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CD51 antibody (Integrin alpha V) (C-Term)

Details for Product anti-ITGAV Antibody No. ABIN966421, Supplier: Log in to see
Antigen
  • 1110004F14Rik
  • 2610028E01Rik
  • CD51
  • D430040G12Rik
  • MSK8
  • VNRA
  • VTNR
  • Cd51
Epitope
C-Term
17
13
5
5
4
3
3
2
2
2
1
1
1
1
1
1
1
1
1
Reactivity
Human, Mouse (Murine), Chicken
203
92
42
3
2
2
Host
Rabbit
120
83
45
1
1
Clonality
Polyclonal
Conjugate
This CD51 antibody is un-conjugated
27
18
14
3
3
3
2
2
2
2
2
2
2
1
Application
Immunohistochemistry (IHC)
139
77
64
43
33
31
27
24
24
14
10
6
4
4
3
2
2
1
Supplier
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Immunogen Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to C-terminal residues of human ITGAV (Integrin alpha-V precursor)
Purification Purified by antigen-specific affinity chromatography.
Alternative Name ITGAV (ITGAV Antibody Abstract)
Background The alpha-V integrins are receptors for vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin and von Willebrand factor. They recognize the sequence R-G-D in a wide array of ligands. Integrin alpha-V contains the heterodimer of an alpha and a beta subunit. The alpha subunit is composed of an heavy and a light chain linked by a disulfide bond. Alpha-V associates with either beta-1, beta-3, beta-5, beta-6 or beta-8 subunit.
Application Notes ELISA, Western blotting: 1µg/ml for 2hrs.
Restrictions For Research Use only
Format Liquid
Buffer This antibody is stored in PBS, 50% glycerol
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 -20 °C
Product cited in: Suzuki, Argraves, Pytela et al.: "cDNA and amino acid sequences of the cell adhesion protein receptor recognizing vitronectin reveal a transmembrane domain and homologies with other adhesion protein receptors." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 83, Issue 22, pp. 8614-8, 1986 (PubMed).

Background publications Krokhin, Cheng, Sousa et al.: "Mass spectrometric based mapping of the disulfide bonding patterns of integrin alpha chains." in: Biochemistry, Vol. 42, Issue 44, pp. 12950-9, 2003 (PubMed).

Zhang, Li, Martin et al.: "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry." in: Nature biotechnology, Vol. 21, Issue 6, pp. 660-6, 2003 (PubMed).

Xiong, Stehle, Diefenbach et al.: "Crystal structure of the extracellular segment of integrin alpha Vbeta3." in: Science (New York, N.Y.), Vol. 294, Issue 5541, pp. 339-45, 2001 (PubMed).

Cheresh, Smith, Cooper et al.: "A novel vitronectin receptor integrin (alpha v beta x) is responsible for distinct adhesive properties of carcinoma cells." in: Cell, Vol. 57, Issue 1, pp. 59-69, 1989 (PubMed).