Mouse Neuropilin 1 (NRP1) Protein

Product specifications

Proteins and Peptides

Neuropilin 1 (NRP1)

E. coli

Mouse

Unconjugated

Molecular Weight: Calculated MW: 14.6 kDa  Observed MW: 14 kDa
Concentration: Prior to lyophilization: 200 µg/ml
Sequence Fragment: Cys27-Phe141
Tag: N-terminal His tag

Recombinant

> 95%

10 µg

50 µg

100 µg

200 µg

500 µg

Lyophilized To keep the original salt concentration, we recommend reconstituting to the original concentration prior to lyophilization (see Concentration) in ddH2O. If a lower concentration is required, dilute in PBS, pH 7.4. If a higher concentration is required, the product can be reconstituted directly in PBS, pH 7.4, though please note that this will change the overall salt concentration. The stock concentration should be between 0.1-1.0 mg/ml. Do not vortex.

WB, SDS-PAGE

Prior to lyophilization: PBS, pH 7.4, containing 0.01% Sarcosyl, 1 mM DTT, 5% Trehalose and Proclin-300.

Shipped within 5-7 working days.

Store at 2-8 °C for up to one month. Store at -80 °C for up to one year. Avoid repeated freeze/thaw cycles.

No

P97333

Vascular endothelial cell growth factor 165 receptor,NP1,NRP,BDCA4,CD304,VEGF165R,

Protein NRP1

RUO

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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