Recombinant Proteins
Product List
HSPA5 Human, Hi-5
Heat shock 70kDa protein 5 Human Recombinant, Hi-5
HSPA5 is fused to an 8 amino acid His Tag at C-Terminus and purified by proprietary chromatographic techniques.
HSPA6 Human
Heat Shock 70kDa Protein 6 Human Recombinant
HSPA6 human recombinant is fused to a 20 amino acid His Tag at N-terminus and purified by conventional chromatography techniques.
HSPA8 Human
Heat Shock 70kDa Protein-8 Human Recombinant
HSC70 human recombinant is fused to 20 amino acid His Tag at N-terminus and purified by convential chromatogrpahy techniques.
HSPA9 Human
Heat Shock 70kDa Protein 9 Human Recombinant
HSP9A is expressed with a 20 amino acid His tag fused at N-Terminus and purified by proprietary chromatographic techniques.
HSPB11 Human
Heat Shock Protein Family B Member 11 Human Recombinant
HSPB11 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 164 amino acids (1-144 a.a.) and having a molecular mass of 18.5kDa (Molecular weight on SDS-PAGE will appear higher).
HSPB11 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
HSPB2 Human
Heat Shock 27kDa Protein 2 Human Recombinant
HSPB2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
HSPB3 Human
Heat Shock 27kDa Protein 3 Human Recombinant
The HSPB3 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
HSPB6 Human
Heat Shock 27kDa Protein 6 Human Recombinant
HSPB7 Human
Heat Shock 27kDa Protein Family, Member 7 Human Recombinant
HSPB8 Human
Heat Shock Protein 22 kDa Protein-8 Human Recombinant
Introduction
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 .
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 .
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 .
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 .
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 .
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 .
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 .
