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Recombinant Human Hsp70-binding protein 1 (HSPBP1)

Recombinant Human Hsp70-binding protein 1 (HSPBP1)

Code
MSDS	MSDS Datasheet
Size	Pls inquire
Source
Conjugate
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Product Details
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Target Background

Product Details

Abbreviation

HSPBP1

Purity

>85% (SDS-PAGE)

Target Names

HSPBP1

Uniprot NO.

Q9NZL4

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)

Source

Yeast

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
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Protein Length

full length protein

Tag Info

N-terminal His-tagged/Tag-Free
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.

Storage Condition

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.

Shelf Life

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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Target Background

Function(From Uniprot)

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 membranes PMID: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 complexes PMID:24454860
shown that HspBP1 binds Tag7 in the conditioned medium of tumor CSML0 cells, thereby preventing formation of the cytotoxic Tag7-Hsp70 complex PMID: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 CHIP PMID: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 proteins PMID:19659607
The cochaperone HspBP1 binds to and inhibits Hsp70 activity. PMID:9830037