Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Usage
For Research Use Only. Not for use in diagnostic or therapeutic procedures.
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.
Gene References into Functions
Findings indicate a critical role of HspBP1 in differential CHIP/Hsp70 activities in neuronal and glial cells and the greater neuronal vulnerability to misfolded proteins in neurodegenerative diseases.PMID:28847953
downregulation of Hsp70 and HspBP1 represents a unique feature of patients with preterm prelabor rupture of membranesPMID:28497897
our results clearly show that HspBP1 acts as an endogenous negative regulator of HIV-1 gene-expression and replication by suppressing NF-kappaB-mediated activation of viral transcription.PMID:26538602
Oxidative stress, inducing formation of disulfide bond, can affect stability and conformational mobility of human HspB1.PMID:24898092
BAG-1M and HspBP1 had differential impacts on the dynamic composition of steroid receptor folding complexesPMID:24454860
shown that HspBP1 binds Tag7 in the conditioned medium of tumor CSML0 cells, thereby preventing formation of the cytotoxic Tag7-Hsp70 complexPMID:22037021
High gene expression of HspBP1 is associated with leukemia.PMID:20694586
Results report cooperative interactions involving Hsp70, Hsp40, and TPR1 that enhance Hsp70-dependent folding of chemically denatured substrates.PMID:14503850
Detection of hsp70 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.PMID:14761400
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 CHIPPMID:16169850
The results demonstrate that Hsp70 and HspBP1 are not coordinately regulated but provide evidence that an increase in the ratio of HspBP1 to Hsp70 correlates with apoptosis, in a similar way to reducing the amount of Hsp70.PMID:16677834
Stress-induced heat shock protein 70 (Hsp70) effectively protects cells against ultraviol ray-induced apoptosis in melanocytes bu penetrating mitchondrial and lysosomal membranes.PMID:16950797
Here, we report that upon the formation of huntingtin aggregates; endogenous cytosolic huntingtin, Hsc70/Hsp70 (heat shock protein and cognate protein of 70kDa) and syntaxin 1A become aggregate-centered.PMID:17208201
that HspBP1, by antagonizing the prosurvival activity of Hsp70, sensitizes tumor cells to cathepsin-mediated cell death.PMID:17855353
Association between endogenous LAP2alpha and Hsp70 in non-transfected cells was confirmed by co-immunoprecipitation.PMID:18261988
The two chaperones, HSP72 and HSPBP1, interact both physically and functionally, leading to the activation of th EGFR-ERK1/2 signalling pathway.PMID:18986301
Results indicate that low HspBP1 expression could be a marker of tumor aggressiveness.PMID:18987994
Our data suggest that HIP may prevent inclusion formation by facilitating the constitutive HSC70 refolding cycle and possibly by preventing aggregation.PMID:19183265
HspBP1 may play a role in tumor (dys)regulation of chaperone proteinsPMID:19659607
The cochaperone HspBP1 binds to and inhibits Hsp70 activity.PMID:9830037