HSPBP1 Antibody

Code CSB-PA010845GA01HU
Size $600
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Product Details

Uniprot No.
Target Names
HSPBP1
Alternative Names
1500019G21Rik antibody; FES1 antibody; Heat shock protein 70 binding protein antibody; Heat shock protein 70 interacting protein antibody; Heat shock protein binding protein 1 antibody; Heat shock protein-binding protein 1 antibody; Heat-shock 70-KD protein-binding protein 1 antibody; HPBP1_HUMAN antibody; Hsp 70 binding protein antibody; Hsp 70 interacting protein antibody; Hsp70 binding protein 1 antibody; Hsp70 binding protein 2 antibody; Hsp70 interacting protein 1 antibody; Hsp70 interacting protein 2 antibody; Hsp70-binding protein 1 antibody; Hsp70-binding protein 2 antibody; Hsp70-interacting protein 1 antibody; Hsp70-interacting protein 2 antibody; HSPA (heat shock 70kDa) binding protein, cytoplasmic cochaperone 1 antibody; HSPA-binding protein 1 antibody; HSPBP antibody; HspBP1 antibody; HspBP2 antibody; PP1845 antibody
Raised in
Rabbit
Species Reactivity
Human,Mouse,Rat
Immunogen
Human HSPBP1
Immunogen Species
Homo sapiens (Human)
Isotype
IgG
Purification Method
Antigen Affinity Purified
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
PBS with 0.1% Sodium Azide, 50% Glycerol, pH 7.3. -20°C, Avoid freeze / thaw cycles.
Tested Applications
ELISA,WB,IHC
Troubleshooting and FAQs
Storage
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.

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Target Background

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.
Gene References into Functions
  1. 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
  2. downregulation of Hsp70 and HspBP1 represents a unique feature of patients with preterm prelabor rupture of membranes PMID: 28497897
  3. 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
  4. Oxidative stress, inducing formation of disulfide bond, can affect stability and conformational mobility of human HspB1. PMID: 24898092
  5. BAG-1M and HspBP1 had differential impacts on the dynamic composition of steroid receptor folding complexes PMID: 24454860
  6. shown that HspBP1 binds Tag7 in the conditioned medium of tumor CSML0 cells, thereby preventing formation of the cytotoxic Tag7-Hsp70 complex PMID: 22037021
  7. High gene expression of HspBP1 is associated with leukemia. PMID: 20694586
  8. Results report cooperative interactions involving Hsp70, Hsp40, and TPR1 that enhance Hsp70-dependent folding of chemically denatured substrates. PMID: 14503850
  9. 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
  10. 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 PMID: 16169850
  11. 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
  12. 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
  13. 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
  14. that HspBP1, by antagonizing the prosurvival activity of Hsp70, sensitizes tumor cells to cathepsin-mediated cell death. PMID: 17855353
  15. Association between endogenous LAP2alpha and Hsp70 in non-transfected cells was confirmed by co-immunoprecipitation. PMID: 18261988
  16. The two chaperones, HSP72 and HSPBP1, interact both physically and functionally, leading to the activation of th EGFR-ERK1/2 signalling pathway. PMID: 18986301
  17. Results indicate that low HspBP1 expression could be a marker of tumor aggressiveness. PMID: 18987994
  18. Our data suggest that HIP may prevent inclusion formation by facilitating the constitutive HSC70 refolding cycle and possibly by preventing aggregation. PMID: 19183265
  19. HspBP1 may play a role in tumor (dys)regulation of chaperone proteins PMID: 19659607
  20. The cochaperone HspBP1 binds to and inhibits Hsp70 activity. PMID: 9830037

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Tissue Specificity
Ubiquitous.
Database Links

HGNC: 24989

OMIM: 612939

KEGG: hsa:23640

STRING: 9606.ENSP00000255631

UniGene: Hs.53066

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