Recombinant Proteins
Product List
DNAJC24 Human
DnaJ (Hsp40) Homolog, Subfamily C, Member 24 Human Recombinant
DNAJC27 Human
DnaJ (Hsp40) Homolog, Subfamily C, Member 27 Human Recombinant
DNAJC27 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
DnaK ATPase-BD E.Coli
DnaK ATPase Binding Domain E.Coli Recombinant
Recombinant DnaK Substrate Binding Domain produced in E.Coli is a single, non-glycosylated polypeptide chain containing 384 amino acids and having a molecular mass of 41.6 kDa.
DnaK E.coli
DnaK (HSP70) E.Coli Recombinant
DnaK Human, His
DnaK Human Recombinant, His Tag
DnaK Lid Covering Substrate E.Coli
DnaK Lid Covering Substrate E.Coli Recombinant
DnaK SBD
DnaK Substrate Binding Domain E.Coli Recombinant
Recombinant DnaK Substrate Binding domain produced in E.Coli is a single, non-glycosylated polypeptide chain containing (385-546 a.a.) 163 amino acids and having a molecular mass of 17.7 kDa.
Dnak SBD C-terminus E.Coli
Dnak Substrate Binding Domain C-terminal E.Coli Recombinant
DsbE E.Coli
Thiol Disulfide Interchange Protein E.Coli Recombinant DsbE
DsbE is purified by conventional chromatography techniques.
DsbG E.Coli
Thiol Disulfide Interchange Protein E.Coli Recombinant DsbG
DsbG is purified by conventional chromatography techniques.
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 .
