Neuropilin-1 Protein, Cynomolgus (592a.a, HEK293, His)

Neuropilin-1 Protein, a transmembrane glycoprotein, regulates axon guidance, angiogenesis, neuronal development, and immune responses. Neuropilin-1 can interacts with VEGF and semaphorins, and promote the growth, survival, and self-renewal of tumors. Neuropilin-1 also acts as an entry factor and potentiate SARS-CoV-2 and Epstein-Barr virus (EBV) infectivity. Furthermore, Neuropilin-1 acts as a co-receptor for TGF-β, and enhances TGF-β activity via the SMAD2/3 signaling pathway^[1][2][3]. Neuropilin-1 Protein, Cynomolgus (592a.a, HEK293, His) is the recombinant cynomolgus-derived Neuropilin-1 protein, expressed by HEK293 , with C-6*His labeled tag. The total length of Neuropilin-1 Protein, Cynomolgus (592a.a, HEK293, His) is 592 a.a., with molecular weight of 80-100 kDa.

Neuropilin-1 (NRP1) protein is a transmembrane glycoprotein. In mice, NRP1 is selectively expressed on thymic-derived Tregs, and enhances immunosuppressive function. In humans, NRP1 is mainly expressed on plasmacytoid dendritic cells (pDCs) where it aids in priming immune responses, as well as on a subset of T regulatory cells (Tregs) isolated from secondary lymph nodes^[1].
Neuropilin-1 transduce signals for VEGFs, together with VEGFR family members. Neuropilin-1 interacts with VEGF and semaphorins, and can promote the growth, survival, and self-renewal of tumors. For example, Neuropilin-1 can complex with VEGFR2 in vascular endothelial cells to induce vessel permeability and angiogenesis^[3].
Neuropilin-1 also acts as an entry factor and potentiate SARS-CoV-2 infectivity. Besides, Neuropilin-1 is an entry receptor for Epstein-Barr virus (EBV) infection of nasopharyngeal epithelial cells, and enhances EBV infection^[2][3]. NRP-1 plays a central role in axonal guidance and pruning by interaction with Semaphorin-3A (a protein seen widely in both the nervous system and the vasculature)^[3].
Furthermore, Neuropilin-1 acts as a co-receptor for TGF-β, and enhances TGF-β activity via the SMAD2/3 signaling pathway. Neuropilin-1 can activate the inactive latent form (LAP-TGF-β), and also promote immune suppression^[1].
Neuropilin-1 plays an important role in angiogenesis, neuronal development, and the regulation of immune responses.

Cynomolgus

HEK293

C-6*His

G7PEQ1 (F22-G613)

102145235  [NCBI]

FRNDKCGDTIKIESPGYLTSPGYPHSYHPSEKCEWLIQAPDPYQRIMINFNPHFDLEDRDCKYDYVEVFDGENENGRLWGKFCGKIAPPPVVSSGQFLFIKFVSDYETHGAGFSIRYEIFKRGPECSQNYTTPSGVIKSPGFPEKYPNSLECTYIVFAPKMSEIILEFESFDLEPDSNPPGGMFCRYDRLEIWDGFPDVGPHIGRYCGQKTPGRIRSSSGILSMVFYTDSAIAKEGFSANYSVLQSSVSEDFKCMEAVGMESGEIHSDQITASSQYSTNWSAERSRLNYPENGWTPGEDSYREWIQVDLGLLRFVTAVGTQGAISKETKKKYYVKTYKIDISSNGEDWITIKEGNKPVLFQGNTNPTDVVVAVFPKPLITRFVRIKPATWETGISLRFEVYGCKITDYPCSGMLGMVSGLISDSQITSSNQGDRNWMPENIRLVTSRSGWALPPAPHSYVNEWLQIDLGEEKIVRGIIIQGGKHRENKVFMRKFKIGYSNNGSDWKMIMDDSKRKAKSFEGNNNYDTPELRTFPALSTRFIRIYPERATHGGLGLRMELLGCEVEAPTAGPTTPNGNPVDECDDDQANCHSG

80-100 kDa

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.