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Inhibits HSPA1A chaperone activity by changing the conformation of the ATP-binding domain of HSPA1A and interfering with ATP binding. Additionally we are shipping HSPA Binding Protein, Cytoplasmic Cochaperone 1 Antibodies (113) and HSPA Binding Protein, Cytoplasmic Cochaperone 1 Proteins (10) and many more products for this protein.
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our results clearly show that HspBP1 acts as an endogenous negative regulator of HIV-1 gene-expression and replication by suppressing NF-kappaB (show NFKB1 ELISA Kits)-mediated activation of viral transcription.
Oxidative stress, inducing formation of disulfide bond, can affect stability and conformational mobility of human HspB1 (show HSPB1 ELISA Kits).
BAG-1M and HspBP1 had differential impacts on the dynamic composition of steroid receptor (show ESR2 ELISA Kits) folding complexes
shown that HspBP1 binds Tag7 (show PGLYRP1 ELISA Kits) in the conditioned medium of tumor CSML0 cells, thereby preventing formation of the cytotoxic Tag7 (show PGLYRP1 ELISA Kits)-Hsp70 (show HSP70 ELISA Kits) complex
High gene expression of HspBP1 is associated with leukemia.
Results report cooperative interactions involving Hsp70 (show HSP70 ELISA Kits), Hsp40 (show DNAJB1 ELISA Kits), and TPR1 that enhance Hsp70 (show HSP70 ELISA Kits)-dependent folding of chemically denatured substrates.
Detection of hsp70 (show HSP70 ELISA Kits) may be used as the screening marker for diagnosis of polycyclic aromatic hydrocarbons (PAHs)-related lung cancer related lung cancer, and may supplement the diagnostic value of conventional cytology.
HspBP1 interferes with the CHIP-induced degradation of immature forms of the cystic fibrosis transmembrane conductance regulator (CFTR (show CFTR ELISA Kits)) and stimulates CFTR (show CFTR ELISA Kits) maturation.
BAG2 binds to the carboxyl terminus of Hsp70-interacting protein (CHIP) and provides a cochaperone-dependent regulatory mechanism for preventing unregulated ubiquitylation of misfolded proteins by CHIP
The results demonstrate that Hsp70 (show HSP70 ELISA Kits) and HspBP1 are not coordinately regulated but provide evidence that an increase in the ratio of HspBP1 to Hsp70 (show HSP70 ELISA Kits) correlates with apoptosis, in a similar way to reducing the amount of Hsp70 (show HSP70 ELISA Kits).
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.
Hsp70 binding protein 1
, heat shock protein-binding protein 1
, hsp70 interacting protein
, hsp70-binding protein 1
, hsp70-binding protein 2
, hsp70-interacting protein 1
, hsp70-interacting protein 2
, HSPA (heat shock 70kDa) binding protein, cytoplasmic cochaperone 1
, SPA ) binding protein, cytoplasmic cochaperone 1