Recombinant Proteins

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HSPB11 Human

Heat Shock Protein Family B Member 11 Human Recombinant

Produced in E. coli, this non-glycosylated HSPB11 protein is a single polypeptide chain with a molecular weight of 18.5 kDa (appears larger on SDS-PAGE). The 164 amino acid sequence includes amino acids 1-144 of the HSPB11 protein and a 20 amino acid His-tag fused at the N-terminus. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18362
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

HSPB2 Human

Heat Shock 27kDa Protein 2 Human Recombinant

Recombinant HSPB2 Human, produced in E. coli, is a single polypeptide chain of 206 amino acids (1-182) with a molecular weight of 22.8kDa. It consists of amino acids 1-182 of HSPB2 fused to a 24 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18452
Source
E.coli.
Appearance
Clear, colorless, and sterile-filtered solution.

HSPB3 Human

Heat Shock 27kDa Protein 3 Human Recombinant

Recombinantly produced in E. coli, HSPB3 Human Recombinant is a single, non-glycosylated polypeptide chain consisting of 170 amino acids (residues 1-150) and possessing a molecular weight of 19.1 kDa. For purification purposes, a 20 amino acid His-Tag is fused to the N-terminus of HSPB3, and proprietary chromatographic techniques are employed.
Shipped with Ice Packs
Cat. No.
BT18516
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

HSPB6 Human

Heat Shock 27kDa Protein 6 Human Recombinant

Recombinant human HSPB6 protein was produced in E. coli. It is a single, non-glycosylated polypeptide chain containing 184 amino acids (residues 1-160) with a molecular mass of 19.7 kDa. The protein is fused to a 24 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18591
Source
Escherichia Coli.
Appearance
A sterile, colorless solution.

HSPB7 Human

Heat Shock 27kDa Protein Family, Member 7 Human Recombinant

Recombinant HSPB7 Human protein, expressed in E. coli, is a non-glycosylated polypeptide chain comprising 190 amino acids (specifically, residues 1-170) with a molecular weight of 20.7 kDa. This protein is engineered with a 20 amino acid His-Tag fused at its N-terminus to facilitate purification via standard chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT18643
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

HSP104 Saccharomyces

Heat Shock Protein 104 Saccharomyces cerevisiae Recombinant

Recombinant HSP104, expressed in E. coli, is a single, non-glycosylated polypeptide chain composed of 908 amino acids with a molecular weight of 102 kDa.
Shipped with Ice Packs
Cat. No.
BT16948
Source
Saccharomyces cerevisiae.
Appearance
A clear, colorless solution, sterile-filtered.

HSP20 Human

Heat Shock Protein 20 Human Recombinant

Recombinant Human Heat Shock Protein 20 produced in E. coli.
Shipped with Ice Packs
Cat. No.
BT17020
Source
Escherichia Coli.
Appearance
Sterile white lyophilized powder.

HSP27 Human

Heat Shock Protein 27 Human Recombinant

Recombinant Human HSP-27, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 205 amino acids. It has a molecular weight of 22.7 kDa. The protein was overexpressed in E. coli and purified using standard chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT17097
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile solution.

HSP90 Alpha Human

Heat Shock Protein-90 Alpha Human Recombinant

This recombinant human HSP90 protein is produced in E. coli. It is a single, non-glycosylated polypeptide chain with a molecular weight of 86.8 kDa. The protein consists of 752 amino acids (aa 1-732), including a 20 amino acid His tag at the N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT17412
Source
Escherichia Coli.
Appearance
Sterile, colorless solution.

HSP90B1 Human

Heat Shock Protein 90kDa Beta (GRP94) Member 1 Human Recombinant

This product consists of the recombinant human HSP90B1 protein, produced in E. coli. The protein sequence spans amino acids 22 to 803, excluding the signal peptide, and includes a 36-amino acid Histidine tag at the N-terminus for purification purposes. The final product is a single, non-glycosylated polypeptide chain with a molecular weight of 94.4 kDa. Purification is achieved using proprietary chromatographic methods, resulting in a highly pure protein suitable for various research applications.
Shipped with Ice Packs
Cat. No.
BT17500
Source
Escherichia Coli.
Appearance
The product is a clear and colorless solution after sterile filtration.
Definition and Classification

Heat shock proteins (HSPs) are a family of proteins produced by cells in response to stressful conditions such as heat, cold, UV light, and other environmental stressors . They function primarily as molecular chaperones, stabilizing new proteins to ensure correct folding or helping to refold proteins that were damaged by cell stress . HSPs are classified based on their molecular weight, with major families including HSP100, HSP90, HSP70, HSP60, and small HSPs .

Biological Properties

Key Biological Properties: HSPs are highly conserved across species, indicating their essential role in cellular function . They are involved in protein folding, preventing aggregation, and assisting in the degradation of misfolded proteins .

Expression Patterns: HSPs are expressed constitutively at low levels under normal conditions but are significantly upregulated in response to stress .

Tissue Distribution: HSPs are ubiquitously present in all tissues, with higher expression in tissues exposed to frequent stress, such as the brain, heart, and muscles .

Biological Functions

Primary Biological Functions: HSPs act as molecular chaperones, aiding in the proper folding of nascent proteins, refolding of misfolded proteins, and preventing protein aggregation . They also play a role in protein trafficking and complex assembly/disassembly .

Role in Immune Responses: HSPs are involved in the immune response by presenting peptides to the immune system, thus aiding in pathogen recognition . They can also modulate the activity of immune cells, enhancing the body’s ability to fight infections .

Modes of Action

HSPs interact with other molecules and cells through their chaperone activity, binding to nascent or misfolded proteins to prevent aggregation and assist in proper folding . They also participate in downstream signaling cascades by stabilizing key signaling proteins and receptors . For example, HSP90 is known to regulate several signal-transduction pathways by stabilizing client proteins involved in these pathways .

Regulatory Mechanisms

Transcriptional Regulation: The expression of HSPs is primarily regulated by heat shock factors (HSFs), which bind to heat shock elements (HSEs) in the promoter regions of HSP genes . Under stress conditions, HSFs are activated and induce the transcription of HSPs .

Post-Translational Modifications: HSPs undergo various post-translational modifications, such as phosphorylation, acetylation, and ubiquitination, which can affect their activity, stability, and interactions with other proteins .

Applications

Biomedical Research: HSPs are extensively studied in biomedical research for their role in protein homeostasis and stress response .

Diagnostic Tools: Elevated levels of HSPs can serve as biomarkers for various diseases, including cancer and neurodegenerative disorders .

Therapeutic Strategies: HSPs are targeted in therapeutic strategies to treat diseases such as cancer, where they help protect cancer cells from stress-induced apoptosis . Inhibitors of HSPs are being developed to enhance the efficacy of cancer treatments .

Role in the Life Cycle

HSPs play crucial roles throughout the life cycle, from development to aging and disease . During development, they assist in the proper folding and assembly of proteins essential for growth . In aging, HSPs help maintain protein homeostasis and protect against age-related diseases by preventing protein aggregation and promoting the degradation of damaged proteins . In disease, HSPs are involved in the cellular response to stress and can influence the progression of various conditions, including cancer and neurodegenerative diseases .

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