BAG (BCL2 associated athanogene) family molecular chaperone regulator-3 (BAG3) is a member of BAG family of co-chaperones that interacts with Hsp70 (Heat shock protein 70).
Synonyms: Anti-BAG family molecular chaperone regulator 3; Anti-BAG-3; Anti-Bcl-2-associated athanogene 3; Anti-Bcl-2-binding protein Bis; Anti-Docking protein CAIR-1
Storage: -20C
Application: All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project (www.proteinatlas.org)and as a result, are supported by the most extensive characterization in the industry. The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.
Biochem Physiol Actions: BAG (BCL2 associated athanogene) family molecular chaperone regulator-3 (BAG3) protein has been described as an anti-apoptotic and pro-autophagic factor. Presence of HIV (Human immunodeficiency virus)-1 TAT protein up-regulates BAG3 levels, stimulating autophagy in human glial cells. BAG3 bind to major vault protein (MVP) and contribute to apoptosis resistance through activation of extracellular signal-regulated kinase1/2 (ERK1/2). This mechanism is responsible for chemotherapy resistance in breast cancer. BAG3 is overexpressed in lung carcinomas and exerts an anti-apoptotic effect in resistance to chemotherapy. Mutation in BAG3 causes myofibrillar myopathy, characterized by the formation of protein aggregates and myofibrillar disintegration.
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