Anti-CD29 [8E3]

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. […]

Contributors

Inventor Institute
Martin Humphries University of Manchester
Cat. #: 152488
Tool sub type: Primary antibody
Unit size: 100 ug
Research Fields: Cancer;Cell biology;Cell signaling and signal transduction;Genetics;Immunology
Application: ELISA ; IHC ; IP ; WB
Target: Integrin beta-1 (CD29), VLA-4 subunit beta
Reactivity: Human
Clone: Array
Host: Mouse
Class: Monoclonal
Alternate name: 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
Product description: 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.
Conjugation: Unconjugated
Isotype: IgG1 kappa
Immunogen: Purified Integrin Beta1 from HT-1080 cells.
Target background: Integrin beta1 (CD29) is a transmembrane glycoprotein that forms noncovalent complexes with various alpha integrin subunits to form the Fn 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.
Format: Liquid
Concentration: 1 mg/ml
Storage buffer: PBS with 0.02% azide
Storage conditions: -15° C to -25° C
Shipping conditions: Dry ice
References:

Tiwari et al. 2011. J Cell Sci. 124(Pt 10):1672-80. PMID: 21511727.

Divalent cations regulate the folding and activation status of integrins during their intracellular trafficking.

Bridger et al. 2008. Biol Reprod. 79(2):274-82. PMID: 18417711.

Integrin activation in bovine placentomes and in caruncular epithelial cells isolated from pregnant cows.

Mould et al. 2005. J Biol Chem. 280(6):4238-46. PMID: 15557320.

Evidence that monoclonal antibodies directed against the integrin beta subunit plexin/semaphorin/integrin domain stimulate function by inducing receptor extension.

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