Recombinant Human Hsp70-binding protein 1 (HSPBP1)

Code CSB-YP885777HU
MSDS
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Source Yeast
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Code CSB-EP885777HU
MSDS
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Source E.coli
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Code CSB-EP885777HU-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP885777HU
MSDS
Size Pls inquire
Source Baculovirus
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Code CSB-MP885777HU
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
HSPBP1
Uniprot No.
Alternative Names
1500019G21Rik; FES1; Heat shock protein 70 binding protein; Heat shock protein 70 interacting protein; Heat shock protein binding protein 1; Heat shock protein-binding protein 1; Heat-shock 70-KD protein-binding protein 1; HPBP1_HUMAN; Hsp 70 binding protein; Hsp 70 interacting protein; Hsp70 binding protein 1; Hsp70 binding protein 2; Hsp70 interacting protein 1; Hsp70 interacting protein 2; 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; HSPA-binding protein 1; HSPBP ; HspBP1; HspBP2; PP1845
Species
Homo sapiens (Human)
Expression Region
1-362
Target Protein Sequence
MSDEGSRGSR LPLALPPASQ GCSSGGGGGG GGGSSAGGSG NSRPPRNLQG LLQMAITAGS EEPDPPPEPM SEERRQWLQE AMSAAFRGQR EEVEQMKSCL RVLSQPMPPT AGEAEQAADQ QEREGALELL ADLCENMDNA ADFCQLSGMH LLVGRYLEAG AAGLRWRAAQ LIGTCSQNVA AIQEQVLGLG ALRKLLRLLD RDACDTVRVK ALFAISCLVR EQEAGLLQFL RLDGFSVLMR AMQQQVQKLK VKSAFLLQNL LVGHPEHKGT LCSMGMVQQL VALVRTEHSP FHEHVLGALC SLVTDFPQGV RECREPELGL EELLRHRCQL LQQHEEYQEE LEFCEKLLQT CFSSPADDSM DR
Protein Length
full length protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ 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.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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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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