Bag1 belongs to the Bcl-2 associated athanogene (BAG) family of multifunctional proteins and was the first of six related proteins isolated from humans. This widely expressed protein interacts with a number of signaling molecules (including Bcl2, HGF receptor and Raf1) as it regulates signaling molecules in pathways involving cell survival, growth and differentiation. The most common role played by Bag1 protein is as an inhibitor of proteins favoring apoptosis. Bag1 also plays a role in Raf1 signaling and binds DNA as a transcription activator. Bag1 protein is a well-characterized inhibitor of its binding partner HSP70. A conserved carboxy-terminal BAG domain within Bag1 interacts with the ATPase domain of HSP70 to negatively regulate heat shock protein chaperone activity. The multiple isoforms of Bag1 protein generated from a single transcript share a common ubiquitin homology domain and a carboxy-terminal Hsp70 binding region but differ in length and cellular localization. The 50 kDa long (Bag1-L) isoform also contains a nuclear localization signal and is often found in the nucleus where it activates transcription. The 46 kDa intermediate (Bag1-M) isoform is found mainly in the cytoplasm but can also translocate to the nucleus when associated with other proteins. The shorter 29-33 kDa isoforms (Bag1-S, Bag-1) isoforms are found primarily in the cytoplasm. High expression of the anti-apoptotic Bag1 protein correlates with increased survival in patients with particular forms of cancer, leading researchers to study possible therapeutic roles for Bag1 protein.
Bag1 belongs to the Bcl-2 associated athanogene (BAG) family of multifunctional proteins and was the first of six related proteins isolated from humans. This widely expressed protein interacts with a number of signaling molecules (including Bcl2, HGF receptor and Raf1) as it regulates signaling molecules in pathways involving cell survival, growth and differentiation. The most common role played by Bag1 protein is as an inhibitor of proteins favoring apoptosis. Bag1 also plays a role in Raf1 signaling and binds DNA as a transcription activator. Bag1 protein is a well-characterized inhibitor of its binding partner HSP70. A conserved carboxy-terminal BAG domain within Bag1 interacts with the ATPase domain of HSP70 to negatively regulate heat shock protein chaperone activity. The multiple isoforms of Bag1 protein generated from a single transcript share a common ubiquitin homology domain and a carboxy-terminal Hsp70 binding region but differ in length and cellular localization. The 50 kDa long (Bag1-L) isoform also contains a nuclear localization signal and is often found in the nucleus where it activates transcription. The 46 kDa intermediate (Bag1-M) isoform is found mainly in the cytoplasm but can also translocate to the nucleus when associated with other proteins. The shorter 29-33 kDa isoforms (Bag1-S, Bag-1) isoforms are found primarily in the cytoplasm. High expression of the anti-apoptotic Bag1 protein correlates with increased survival in patients with particular forms of cancer, leading researchers to study possible therapeutic roles for Bag1 protein.
Size
100μl(100μg)
Species
Homo Sapiens (Human)
Subcellular Location
Isoform 1: Nucleus, Cytoplasm, Note=Isoform 1 localizes predominantly to the nucleus, SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, Nucleus, Note=Isoform 2 localizes to the cytoplasm and shuttles into the nucleus in response to heat shock, SUBCELLULAR LOCATION: Isoform 4: Cytoplasm, Nucleus
The oncogene BCL2 is a membrane protein that blocks a step in a pathway leading to apoptosis or programmed cell death. This protein binds to BCL2 and is referred to as BCL2-associated athanogene. It enhances the anti-apoptotic effects of BCL2 and represents a link between growth factor receptors and anti-apoptotic mechanisms. At least three protein isoforms are encoded by this mRNA through the use of a non-AUG (CUG) start site, and alternative, downstream, AUG translation initiation sites.
Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release. Nucleotide release is mediated via its binding to the nucleotide-binding domain (NBD) of HSPA8/HSC70 where as the substrate release is mediated via its binding to the substrate-binding domain (SBD) of HSPA8/HSC70
Pathway
Protein processing in endoplasmic reticulum
Tissue Specificity
Isoform 4 is the most abundantly expressed isoform. It is ubiquitously expressed throughout most tissues, except the liver, colon, breast and uterine myometrium. Isoform 1 is expressed in the ovary and testis. Isoform 4 is expressed in several types of tu
Buffer
Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.
Format
liquid
Purification
Affinity purification
Purity
Affinity purification
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Storage Buffer
Store at -20oC or -80oC. Avoid freeze / thaw cycles. Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.