Anti-Integrin β1 Antibody, clone MB1.2 Antibody, Alexa Fluor^™ 647 Conjugate

Evaluated by Immunocytochemistry in NIH/3T3 cells.

Immunocytochemistry Analysis: A 1:100 dilution of this antibody detected Integrin-beta1 in NIH/3T3 cells.

Anti-Integrin 1, clone MB1.2, Alexa Fluor^™ 647 Conjugate, Cat. No. MAB1997-AF647, is a highly specific rat monoclonal antibody that targets Integrin 1 and has been tested in Flow Cytometry and Immunocytochemistry.

Flow Cytometry Analysis: 0.2 µL from a representative lot detected Integrin 1 on the surface of one million NIH/3T3 cells.

The unconjugated antibody (Cat. No. MAB1997) and FITC conjugate (Cat. No. FCMAB269F) are also available for Flow Cytometry, Immunohistochemistry, Immunoprecipitation, and Western Blotting applications.

Research Category
Epigenetics & Nuclear Function

The specificity of MB1.2 was determined by its binding to antigen, and the ability of antiserum against the carboxyl terminal of VLA-beta 1 subunit to deplete antigens for MB1.2 in sequential immunoprecipitation experiments. MB1.2 had no effect on cell adhesion to matrix proteins (Von Ballestrem, C.G., et al. (1996). Hybridoma. 15(2):125-132).

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Integrin beta-1 (UniProt P09055; also known as CD29, Fibronectin receptor subunit beta, GpIIa, VLA-1/2/3/4/5/6 subunit beta) is encoded by the Itgb1 (also known as Fnrb) gene (Gene ID 16412) in murine species. The integrin family of cell adhesion receptors consists of at least 16 membrane-associated heterodimers, composed of an alpha and beta subunit that associate in a non-covalent manner. The structure and functional diversity of the integrin family are based upon the pairing abilities of the individual alpha and beta subunits. Key to these molecular interactions between the integrin receptors and their respective ligands is the recognition of the Arg-Gly-Asp (RGD) sequence known to be present in the extracellular matrix components fibronectin, vitronectin, collagen, fibrinogen, and von Willebrand factor. Integrin beta-1 is a 130 kDa transmembrane glycoprotein that interact with various integrin alpha subunits (including alpha 1, alpha 2, alpha 3, alpha 4, alpha 5, and alpha 6) to form the functional receptor complexes that bind to specific extracellular matrix proteins. Integrin receptors regulate a variety of important biological functions, including embryonic development, wound repair, hemostasis, and prevention of programmed cell death. They are also implicated in abnormal pathological states such as tumor directed angiogenesis, tumor growth and metastasis. These heterodimeric receptors bridge the cytoplasmic actin cytoskeleton with proteins present in the extracellular matrix and/or on adjacent cells. Interactions between integrins and the extracellular matrix lead to the activation of signal transduction pathways and regulation of gene expression.

~88 kDa (non-glycosylated) and ~130 kDa ( glycosylated).

Mouse Integrin beta-1 (Von Ballestrem, C.G., et al. (1996). Hybridoma. 15(2):125-132).

Concentration: Please refer to lot specific datasheet.

Protein G purified.

Purified rat IgG2a Alexa Fluor^™ 647 conjugate in buffer containing PBS, 1.5% BSA with 0.05% sodium azide.

Stable for 1 year at 2-8°C from date of receipt.

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