HSPBP1 Human

Heat Shock Protein-Binding Protein 1 Human Recombinant

Cat. No.

BT19035

Source

Escherichia Coli.

Synonyms

Hsp70-binding protein 1, Heat shock protein-binding protein 1, Hsp70-interacting protein 1, Hsp70-binding protein 2, Hsp70-interacting protein 2, HspBP1, HspBP2, HSPBP1, HSPBP, FES1.

Appearance

Sterile filtered colorless solution.

Purity

Greater than 95% as determined by SDS-PAGE.

Usage

THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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Description

HSPBP1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 382 amino acids (1-362 a.a.) and having a molecular mass of 41.6kDa. HSPBP1 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction

Hsp70-binding protein 1 (HSPBP1) belongs to a family of eukaryotic proteins known as nucleotide exchange factors for HSP 70. These proteins demonstrate varying degrees of specificity for compartments and species. HSPBP1 is primarily found in the cytoplasm and nucleus, but it can also be detected outside of cells. Its expression is highest in heart and skeletal muscle. HSPBP1 interacts with HSP 70, inhibiting its activity and facilitating the release of nucleotides from the ATPase domain of HSP 70. Moreover, HSPBP1 hinders the chaperone activity of HSPA1A by altering the conformation of its ATP-binding domain, thereby impeding ATP binding. There is a possibility that HSPBP1 plays a role in the (dys)regulation of chaperone proteins in tumors. Additionally, HSPBP1 interferes with STUB1-mediated ubiquitination and hampers the chaperone-assisted degradation of immature CFTR.

Description

Recombinant human HSPBP1, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 382 amino acids (specifically, amino acids 1 to 362). It possesses a molecular weight of 41.6 kDa. A 20 amino acid His Tag is fused to the N-terminus of HSPBP1. The protein undergoes purification using proprietary chromatographic methods.

Physical Appearance

A clear, colorless solution that has been sterilized by filtration.

Formulation

HSPBP1 solution is prepared in a buffer containing 20mM Tris-HCl (pH 8.0), 2mM DTT, 30% glycerol, 2mM EDTA, and 0.1M NaCl.

Stability

Recombinant human HSPBP1 maintains stability for 1 week when stored at 4°C. However, it is recommended to store the protein at a temperature below -18°C to ensure optimal long-term stability. Repeated freeze-thaw cycles should be avoided.

Purity

The purity of the protein is determined to be greater than 95% based on SDS-PAGE analysis.

Synonyms

Hsp70-binding protein 1, Heat shock protein-binding protein 1, Hsp70-interacting protein 1, Hsp70-binding protein 2, Hsp70-interacting protein 2, HspBP1, HspBP2, HSPBP1, HSPBP, FES1.

Source

Escherichia Coli.

Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH 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.

Product Science Overview

Introduction

Heat Shock Protein-Binding Protein 1 (HSBP1) is a crucial component in the cellular response to stress. It is a 76-amino-acid protein that binds to Heat Shock Factor 1 (HSF1), a transcription factor involved in the heat shock response. This response is triggered by exposure to thermal and chemical stress, leading to the elevated expression of heat-shock-induced genes.

Structure and Function

HSBP1 is nuclear-localized and interacts with the active trimeric state of HSF1 to negatively regulate HSF1 DNA-binding activity. During the heat shock response, HSF1 undergoes a conformational transition from an inert non-DNA-binding monomer to active functional trimers. HSBP1 binds to these trimers, repressing the transactivation activity of HSF1.

Role in Cellular Stress Response

The heat shock response is a protective mechanism that helps cells survive under adverse conditions such as elevated temperatures, toxins, and other stressors. HSBP1 plays a negative regulatory role in this process. Overexpression of HSBP1 in mammalian cells represses the transactivation activity of HSF1, thereby modulating the heat shock response. In model organisms like C. elegans, overexpression of HSBP1 has severe effects on survival after thermal and chemical stress, consistent with its role as a negative regulator.

Implications in Aging and Disease

HSBP1 may also have a role in the suppression of the activation of the stress response during the aging process. Its interaction with HSF1 and the subsequent regulation of heat shock proteins (HSPs) are crucial for maintaining cellular homeostasis. Dysregulation of HSBP1 and HSF1 activity has been implicated in various diseases, including cancer.

Recombinant HSBP1

Recombinant HSBP1 is produced using recombinant DNA technology, which involves inserting the HSBP1 gene into an expression vector and introducing it into a host cell, such as E. coli or yeast. The host cells then produce the HSBP1 protein, which can be purified for research and therapeutic purposes. Recombinant HSBP1 is used in various studies to understand its function and role in the heat shock response and other cellular processes.

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HSPBP1 Human

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