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Rabbit Anti-BAG3 Recombinant Antibody (CBYY-0164) (CBMAB-0165-YY)

This product is rabbit antibody that recognizes BAG3. The antibody CBYY-0164 can be used for immunoassay techniques such as: WB, IP, IHC-P
See all BAG3 antibodies

Summary

Host Animal
Rabbit
Specificity
Human, Mouse
Clone
CBYY-0164
Antibody Isotype
IgG
Application
WB, IHC-P

Basic Information

Immunogen
A synthetic peptide corresponding to a sequence within amino acids 50-150 of human BAG3.
Specificity
Human, Mouse
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:500-1:2,000
IHC-P1:50-1:200

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, 0.05% BSA, 50% glycerol, pH7.3
Preservative
0.02% sodium azide
Concentration
Batch dependent
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
C-terminus

Target

Full Name
BCL2 Associated Athanogene 3
Introduction
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 protein encoded by this gene contains a WW domain in the N-terminal region and a BAG domain in the C-terminal region. 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.
Entrez Gene ID
9531
UniProt ID
O95817
Alternative Names
BCL2 Associated Athanogene 3; Bcl-2-Binding Protein Bis; Docking Protein CAIR-1; BAG-3; BIS; BAG Family Molecular Chaperone Regulator 3;
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. 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 (PubMed:9873016, PubMed:27474739).
Has anti-apoptotic activity (PubMed:10597216).
Plays a role in the HSF1 nucleocytoplasmic transport (PubMed:26159920).
Biological Process
Aggresome assembly Source: ARUK-UCL
Autophagosome assembly Source: Ensembl
Brain development Source: Ensembl
Cellular response to heat Source: UniProtKB
Cellular response to mechanical stimulus Source: Ensembl
Cellular response to unfolded protein Source: ARUK-UCL
Chaperone-mediated autophagy Source: Ensembl
Chaperone-mediated protein transport Source: ARUK-UCL
Extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
Extrinsic apoptotic signaling pathway via death domain receptors Source: MGI
Muscle cell cellular homeostasis Source: ARUK-UCL
Negative regulation of apoptotic process Source: UniProtKB
Negative regulation of protein targeting to mitochondrion Source: Ensembl
Negative regulation of striated muscle cell apoptotic process Source: ARUK-UCL
Negative regulation of transcription from RNA polymerase II promoter in response to stress Source: UniProtKB
Positive regulation of aggrephagy Source: ARUK-UCL
Positive regulation of protein export from nucleus Source: UniProtKB
Positive regulation of protein import into nucleus Source: UniProtKB
Protein folding Source: UniProtKB
Protein stabilization Source: ARUK-UCL
Protein transport along microtubule Source: ARUK-UCL
Regulation of cellular response to heat Source: Reactome
Spinal cord development Source: Ensembl
Cellular Location
Cytoplasm; Nucleus. Colocalizes with HSF1 to the nucleus upon heat stress (PubMed:26159920).
Involvement in disease
Myopathy, myofibrillar, 6 (MFM6): A form of myofibrillar myopathy, a group of chronic neuromuscular disorders characterized at ultrastructural level by disintegration of the sarcomeric Z disk and myofibrils, and replacement of the normal myofibrillar markings by small dense granules, or larger hyaline masses, or amorphous material. MFM6 is characterized by early-onset of severe, progressive, diffuse muscle weakness associated with cardiomyopathy, severe respiratory insufficiency during adolescence, and a rigid spine in some patients.
Cardiomyopathy, dilated 1HH (CMD1HH): A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.

Kirk, J. A., Cheung, J. Y., & Feldman, A. M. (2021). Therapeutic targeting of BAG3: considering its complexity in cancer and heart disease. Journal of Clinical Investigation, 131(16), e149415.

Lövenich, L., Dreissen, G., Hoffmann, C., Konrad, J., Springer, R., Höhfeld, J., ... & Hoffmann, B. (2021). Strain-induced mechanoresponse depends on cell contractility and BAG3-mediated autophagy. Molecular Biology of the Cell, 32(20), ar9.

Ruparelia, A. A., McKaige, E. A., Williams, C., Schulze, K. E., Fuchs, M., Oorschot, V., ... & Bryson-Richardson, R. J. (2020). Metformin rescues muscle function in BAG3 myofibrillar myopathy models. Autophagy, 1-17.

Kögel, D., Linder, B., Brunschweiger, A., Chines, S., & Behl, C. (2020). At the crossroads of apoptosis and autophagy: multiple roles of the co-chaperone BAG3 in stress and therapy resistance of cancer. Cells, 9(3), 574.

Wang, J. M., Liu, B. Q., Du, Z. X., Li, C., Sun, J., Yan, J., ... & Wang, H. Q. (2020). p53‐dependent transcriptional suppression of BAG3 protects cells against metabolic stress via facilitation of p53 accumulation. Journal of cellular and molecular medicine, 24(1), 562-572.

Diofano, F., Weinmann, K., Schneider, I., Thiessen, K. D., Rottbauer, W., & Just, S. (2020). Genetic compensation prevents myopathy and heart failure in an in vivo model of Bag3 deficiency. PLoS genetics, 16(11), e1009088.

Li, X. Y., Yan, J., Sun, J., Li, C., Jiang, J. Y., Wang, J. M., ... & Wang, H. Q. (2019). BAG3 deletion suppresses stem cell-like features of pancreatic ductal adenocarcinoma via translational suppression of ISG15. Biochimica et Biophysica Acta (BBA)-Molecular Cell Research, 1866(5), 819-827.

Furusawa, Y., Yunoki, T., Hirano, T., Minagawa, S., Izumi, H., Mori, H., ... & Tabuchi, Y. (2018). Identification of genes and genetic networks associated with BAG3‑dependent cell proliferation and cell survival in human cervical cancer HeLa cells. Molecular medicine reports, 18(4), 4138-4146.

Mizushima, W., & Sadoshima, J. (2017). BAG3 plays a central role in proteostasis in the heart. The Journal of clinical investigation, 127(8), 2900-2903.

Liu, B. Q., Zhang, S., Li, S., An, M. X., Li, C., Yan, J., ... & Wang, H. Q. (2017). BAG3 promotes stem cell-like phenotype in breast cancer by upregulation of CXCR4 via interaction with its transcript. Cell death & disease, 8(7), e2933-e2933.

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For research use only. Not intended for any clinical use.

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