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Mouse Anti-HSPBP1 Recombinant Antibody (CBFYH-2413) (CBMAB-H3425-FY)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBFYH-2413
Antibody Isotype
IgG2b
Application
WB, IHC, IF, FC

Basic Information

Immunogen
Full length human recombinant protein of human HSPBP1 produced in HEK293T cell
Specificity
Human
Antibody Isotype
IgG2b
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

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

Format
Liquid
Buffer
PBS, PH 7.3, 1% BSA, 50% glycerol
Preservative
0.02% Sodium azide
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
HSPA (Hsp70) Binding Protein 1
Introduction
HSPBP1 (HSPA (Hsp70) Binding Protein 1) is a Protein Coding gene. Diseases associated with HSPBP1 include Long Qt Syndrome 2. Among its related pathways are Protein processing in endoplasmic reticulum and Mechanisms of CFTR activation by S-nitrosoglutathione (normal and CF). Gene Ontology (GO) annotations related to this gene include binding and enzyme inhibitor activity.
Entrez Gene ID
23640
UniProt ID
Q9NZL4
Alternative Names
HSPA (Hsp70) Binding Protein 1; HSPA (Heat Shock 70kDa) Binding Protein, Cytoplasmic Cochaperone 1; Heat Shock Protein-Binding Protein 1; Hsp70 Interacting Protein; Hsp70-Interacting Protein 1; Hsp70-Interacting Protein 2; Hsp70-Binding Protein 1
Function
Inhibits HSPA1A chaperone activity by changing the conformation of the ATP-binding domain of HSPA1A and interfering with ATP binding. Interferes with ubiquitination mediated by STUB1 and inhibits chaperone-assisted degradation of immature CFTR.
Biological Process
Positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: BHF-UCL
Positive regulation of protein ubiquitination Source: BHF-UCL
Protein folding Source: ProtInc
More Infomation

Iyer, K., Mitra, A., & Mitra, D. (2023). Identification of 5’upstream sequence involved in HSPBP1 gene transcription and its downregulation during HIV-1 infection. Virus Research, 324, 199034.

Bracher, A., & Verghese, J. (2022). Nucleotide Exchange Factors for Hsp70 Molecular Chaperones: GrpE, Hsp110/Grp170, HspBP1/Sil1, and BAG Domain Proteins. The Networking of Chaperones by Co-Chaperones, 1-39.

Youn, C. K., Lee, J. H., Hariharasudhan, G., Kim, H. B., Kim, J., Lee, S., ... & You, H. J. (2022). HspBP1 is a dual function regulatory protein that controls both DNA repair and apoptosis in breast cancer cells. Cell death & disease, 13(4), 309.

Yang, Y. X., Huang, J. P., Li, S. N., Li, J., Ling, T., Xie, T., & Xu, L. G. (2021). HSPBP1 facilitates cellular RLR-mediated antiviral response by inhibiting the K48-linked ubiquitination of RIG-I. Molecular Immunology, 134, 62-71.

Mahboubi, H., Moujaber, O., Kodiha, M., & Stochaj, U. (2020). The co-chaperone HspBP1 is a novel component of stress granules that regulates their formation. Cells, 9(4), 825.

Ceccin, A. D. F., Souza, A. P. D., Hilário, G. T., Muller, D. M., Romão, P. R. T., & Rodrigues Junior, L. C. (2019). HspBP1 and anti‐HspBP1 levels in the serum of HIV‐infected individuals are associated to the disease progression. Journal of applied microbiology, 127(2), 576-585.

Gowda, N. K., Kaimal, J. M., Kityk, R., Daniel, C., Liebau, J., Öhman, M., ... & Andréasson, C. (2018). Nucleotide exchange factors Fes1 and HspBP1 mimic substrate to release misfolded proteins from Hsp70. Nature structural & molecular biology, 25(1), 83-89.

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

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