Recombinant Proteins

p53
LBP
CEA
HLA
TCL
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NPM
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HSF1 Human

Heat Shock Transcription Factor-1 Human Recombinant

Recombinant Human HSF1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing a total of 549 amino acids (1-529) and having a molecular mass of 59.4kDa.
The HSF1 protein is fused to a 20 aa His-Tag at N-terminus.
Shipped with Ice Packs
Cat. No.
BT16676
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

HSF2BP Human

Heat Shock Transcription Factor 2 Binding Protein Human Recombinant

HSF2BP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 357 amino acids (1-334 a.a) and having a molecular mass of 40kDa.
HSF2BP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT16761
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

HSFY1 Human

Heat Shock Transcription Factor, Y-Linked 1 Human Recombinant

HSFY1 Human Recombinant produced in E. coli is a single polypeptide chain containing 424 amino acids
(1-401) and having a molecular mass of 47.5kDa.
HSFY1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT16845
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

HSP104 Saccharomyces

Heat Shock Protein 104 Saccharomyces cerevisiae Recombinant

Recombinant HSP104 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 908 amino acids and having a molecular mass of 102 kDa.
Shipped with Ice Packs
Cat. No.
BT16948
Source
Saccharomyces cerevisiae.
Appearance
Sterile filtered colorless solution.

HSP20 Human

Heat Shock Protein 20 Human Recombinant

Heat Shock Protein 20 Human Recombinant produced in E.Coli.
Shipped with Ice Packs
Cat. No.
BT17020
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

HSP27 Human

Heat Shock Protein 27 Human Recombinant

Recombinant Human HSP-27 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 205 amino acids and having a molecular mass of 22.7 kDa. Hsp27 was over-expressed in E. coli and purified by conventional chromatography.
Shipped with Ice Packs
Cat. No.
BT17097
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.
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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