Anti-BAG3 (BAG Family Molecular Chaperone Regulator 3, BAG-3, Bcl-2-associated Athanogene 3, Bcl-2-b

The BAG (Bcl-2-associated anthanogene) proteins are a family of chaperone regulators that modulate a number of diverse processes including proliferation, survival, stress responses, tumorigenesis, neuronal differentiation, growth arrest and apoptosis. BAG proteins have been characterized as co-chaperones and interact with the chaperone heat shock proteins 70, both constitutive Hsc70 and inducible Hsp70. BAG proteins bind through their BAG domain to the ATPase domain of Hsc70/Hsp70, and can modulate either positively or negatively the functions of the Hsc70/Hsp70 chaperone proteins. The BAG domain has been shown to contribute to the anti-apoptotic activity of BAG- family proteins. The anti-apoptotic activities of BAG-family proteins may be dependent on their interactions with Hsc70/Asp70 and/or binding to Bcl-2. In addition to the conserved BAG domain, BAG-family proteins also contain additional domains which enable them to interact with specific target proteins or to target them to specific locations within cells. The BAG family contains at least six family members, including BAG-1 and its various isoforms [including BAG-1S , BAG-1M (RAP46/HAP46), and BAG-1L, BAG2, BAG3 (CAIR-1, Bis,), BAG4 (SODD), BAG5 and BAG6 (Scythe, BAT3). Applications: Suitable for use in Western Blot, Immunohistochemistry and Immunoprecipitation. Other applications not tested. Recommended Dilution: Western Blot: 1:1000-1:2000, Immunohistochemistry (formalin fixed paraffin embedded): 1:1000-1:5000, Immunoprecipitation: 1:50-1:200, Immunohistochemistry: Frozen, Optimal dilutions to be determined by the researcher. Positive Control: Muscle, muscle, PANC-1 pancreatic cell line (ATCC-CRL 1469), Storage and Stability: May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.