Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
express system | HEK293 |
product tag | C-His-Avi |
purity | > 95% as determined by Tris-Bis PAGE;> 90% as determined by HPLC |
background | Integrin alpha 5/ beta 1, also known as VLA-5, is a widely expressed non-covalent heterodimer of a 160 kDa alpha 5 and a 130 kDa beta 1 Integrin subunit.Alpha 5/ beta 1 is up‑regulated on tumor vasculature and promotes angiogenesis. |
molecular weight | The protein has a predicted MW of 111.8 kDa (ITGA5)&83.2 kDa (ITGB1). Due to glycosylation, the protein migrates to 110-140 kDa based on Tris-Bis PAGE result. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Biotinylated Human Integrin alpha 5 beta 1 (ITGA5&ITGB1) Heterodimer Protein 3064
$600.00 – $2,000.00
Summary
- Expression: HEK293
- Functional: Yes (ELISA)
- Amino Acid Range: Phe42-Tyr995(ITGA5)acidic tail & Gln21-Asp728(ITGB1)basic tail
Biotinylated Human Integrin alpha 5 beta 1 (ITGA5&ITGB1) Heterodimer Protein 3064
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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Integrin alpha 5/ beta 1, also known as VLA-5, is a widely expressed non-covalent heterodimer of a 160 kDa alpha 5 and a 130 kDa beta 1 Integrin subunit.Alpha 5/ beta 1 is up-regulated on tumor vasculature and promotes angiogenesis. |
Protein names Integrin alpha-5 (CD49 antigen-like family member E) (Fibronectin receptor subunit alpha) (Integrin alpha-F) (VLA-5) (CD antigen CD49e) [Cleaved into: Integrin alpha-5 heavy chain; Integrin alpha-5 light chain] |
Gene names ITGA5,ITGA5 FNRA |
Protein family Integrin alpha chain family |
Mass 9606Da |
Function Integrin alpha-5/beta-1 (ITGA5:ITGB1) is a receptor for fibronectin and fibrinogen. It recognizes the sequence R-G-D in its ligands. ITGA5:ITGB1 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1 (PubMed:18635536, PubMed:25398877). ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1 (PubMed:12807887, PubMed:17158881). ITGA5:ITGB1 acts as a receptor for fibronectin (FN1) and mediates R-G-D-dependent cell adhesion to FN1 (PubMed:33962943). ITGA5:ITGB1 is a receptor for IL1B and binding is essential for IL1B signaling (PubMed:29030430). ITGA5:ITGB3 is a receptor for soluble CD40LG and is required for CD40/CD40LG signaling (PubMed:31331973).; (Microbial infection) Integrin ITGA5:ITGB1 acts as a receptor for Human metapneumovirus.; (Microbial infection) Integrin ITGA2:ITGB1 acts as a receptor for Human parvovirus B19.; (Microbial infection) In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions. |
Catalytic activity BINDING 262; /ligand="a protein"; /ligand_id="ChEBI:CHEBI:16541"; /ligand_part="L-arginine residue"; /ligand_part_id="ChEBI:CHEBI:29965"; /ligand_part_note="Arg of R-G-D sequence recognized in fibronectin and fibrinogen"; /evidence="ECO:0000269|PubMed:22451694"; BINDING 269; /ligand="a protein"; /ligand_id="ChEBI:CHEBI:16541"; /ligand_part="L-arginine residue"; /ligand_part_id="ChEBI:CHEBI:29965"; /ligand_part_note="Arg of R-G-D sequence recognized in fibronectin and fibrinogen"; /evidence="ECO:0000269|PubMed:22451694"; BINDING 280; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000269|PubMed:33962943, ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3, ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"; BINDING 282; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000269|PubMed:33962943, ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3, ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"; BINDING 284; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000269|PubMed:33962943, ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3, ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"; BINDING 286; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000269|PubMed:33962943, ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3, ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"; BINDING 288; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000269|PubMed:33962943, ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3, ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"; BINDING 334; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:33962943, ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3, ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"; BINDING 336; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:33962943, ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3, ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"; BINDING 338; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:33962943, ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3, ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"; BINDING 340; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:33962943, ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3, ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"; BINDING 342; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:33962943, ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3, ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"; BINDING 401; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000269|PubMed:33962943, ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3, ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"; BINDING 403; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000269|PubMed:33962943, ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3, ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"; BINDING 405; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000269|PubMed:33962943, ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3, ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"; BINDING 407; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000269|PubMed:33962943, ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3, ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"; BINDING 409; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000269|PubMed:33962943, ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3, ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"; BINDING 465; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="4"; /evidence="ECO:0000269|PubMed:33962943, ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3, ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"; BINDING 467; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="4"; /evidence="ECO:0000269|PubMed:33962943, ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3, ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"; BINDING 469; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="4"; /evidence="ECO:0000269|PubMed:33962943, ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3, ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"; BINDING 471; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="4"; /evidence="ECO:0000269|PubMed:33962943, ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3, ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"; BINDING 473; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="4"; /evidence="ECO:0000269|PubMed:33962943, ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3, ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL" |
Subellular location Cell membrane ; Single-pass type I membrane protein. Cell junction, focal adhesion . |
Tissues Expressed in placenta (at protein level). |
Structure Heterodimer of an alpha and a beta subunit. The alpha subunit is composed of a heavy and a light chain linked by a disulfide bond. ITGA5/Alpha-5 associates with ITGB1/beta-1 (PubMed:33962943). Interacts with NISCH (PubMed:11912194). Interacts with HPS5 (PubMed:10094488). Interacts with RAB21 and COMP. Interacts with CIB1. ITGA5:ITGB1 interacts with CCN3. ITGA5:ITGB1 interacts with FBN1 (PubMed:12807887, PubMed:17158881). ITGA5:ITGB1 interacts with IL1B (PubMed:29030430). ITGA5:ITGB1 interacts with ACE2 (PubMed:33102950). ITGA5:ITGB1 interacts with SELP (PubMed:37184585). Interacts with ANGPT2 (PubMed:32908006).; (Microbial infection) Integrin ITGA5:ITGB1 interacts with human metapneumovirus fusion protein.; (Microbial infection) Integrin ITGA5:ITGB1 interacts with human parvovirus B19 capsid proteins.; (Microbial infection) Interacts with HIV-1 Tat.; (Microbial infection) ITGA5:ITGB1 interacts with SARS coronavirus-2/SARS-CoV-2 spike protein. |
Post-translational modification Proteolytic cleavage by PCSK5 mediates activation of the precursor. |
Target Relevance information above includes information from UniProt accession: P08648 |
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
relevant to this product |
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Documents
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