolgus Neuropilin-1 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.