Recombinant Proteins
Product List
HSPB8 Human, His
Heat Shock 22kDa Protein 8 Human Recombinant, His Tag
HSPB9 Human
Heat Shock Protein B9 Human Recombinant
HSPB9 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
HSPBAP1 Human
HSPB Associated Protein 1 Human Recombinant
The HSPBAP1 is purified by proprietary chromatographic techniques.
HSPBP1 Human
Heat Shock Protein-Binding Protein 1 Human Recombinant
HSPH1 Human
Heat Shock Protein 105 Human Recombinant
SERPINH1 Human
Heat Shock 47kDa Human Recombinant
Recombinant Human HSP47 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 439 amino acids (18-418 a.a.) and having a molecular mass of 48.9 kDa. HSP47 human recombinant is fused to a 38 amino acid His Tag at N-terminus and purified by convential chromatogrpahy techniques.
SKP E. Coli
Chaperone Protein SKP E.Coli Recombinant
ST13 Human
HSP70 Interacting Protein Human Recombinant
ST13 human recombinant is purified by conventional chromatography techniques.
STUB1 Human
STIP1 Homology and U-Box Containing Protein 1 Human Recombinant
STUB1 is expressed and purified by proprietary chromatographic techniques.
AHA1 Human
Activator of HSP90 ATPase-1 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 .
