Human Neuropilin 1 (NRP1) Protein

Este producto es parte de NRP1 - neuropilin 1
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260€ (50 µg)

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935106861
info@markelab.com
name
Human Neuropilin 1 (NRP1) Protein
category
Proteins and Peptides
provider
Abbexa
reference
abx620031
tested applications
SDS-PAGE

Description

Human Neuropilin 1 (NRP1) Protein is a recombinant Human protein expressed in E. coli.

Documents del producto

Instrucciones
Data sheet
Descargar

Product specifications

Category
Proteins and Peptides
Immunogen Target
Neuropilin 1 (NRP1)
Host
E. coli
Origin
Human
Observed MW
Molecular Weight: Calculated MW: 72.14 kDa
Sequence Fragment: Phe22-Lys644
Tag: His tag
Expression
Recombinant
Purity
> 90% (SDS-PAGE)
Size 1
50 µg
Size 2
100 µg
Size 3
1 mg
Form
 
Tested Applications
SDS-PAGE
Buffer
Prior to lyophilization: PBS, pH 7.5.
Availability
Shipped within 5-10 working days.
Dry Ice
No
UniProt ID
O14786
Gene ID
8829
OMIM
602069
Alias
Vascular endothelial cell growth factor 165 receptor,NP1,NRP,BDCA4,CD304,VEGF165R,
Background
Protein NRP1
Status
RUO
Note
This product is for research use only.   Not for human consumption, cosmetic, therapeutic or diagnostic use.

Descripción

Neuropilin-1 (NRP1) is a multifunctional transmembrane glycoprotein that plays critical roles in multiple physiological processes, including vascular development, neural guidance, immune modulation, and cancer progression. First characterized as a receptor involved in the guidance of axons, NRP1 is now known to act as a co-receptor for various ligands, including vascular endothelial growth factor (VEGF) and semaphorin family proteins, which control angiogenesis and axonal guidance, respectively. NRP1 is widely expressed in endothelial cells, neurons, immune cells, and several tumor cell types. Its role in mediating signal transduction for multiple growth factors makes it highly significant in both normal developmental biology and pathologies, including cancer and cardiovascular diseases. NRP1’s structure allows it to interact with a variety of ligands, facilitating its participation in different signaling pathways. Importantly, NRP1 lacks intrinsic kinase activity and instead functions by associating with other receptor complexes. This co-receptor capability is vital for its role in angiogenesis, where it enhances VEGF signaling by complexing with VEGF receptors (particularly VEGFR2), and in immune regulation, where it modulates T cell activity and antigen presentation. NRP1 has therefore become a target of interest for therapeutic intervention in diseases involving abnormal cell growth, such as cancer and chronic inflammatory conditions.

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