antibody

Anti-CD29 [8E3]

152488

monoclonal

mouse

nonconjugated

3688

western blot, ELISA, immunohistochemistry, immunoprecipitation

152488

ELISA IHC IP WB

Integrin beta-1 (CD29), VLA-4 subunit beta

Integrin Subunit Beta 1; Glycoprotein Iia; MSK12; GPIIA; FNRB; MDF2; Very Late Activation Protein; Beta Polypeptide; Fibronectin Receptor Subunit Beta; Integrin VLA-4 Beta Subunit; CD29 Antigen; VLA-BETA; CD29; VLAB

Human

Integrin beta1 (CD29) is a transmembrane glycoprotein that forms noncovalent complexes with various alpha integrin subunits to form the functional receptors that bind to specific extracellular matrix proteins. Integrin receptors are involved in cell adhesion and recognition in a variety of processes including embryogenesis, hemostasis, tissue repair, immune response and metatastatic diffusion of tumor cells. Interactions between integrins and extracellular matrix lead to activation of signal transduction pathways and regulation of gene expression. Phosphorylation of threonines 788 and 789 on integrin beta1 receptor may play a key role in cell-cycle dependent regulation.

Mouse

Purified Integrin Beta1 from HT-1080 cells.

IgG1 kappa

HT-1080 cell lysate

Adhesion, Cancer, Cell Signaling & Signal Transduction, Epigenetics & Nuclear Signalling, Gene Expression, Immunology

Western Blot Analysis: A 1:100,000 dilution from a representative lot detected Integrin protein in WB under non-reducing conditions. Activity Assay Analysis: A representative lot from an independent laboratory stimulated cellular adhesion and increased ligand binding activity of Integrin Beta1 (Mould, A. P., et al. (2004). J Biol Chem. 280(56):4238-4226.). Immunoprecipitation Analysis: A representative lot from an independent laboratory immunoprecipitated Integrin Beta1 in IP (Tiwari, S., et al. (2011). J Cell Sci. 124(10):1672-1680.). Epitope: N-terminus of the PSI domain. This antibody recognizes the N-terminus of the PSI domain of Integrin Beta1. Under native conditions, clone 8E3 is shown to recognize the unbent, monomeric ER form of Integrin Beta1 at the PSI domain; however, the epitope only becomes exposed in the Golgi form after denaturation. This observation suggests that the epitopes are present in monomeric beta 1-integrins, but become lost following assembly with alpha-integrin subunits (Tiwari, S., et al. (2011). J Cell Sci. 124(10):1672-1680.; Mould, A. P., et al. (2004). J Biol Chem. 280(56):4238-4226.)