Integrin, alpha 5 (Fibronectin Receptor, alpha Polypeptide) (ITGA5) antibody

Details for Product No. ABIN969221
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Antigen
Synonyms ITGA5, Cd49e, Fnra, VLA5, CD49e, FNRA, VLA5A, Itga5_retired
Reactivity
Human
(110), (108), (35), (13), (12), (3), (1)
Host
Mouse
(62), (51), (46), (37), (1)
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
(32), (19), (13), (3), (3), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1)
Application
ELISA, Western Blotting (WB), Immunohistochemistry (IHC), Fluorescence Microscopy (FM)
(131), (70), (46), (41), (34), (27), (15), (13), (10), (10), (6), (1), (1)
Pubmed 5 references available
Quantity 100 μL
Options
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Catalog No. ABIN969221
363.00 $
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Immunogen Purified recombinant fragment of human ITGA5 expressed in E. coli.
Clone 10F6
Isotype IgG2a
Purification Ascites
Alternative Name ITGA5
Background Synonyms:
FNRA, CD49e, VLA5A, ITGA5
The product of this gene belongs to the integrin α chain family. Integrins are heterodimeric integral membrane proteins composed of an α chain and a β chain. This gene encodes the integrin α 5 chain. α chain 5 undergoes post-translational cleavage in the extracellular domain to yield disulfide-linked light and heavy chains that join with β 1 to form a fibronectin receptor. In addition to adhesion, integrins are known to participate in cell-surface mediated signalling. Integrin α 5 is a heterodimer that associates noncovalently with CD29/integrin β 1 subunit to form the α-5-β-1 very late antigen (VLA-5) complex. VLA-5 is a fibronectin receptor that is expressed on thymocytes, T-cells, monocytes and platelets. It is also found on very early B-cells and activated B-cells. VLA-5-mediated binding to fibronectin sends a costimulatory signal to T-cells and enhances Fc-γ-R- and complement receptor-mediated phago-cytosis. It is also involved in monocyte migration into extracellular tissues.
Molecular Weight 114 kDa
Gene ID 3678
Application Notes Recommended Dilution:
ELISA: 1/10000, WB: 1/500 - 1/2000, IHC: 1/200 - 1/1000, FCM: 1/200 - 1/400
Not yet tested in other applications.
Determining optimal working dilutions by titration test.
Restrictions For Research Use only
Format Liquid
Buffer Ascitic fluid containing 0.03 % sodium azide.
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage 4 °C/-20 °C
Storage Comment Store at 4 °C or at -20 °C for long term.
Supplier Images
anti-Integrin, alpha 5 (Fibronectin Receptor, alpha Polypeptide) (ITGA5) antibody Figure 3: Flow cytometric analysis of Hela cells using ITGA5 mouse mAb (green) and negative control (purple) .
anti-Integrin, alpha 5 (Fibronectin Receptor, alpha Polypeptide) (ITGA5) antibody (2) Figure 2: Immunohistochemical analysis of paraffin-embedded human Placenta tissues using ITGA5 mouse mAb
anti-Integrin, alpha 5 (Fibronectin Receptor, alpha Polypeptide) (ITGA5) antibody (3) Figure 1: Western blot analysis using ITGA5 mouse mAb against ITGA5-hIgGFc transfected HEK293 cell lysate.
Product cited in: Jones, Gockerman, Busby et al.: "Insulin-like growth factor binding protein 1 stimulates cell migration and binds to the alpha 5 beta 1 integrin by means of its Arg-Gly-Asp sequence." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 90, Issue 22, pp. 10553-7, 1993 (PubMed).

Byzova, Plow: "Activation of alphaVbeta3 on vascular cells controls recognition of prothrombin." in: The Journal of cell biology, Vol. 143, Issue 7, pp. 2081-92, 1999 (PubMed).

Wong, Wiedle, Ballestrem et al.: "PECAM-1/CD31 trans-homophilic binding at the intercellular junctions is independent of its cytoplasmic domain; evidence for heterophilic interaction with integrin alphavbeta3 in Cis." in: Molecular biology of the cell, Vol. 11, Issue 9, pp. 3109-21, 2000 (PubMed).

Zhao, Newman: "Integrin activation by regulated dimerization and oligomerization of platelet endothelial cell adhesion molecule (PECAM)-1 from within the cell." in: The Journal of cell biology, Vol. 152, Issue 1, pp. 65-73, 2001 (PubMed).

Mould, Askari, Barton et al.: "Integrin activation involves a conformational change in the alpha 1 helix of the beta subunit A-domain." in: The Journal of biological chemistry, Vol. 277, Issue 22, pp. 19800-5, 2002 (PubMed).

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