Integrin beta 5 Monoclonal Antibody (KN52), eBioscience™, Invitrogen™

Description

• Description: The KN52 antibody reacts with human integrin beta 5, an approximately 100,000 Mr (reduced) and 95,000 Mr (nonreduced) a member of the integrin family
• Only a single alpha chain, the alpha v subunit, associates with the integrin beta 5 to form the vitronectin receptor complex
• Integrin alpha v/beta 5 complex also binds to the basic domain of Tat (he sequence RKKRRQRRR)
• The integrin beta 5 is found on carcinoma cell lines, hepatoma and fibroblast cell lines, and is absent from lymphoblastoid cells and platelets
• The KN52 monoclonal antibody has been shown to inhibit migration
• Applications Reported: This KN52 antibody has been reported for use in flow cytometric analysis
• Applications Tested: This KN52 antibody has been tested by flow cytometric analysis of Chinese Hamster Ovary (CHO), A549 and normal human peripheral blood cells
• This can be used at less than or equal to 0.25 μg per test
• A test is defined as the amount (μg) of antibody that will stain a cell sample in a final volume of 100 μL
• Cell number should be determined empirically but can range from 10^5 to 10^8 cells/test
• It is recommended that the antibody be carefully titrated for optimal performance in the assay of interest
• Purity: Greater than 90%, as determined by SDS-PAGE
• Aggregation: Less than 10%, as determined by HPLC
• Filtration: 0.2 μm post-manufacturing filtered
• Integrins are important extracellular matrix (ECM) receptor proteins located on cell surfaces
• They are hetrodimers composed of an alpha and a beta transmembrane glycoprotein subunit
• Around 22 different integrins (different alpha/ beta subunit combinations) are found in nature
• Integrins are generally present in high concentrations at the cell surface, but, unlike most other cell-surface receptors, they bind ligands with very low affinity
• Due to their weak individual binding, integrins need to cluster and bind in-groups in order to effectively bind the ECM
• Integrins bind many different ligands including laminin
• Each integrin is made up of a large N-terminal extracellular domain that binds the ECM ligand and a small C-terminal cytoplasmic domain that mediates interaction with the actin cytoskeleton and signaling function.