HSBP 1 Human

Heat Shock Factor Binding Protein - 1 Human Recombinant
Cat. No.
BT16516
Source
Escherichia Coli.
Synonyms
NPC-A-13, HSBP1, Heat shock factor-binding protein 1, Nasopharyngeal carcinoma-associated antigen 13, HSF1BP, DKFZp686D1664, DKFZp686O24200.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

Recombinant Human HSBP1 produced in E.Coli is a single,non-glycosylated polypeptide chain containing 76 amino acids and having a molecular mass of 8.5 kDa.

Product Specs

Introduction
Heat shock factor binding protein-1 (HSBP1) is a 76-amino-acid protein that negatively regulates the heat shock response. HSBP1 binds to heat shock factor 1 (HSF1), a transcription factor activated during cellular stress. Upon activation, HSF1 transitions from an inactive monomer to an active trimer, binding DNA and initiating the transcription of heat shock genes. HSBP1 interacts with the active HSF1 trimer, inhibiting its DNA-binding activity and thereby suppressing the expression of heat shock genes. Studies have shown that overexpression of HSBP1 in mammalian cells hinders HSF1's ability to activate transcription. Similarly, in C. elegans, elevated HSBP1 levels negatively impact the organism's survival after exposure to heat or chemical stress, further supporting its role as a negative regulator of the heat shock response.
Description
Recombinant Human HSBP1 is a non-glycosylated polypeptide chain containing 76 amino acids, with a molecular weight of 8.5 kDa. It is produced in E. coli and purified to a single band.
Physical Appearance
Clear, colorless solution, sterile-filtered.
Formulation
The HSBP1 protein solution is supplied at a concentration of 1 mg/ml in a buffer consisting of 20mM Tris-HCl (pH 7.5), 50mM NaCl, 1mM EDTA, and 20% glycerol.
Stability
For short-term storage (up to 4 weeks), the protein solution can be stored at 4°C. For long-term storage, it is recommended to store the solution at -20°C. The addition of a carrier protein such as HSA or BSA (0.1%) is advised for long-term storage. Repeated freezing and thawing should be avoided.
Purity
The purity of HSBP1 is greater than 95%, as determined by SDS-PAGE analysis.
Synonyms
NPC-A-13, HSBP1, Heat shock factor-binding protein 1, Nasopharyngeal carcinoma-associated antigen 13, HSF1BP, DKFZp686D1664, DKFZp686O24200.
Source
Escherichia Coli.
Amino Acid Sequence

MAETDPKTVQ DLTSVVQTLL QQMQDKFQTM SDQIIGRIDD MSSRIDDLEK NIADLMTQAG VEELESENKI PATQKS.

Product Science Overview

Introduction

Heat Shock Factor Binding Protein 1 (HSBP1) is a protein that plays a crucial role in the regulation of the heat shock response. This response is a cellular defense mechanism against stress conditions such as elevated temperatures, toxins, and other environmental stressors. HSBP1 is known to interact with Heat Shock Factor 1 (HSF1), a transcription factor that activates the expression of heat shock proteins (HSPs) which help in protein folding and protection against stress-induced damage .

Structure and Function

HSBP1 is a small protein consisting of 76 amino acids. It is predominantly localized in the nucleus and interacts with the active trimeric state of HSF1. HSF1, in its inactive form, exists as a monomer with low affinity for DNA. Upon exposure to stress, HSF1 undergoes a conformational change to form an active trimer that binds to heat shock elements (HSEs) in the promoters of heat shock genes, thereby inducing their transcription .

HSBP1 acts as a negative regulator of HSF1. It binds to the trimeric form of HSF1 and inhibits its DNA-binding activity, thereby modulating the heat shock response. Overexpression of HSBP1 in mammalian cells has been shown to repress the transactivation activity of HSF1, indicating its role in fine-tuning the cellular response to stress .

Biological Significance

The heat shock response is essential for cellular homeostasis and survival under stress conditions. HSBP1, by regulating HSF1 activity, ensures that the heat shock response is appropriately controlled. This regulation is crucial not only during stress but also in normal physiological conditions such as development, metabolism, and aging .

Recent studies have highlighted the broader role of HSF1 beyond the heat shock response. HSF1 is involved in various cellular processes, including metabolism, gametogenesis, and aging. Its dysregulation has been implicated in several pathologies, including cancer progression . Therefore, understanding the function and regulation of HSBP1 is important for comprehending the complex network of cellular stress responses and their implications in health and disease.

Recombinant HSBP1

Recombinant HSBP1 refers to the protein produced through recombinant DNA technology, which involves inserting the gene encoding HSBP1 into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities. This recombinant protein can be used in various research applications to study its function, interactions, and regulatory mechanisms.

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