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Osteopontin Monoclonal Antibody (2F10), eBioscience™, Invitrogen™

Mouse Monoclonal Antibody

Supplier:  Invitrogen 14909682

Encompass_Preferred

Catalog No. 50-112-2755


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Description

Description

Description: The 2F10 monoclonal antibody recognizes human osteopontin (OPN), a secreted glycophosphoprotein expressed by multiple cell types, including leukocytes, fibroblasts, dendritic cells, macrophages, myoblasts, bone-forming cells, and epithelial cells. OPN is an extracellular matrix protein with multiple roles, including bone resorption and calcification, immune system regulation, wound healing, and tumorigenesis. Thrombin cleavage of OPN allows binding of integrin receptors, expressed by immune cells, and subsequent modulation of cell adhesion, migration, and survival. OPN is expressed in bones, teeth, placenta, blood vessels, kidney, and various tumors. Osteopontin has been identified as a potential therapeutic target in the treatment of autoimmune disease, cancer metastasis, bone mineralization diseases, and osteoporosis. Applications Reported: This 2F10 antibody has been reported for use in western blotting, immunohistochemical staining of formalin-fixed paraffin embedded tissue sections, and immunocytochemistry. Applications Tested: This 2F10 antibody has been tested by immunohistochemistry of formalin-fixed paraffin embedded human tissue using either low or high pH antigen retrieval and can be used at less than or equal to 5 μg/mL. This 2F10 antibody has been tested by immunocytochemistry of either methanol-fixed or formaldehyde-fixed and permeabilized human cells and can be used at less than or equal to 10 μg/mL.

Osteopontin is an arginine-glycine-aspartic acid (RGD)-containing glycoprotein that interacts with integrins and CD44 as major receptors. It is a multifunctional protein involved in bone mineralization, cell adhesion, cell migration, chronic inflammatory disease and transformation. Proteolytic cleavage by thrombin and matrix metalloproteinases close to the integrin-binding Arg-Gly-Asp sequence modulates the function of OPN and its integrin binding properties. Thrombin-cleaved fragments of Osteopontin are overexpressed in malignant glial tumors and provide a molecular niche with survival advantage and provide a novel substrate for plasmin and cathepsin D.
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