HSPBP1 Protein, Human
Based on 1 publication(s) in Google Scholar
HSPBP1 protein regulates HSPA1A chaperone activity by inducing conformational changes in the ATP-binding domain and disrupting ATP binding. This interference inhibits the STUB1-mediated ubiquitination process and blocks chaperone-assisted degradation of immature CFTR. HSPBP1 Protein, Human is the recombinant human-derived HSPBP1 protein, expressed by E. coli , with tag free.
- Species: Human
- Source: E. coli
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Storage:Stored at -80°C for 1 year from date of receipt. It is stable at -20°C for 3 months after opening. It is recommended to freeze aliquots at -80°C for extended storage. Avoid repeated freeze-thaw cycles.
Biological Activity
HSPBP1 protein regulates HSPA1A chaperone activity by inducing conformational changes in the ATP-binding domain and disrupting ATP binding. This interference inhibits the STUB1-mediated ubiquitination process and blocks chaperone-assisted degradation of immature CFTR. HSPBP1 Protein, Human is the recombinant human-derived HSPBP1 protein, expressed by E. coli , with tag free.
HSPBP1 Protein exerts regulatory control over HSPA1A chaperone activity by inducing conformational changes in the ATP-binding domain of HSPA1A, thereby disrupting ATP binding. This interference results in the inhibition of ubiquitination processes mediated by STUB1 and impedes the chaperone-assisted degradation of immature CFTR. The protein is known to interact with the ATP-binding domain of HSPA1A, forming a ternary complex with STUB1 and HSPBP1. Additionally, its interaction with PGLYRP1 serves to block the cytotoxic activity of the PGLYRP1-HSPA1A complex, highlighting the multifaceted regulatory roles of HSPBP1 in cellular processes.
Publications (1)
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Journal Impact Factor
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Most Recent
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Cell Death Dis
Identification of human MLKL Cys184 and HSPBP1 Cys201 as novel cellular targets for necroptosis. [Abstract]2026 Apr 22;17(1):528. PMID: 42014672
Technical Parameters
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Species Human
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Source E. coli
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Tag Tag Free
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Accession
Q9NZL4 (R84-R359)
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Gene ID23640
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Molecular Construction
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N-term
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HSPBP1 (R84-R359)
Accession # Q9NZL4 -
C-term
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Protein Length
Partial
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Synonyms
HSPBP1; Hsp70-Interacting Protein 2; HSPA (Hsp70) Binding Protein 1; Hsp70-Interacting Protein 1; FES1; Hsp70-Binding Protein 2; HSPA (Heat Shock 70kDa) Binding Protein, Cytoplasmic Cochaperone 1; HspBP2; Heat Shock Protein-Binding Protein 1; HspBP1; Hsp7
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AA Sequence
RGQREEVEQMKSCLRVLSQPMPPTAGEAEQAADQQEREGALELLADLCENMDNAADFCQLSGMHLLVGRYLEAGAAGLRWRAAQLIGTCSQNVAAIQEQVLGLGALRKLLRLLDRDACDTVRVKALFAISCLVREQEAGLLQFLRLDGFSVLMRAMQQQVQKLKVKSAFLLQNLLVGHPEHKGTLCSMGMVQQLVALVRTEHSPFHEHVLGALCSLVTDFPQGVRECREPELGLEELLRHRCQLLQQHEEYQEELEFCEKLLQTCFSSPADDSMDR
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Predicted Molecular Mass
30.9 kDa
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Purity
≥ 90%, as determined by reducing SDS-PAGE.
Product Properties
Solution.
Supplied as a 0.22 μm filtered solution of 50 mM Tris-HCl, pH7.5, 200 mM NaCl, 20% glycerol.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.
<1 EU/μg, determined by LAL method.
Please use rapid thawing with running water to thaw the protein.
Stored at -80°C for 1 year from date of receipt. It is stable at -20°C for 3 months after opening. It is recommended to freeze aliquots at -80°C for extended storage. Avoid repeated freeze-thaw cycles.
Shipping with dry ice.
Documentation
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Data Sheet (236 KB)
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SDS (251 KB)
- English - EN (251 KB)
- Français - FR (251 KB)
- Deutsch - DE (251 KB)
- Norwegian - NO (251 KB)
- Español - ES (251 KB)
- Swedish - SV (251 KB)
- Italian - IT (251 KB)
- Korean - KR (251 KB)
- Portuguese - PT (251 KB)
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Handling Instructions (2659 KB)
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)