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VLA alpha 4 (C-Term) antibody

Details for Product No. ABIN650602
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Antigen
Epitope
C-Term
Reactivity
Human
Host
Rabbit
Clonality
Monoclonal
Application
Western Blotting (WB), Immunohistochemistry (IHC)
Pubmed 3 references available
Quantity 100 µL
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Catalog No. ABIN650602
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Immunogen A synthetic peptide corresponding to residues near the C-terminus of human VLA-alpha 4 was used as an immunogen.
Specificity A synthetic peptide corresponding to residues near the C-terminus of human VLA-alpha 4 was used as an immunogen.
Background VLA-4 is a cell surface heterodimer in the integrin superfamily of adhesion receptors. Anti-VLA-4 antibodies inhibited cytolytic T cell activity, with inhibitory activity directed against the effector T cells rather than their targets. Thus, whereas other VLA receptors appear to mediate cell--matrix interactions, VLA-4 may have a cell--cell adhesion function. Alpha 4 stands apart from all other known integrin alpha subunit sequences because (i) alpha 4 has neither an inserted I-domain, nor a disulfide-linked C-terminal fragment, (ii) its sequence is the most unique and (iii) only alpha 4 has a potential protease cleavage site, near the middle of the coding region, which appears responsible for the characteristic 80,000 and 70,000 Mr fragments of alpha 4 (1). Unlike any other integrin alpha subunit, the intact (150 kDa) alpha 4 subunit of VLA-4 can sometimes be cleaved into two noncovalently associated fragments (80 and 70 kDa) (2). The VLA-4 integrins are indispensable for embryogenesis, hematopoiesis and immune responses, possibly because alpha4 regulates cellular functions differently from other integrins through its cytoplasmic tail (3).
Synonyms: ITGA4, CD49D, Integrin alpha-4, Integrin alpha-IV,VLA-4,CD49 antigen-like family member D
Molecular Weight 150 kDA
Gene ID 3676
UniProt P13612
Research Area Phospho-specific antibodies, Protein Modifications, Cell Structure
Application Notes IHC: = 1:100-250, WB: = 1:1000-2000
Comment

Background: VLA-4 is a cell surface heterodimer in the integrin superfamily of adhesion receptors. Anti-VLA-4 antibodies inhibited cytolytic T cell activity, with inhibitory activity directed against the effector T cells rather than their targets. Thus, whereas other VLA receptors appear to mediate cell--matrix interactions, VLA-4 may have a cell--cell adhesion function. Alpha 4 stands apart from all other known integrin alpha subunit sequences because (i) alpha 4 has neither an inserted I-domain, nor a disulfide-linked C-terminal fragment, (ii) its sequence is the most unique and (iii) only alpha 4 has a potential protease cleavage site, near the middle of the coding region, which appears responsible for the characteristic 80,000 and 70,000 Mr fragments of alpha 4 (1). Unlike any other integrin alpha subunit, the intact (150 kDa) alpha 4 subunit of VLA-4 can sometimes be cleaved into two noncovalently associated fragments (80 and 70 kDa) (2). The VLA-4 integrins are indispensable for embryogenesis, hematopoiesis and immune responses, possibly because alpha4 regulates cellular functions differently from other integrins through its cytoplasmic tail (3).

Restrictions For Research Use only
Format Liquid
Buffer 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
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 VLA alpha 4 Antibody can be stored at -20°C for up to 12 months from time of receipt.
Expiry Date 12 months
Background publications Teixidó, Parker, Kassner et al.: "Functional and structural analysis of VLA-4 integrin alpha 4 subunit cleavage." in: The Journal of biological chemistry, Vol. 267, Issue 3, pp. 1786-91, 1992 (PubMed).

Takada, Elices, Crouse et al.: "The primary structure of the alpha 4 subunit of VLA-4: homology to other integrins and a possible cell-cell adhesion function." in: The EMBO journal, Vol. 8, Issue 5, pp. 1361-8, 1989 (PubMed).

Liu, Thomas, Woodside et al.: "Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses." in: Nature, Vol. 402, Issue 6762, pp. 676-81, 2000 (PubMed).

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