Quick Order

Home>NRP1
Text Size:AAA

Neuropilin-1/NRP1/CD304  Protein, Antibody, ELISA Kit, cDNA Clone

Description: Active  
Expression host: Human Cells  
10011-H02H-50
10011-H02H-20
50 µg 
20 µg 
Add to Cart
  • Slide 1
Description: Active  
Expression host: Human Cells  
10011-H08H-50
10011-H08H-20
50 µg 
20 µg 
Add to Cart
  • Slide 1
Expression host: Human Cells  
90297-C08H-5
90297-C08H-20
5 µg 
20 µg 
Add to Cart
  • Slide 1
Expression host: Human Cells  
90297-C02H-50
90297-C02H-20
50 µg 
20 µg 
Add to Cart
  • Slide 1
Expression host: Human Cells  
90297-CCCH-50
90297-CCCH-20
50 µg 
20 µg 
Add to Cart
  • Slide 1

Neuropilin-1/NRP1/CD304 Related Area

Neuropilin-1/NRP1/CD304 Related Pathways

Neuropilin-1/NRP1/CD304 Related Protein, Antibody, cDNA Gene, and ELISA Kits

Featured Reagent Products

Neuropilin-1/NRP1/CD304 Summary & Protein Information

Neuropilin-1/NRP1/CD304 Background

Gene Summary: This gene encodes one of two neuropilins, which contain specific protein domains which allow them to participate in several different types of signaling pathways that control cell migration. Neuropilins contain a large N-terminal extracellular domain, made up of complement-binding, coagulation factor V/VIII, and meprin domains. These proteins also contains a short membrane-spanning domain and a small cytoplasmic domain. Neuropilins bind many ligands and various types of co-receptors; they affect cell survival, migration, and attraction. Some of the ligands and co-receptors bound by neuropilins are vascular endothelial growth factor (VEGF) and semaphorin family members. Several alternatively spliced transcript variants that encode different protein isoforms have been described for this gene
General information above from NCBI
Subunit structure: Homodimer, and heterodimer with NRP2. Interacts with FER (By similarity). Binds PLXNB1. {ECO:0000250, ECO:0000269|PubMed:10520995, ECO:0000269|PubMed:17989695}.
Domain: The tandem CUB domains mediate binding to semaphorin, while the tandem F5/8 domains are responsible for heparin and VEGF binding.
Subcellular location: Cell membrane; Single-pass type I membrane protein.; Isoform 2: Secreted.
Tissue specificity: The expression of isoforms 1 and 2 does not seem to overlap. Isoform 1 is 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. Isoform 2 is found in liver hepatocytes, kidney distal and proximal tubules.
Sequence similarity: Belongs to the neuropilin family. {ECO:0000305}.; Contains 2 CUB domains. {ECO:0000255|PROSITE-ProRule:PRU00059}.; Contains 2 F5/8 type C domains. {ECO:0000255|PROSITE-ProRule:PRU00081}.; Contains 1 MAM domain. {ECO:0000255|PROSITE-ProRule:PRU00128}.
General information above from UniProt

Neuropilin is a type I transmembrane protein and the molecular mass is 120 kDa. Two homologues, Neuropilin-1 and Neuropilin-2, are identified. The primary structure of Neuropilin-1 and Neuropilin-2 is well conserved and is divided into four domains, CUB (a1/a2) domain, FV/FVIII (b1/b2) domain, MAM (c) domain, and (d) domain that contains a transmembrane and a short cytoplasmic region. Neuropilin-1 (NRP1) acts as a receptor for two different extracellular ligands, class 3 semaphorins and specific isoforms of vascular endothelial growth factor. The functions of NRP1 and NRP2 have been extensively studied in neurons where they act in axon guidance and in endothelial cells where they promote angiogenesis and cell migration. Neuropilin-1 is likely to mediate contacts between the dendritic cells and the T lymphocytes via homotypic interactions and is essential for the initiation of the primary immune response. NRP1 is a co-receptor for VEGF receptor-2 (VEGFR2) that enhances the binding of VEGF165 to VEGFR2 and VEGF165-mediated chemotaxis. NRP1 expression is regulated in EC by tumor necrosis factor-alpha, the transcription factors dHAND and Ets-1, and vascular injury. NRP1 upregulation is positively correlated with the progression of various tumors. Overexpression of NRPI in rat tumor cells results in enlarged tumors and substantially enhanced tumor angiogenesis. On the other hand, soluble NRP1 (sNRP1) is an antagonist of tumor angiogenesis.

Neuropilin-1/NRP1/CD304 Alternative Name

Neuropilin-1/NRP1/CD304 Related Studies

  • Nakamura F, et al. (2002) Structural and functional relation of neuropilins. Adv Exp Med Biol. 515: 55-69.
  • Romeo PH, et al. (2002) Neuropilin-1 in the immune system. Adv Exp Med Biol. 515: 49-54.
  • Klagsbrun M, et al. (2002) The role of neuropilin in vascular and tumor biology. Adv Exp Med Biol. 515: 33-48.
  • Staton CA, et al. (2007) Neuropilins in physiological and pathological angiogenesis. J Pathol. 212(3): 237-48.
  • Bagri A, et al. (2009) Neuropilins in tumor biology. Clin Cancer Res. 15(6): 1860-4.
  • Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"