Recombinant Proteins
Product List
HSP27 Human, His
Heat Shock Protein 27 Human Recombinant, His Tag
HSP27 Mouse
Heat Shock Protein 27 Mouse Recombinant
HSP27 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (1-209 a.a) and having a molecular mass of 25.4kDa. HSP27 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
HSP90 Alpha Human
Heat Shock Protein-90 Alpha Human Recombinant
HSP90B1 Human
Heat Shock Protein 90kDa Beta (GRP94) Member 1 Human Recombinant
HSP90B1 is expressed with a 36 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
HSP90B1 Human, HEK
Heat Shock Protein 90kDa Beta (GRP94) Member 1 Human Recombinant, HEK
HSPA13 Human
Heat shock 70kDa protein 13 Human Recombinant
HSPA13 is fused to a 40 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
HSPA1B Human
Heat Shock 70kDa protein 1B Human Recombinant
HSPA1B is fused to a 10 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Filtered White lyophilized (freeze-dried) powder.
HSPA5 Mouse
Heat Shock 70kDa protein 5 Recombinant Mouse
HSPA5 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 659 amino acids (20-655 a.a) and having a molecular mass of 72.9kDa. HSPA5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
HSPA5 (19-654) Human
Heat Shock 70kDa protein 5 (19-654 a.a.) Human Recombinant
HSPA5 (19-654) is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
HSPA5 Human
Heat Shock 70kDa Protein 5 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 .
