Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
accession | Q15223 |
express system | HEK293 |
product tag | C-His-Avi |
purity | > 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC |
background | Nectins are a small family of Ca -independent immunoglobulin (Ig)-like cell adhesion molecules (CAMs) that organize intercellular junctions. They are highly homologous to the human receptor for poliovirus, and as such have been alternately named poliovirus receptor-related proteins.Nectin-1 promotes cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions have been detected between Nectin-1 and Nectin-3 and between Nectin-1 and Nectin-4. Has some neurite outgrowth-promoting activity. |
molecular weight | The protein has a predicted MW of 36.9 kDa. Due to glycosylation, the protein migrates to 52-70 kDa based on Tris-Bis PAGE result. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Human Nectin-1/PVRL1/CD111 Protein 4591
$240.00 – $800.00
Summary
- Expression: HEK293
- Functional: Yes (ELISA)
- Amino Acid Range: Gln31-Thr334
Human Nectin-1/PVRL1/CD111 Protein 4591
protein |
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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 |
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Nectins are a small family of Ca -independent immunoglobulin (Ig)-like cell adhesion molecules (CAMs) that organize intercellular junctions. They are highly homologous to the human receptor for poliovirus, and as such have been alternately named poliovirus receptor-related proteins.Nectin-1 promotes cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions have been detected between Nectin-1 and Nectin-3 and between Nectin-1 and Nectin-4. Has some neurite outgrowth-promoting activity. |
Protein names Nectin-1 (Herpes virus entry mediator C) (Herpesvirus entry mediator C) (HveC) (Herpesvirus Ig-like receptor) (HIgR) (Nectin cell adhesion molecule 1) (Poliovirus receptor-related protein 1) (CD antigen CD111) |
Gene names NECTIN1,NECTIN1 HVEC PRR1 PVRL1 |
Protein family Nectin family |
Mass 9606Da |
Function Promotes cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions have been detected between NECTIN1 and NECTIN3 and between NECTIN1 and NECTIN4. Has some neurite outgrowth-promoting activity.; (Microbial infection) Acts as a receptor for herpes simplex virus 1/HHV-1, herpes simplex virus 2/HHV-2, and pseudorabies virus/PRV. |
Subellular location [Isoform Alpha]: Cell membrane; Single-pass type I membrane protein. Presynaptic cell membrane .; [Isoform Delta]: Cell membrane; Single-pass type I membrane protein.; [Isoform Gamma]: Secreted. |
Structure Interacts (via Ig-like C2-type domain 2) with FGFR1, FGFR2 and FGFR3 (By similarity). Cis- and trans-homodimer. Can form trans-heterodimers with NECTIN3 and with NECTIN4. Interaction between NECTIN1 and NECTIN3 on the pre- and postsynaptic sites, respectively, initiates the formation of puncta adherentia junctions between axons and dendrites. Interacts (via cytoplasmic domain) with AFDN (via PDZ domain); this interaction recruits NECTIN1 to cadherin-based adherens junctions and provides a connection with the actin cytoskeleton. Interacts with integrin alphaV/beta3.; (Microbial infection) Interacts with herpes simplex virus 1/HHV-1, herpes simplex virus 2/HHV-2, and pseudorabies virus/PRV envelope glycoprotein D (PubMed:21980294, PubMed:22146396, PubMed:9657005, PubMed:9696799). |
Domain Ig |
Target Relevance information above includes information from UniProt accession: Q15223 |
The UniProt Consortium |
Data
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.pmid | title | authors | citation |
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Protocols
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Documents
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