Product Pathways - Adhesion
Integrin α4 Antibody #4600
|4600S||100 µl (10 western blots)||---||In Stock||---|
|4600P||40 µl (4 western blots)||---||In Stock||---|
|4600||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human||Endogenous||70, 140, 150, (180)||Rabbit|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation
Specificity / Sensitivity
Integrin α4 Antibody detects endogenous levels of integrin α4 mature protein (150kDa), α4 precursor protein (140kDa), as well as 70 kDa cleaved C-terminal α4 fragment.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser1027 of human integrin α4. Antibodies are purified by peptide affinity chromatography.
Integrins are α/β heterodimeric cell surface receptors that play a pivotal role in cell adhesion and migration, as well as in growth and survival (1,2). The integrin family contains at least 18 α and 8 β subunits that form 24 known integrins with distinct tissue distribution and overlapping ligand specificities (3). Integrins not only transmit signals to cells in response to the extracellular environment (outside-in signaling), but also sense intracellular cues to alter their interaction with the extracellular environment (inside-out signaling) (1,2).
A pair of important α4 integrins, α4β1 and α4β7, interact with VCAM-1, fibronectin, and MAdCAM-1 at cell adhesions (3). Gene knockout and antibody blocking research reveal that α4 integrins play important roles in embryonic liver and heart development and in fetal lymphocyte homing (4-6). Phosphorylation at Ser988 within the cytoplasmic tail of integrin α4 blocks binding to paxillin and promotes leading edge migration (7,8).
On SDS-PAGE, integrin α4 can migrate at several different apparent molecular sizes, a 150 kDa mature protein and a 140 kDa precursor protein (a 180 kDa protein also exists under mild non-reducing conditions) (9). Integrin α4 has a cleavage site at Arg558, which results in a small portion of the protein as either an 80 kDa N-terminal or 70 kDa C-terminal fragment (10).
- Hood, J.D. and Cheresh, D.A. (2002) Nat Rev Cancer 2, 91-100.
- Liu, S. et al. (2000) J Cell Sci 113 ( Pt 20), 3563-71.
- Plow, E.F. et al. (2000) J Biol Chem 275, 21785-8.
- Bonder, C.S. et al. (2005) Immunity 23, 153-63.
- Arroyo, A.G. et al. (1999) Immunity 11, 555-66.
- Yang, J.T. et al. (1995) Development 121, 549-60.
- Nishiya, N. et al. (2005) Nat Cell Biol 7, 343-52.
- Alon, R. et al. (2005) J Cell Biol 171, 1073-84.
- Teixidó, J. et al. (1992) J Biol Chem 267, 1786-91.
- Pujades, C. et al. (1996) Biochem J 313 ( Pt 3), 899-908.
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For Research Use Only. Not For Use In Diagnostic Procedures.
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