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The region for expressing recombinant Human BAG2 contains amino acids 1-211. This BAG2 protein is theoretically predicted to have a molecular weight of 50.8 kDa. The BAG2 protein was expressed in e.coli. The N-terminal GST tag was fused into the coding gene segment of BAG2, making it easier to detect and purify the BAG2 recombinant protein in the later stages of expression and purification.The research of BAG family molecular chaperone regulator 2 (BAG2) covers various scientific areas. In cancer research, the expression of BAG2 is closely associated with the occurrence and development of multiple tumors, particularly playing a crucial role in regulating cell apoptosis, proliferation, and migration. Scientists have discovered that BAG2, through interactions with molecular chaperones, is involved in protein folding and degradation, playing a vital role in intracellular protein quality control. In the field of neurology, the study of BAG2 involves the pathogenic mechanisms of neurodegenerative diseases, as its relationship with protein stability is believed to potentially impact the survival of neurons.
The region for expressing recombinant Human BAG2 contains amino acids 1-211. This BAG2 protein is theoretically predicted to have a molecular weight of 50.8 kDa. The BAG2 protein was expressed in e.coli. The N-terminal GST tag was fused into the coding gene segment of BAG2, making it easier to detect and purify the BAG2 recombinant protein in the later stages of expression and purification.The research of BAG family molecular chaperone regulator 2 (BAG2) covers various scientific areas. In cancer research, the expression of BAG2 is closely associated with the occurrence and development of multiple tumors, particularly playing a crucial role in regulating cell apoptosis, proliferation, and migration. Scientists have discovered that BAG2, through interactions with molecular chaperones, is involved in protein folding and degradation, playing a vital role in intracellular protein quality control. In the field of neurology, the study of BAG2 involves the pathogenic mechanisms of neurodegenerative diseases, as its relationship with protein stability is believed to potentially impact the survival of neurons.
| Cat.No | ACP03413 | Target Name | BAG2 |
|---|---|---|---|
| Form | Liquid or Lyophilized powder | Expression System | E.coli |
| Expression Range | 1-211aa | Mol Weight | 50.6kDa |
| Protein Length | Full length | Purity | Greater than 90% as determined by SDS-PAGE. |
| Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | O95816 |
|---|
Uniprot Id
O95816
Target Species
Human
Target Name
BAG2
Target Full Name
BAG family molecular chaperone regulator 2
Target Function
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.
Target Research Area
Cell Biology
Target Synonyms
BAG 2; BAG family molecular chaperone regulator 2; BAG-2; BAG-family molecular chaperone regulator-2; Bag2; BAG2_HUMAN; BCL 2 associated athanogene 2; Bcl-2-associated athanogene 2; BCL2 associated athanogene 2; BCL2-associated athanogene 2; dJ417I1.2 (BAG family molecular chaperone regulator 2); dJ417I1.2; KIAA0576; MGC149462; OTTHUMP00000016668
Target Background
BAG proteins compete with Hip for binding to the Hsc70/Hsp70 ATPase domain and promote substrate release. All the BAG proteins have an approximately 45-amino acid BAG domain near the C terminus but differ markedly in their N-terminal regions. The predicted BAG2 protein contains 211 amino acids. The BAG domains of BAG1, BAG2, and BAG3 interact specifically with the Hsc70 ATPase domain in vitro and in mammalian cells. All 3 proteins bind with high affinity to the ATPase domain of Hsc70 and inhibit its chaperone activity in a Hip-repressible manner.
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