Recombinant Proteins

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DNAJB8 Human

DnaJ (Hsp40) Homolog, Subfamily B, Member 8 Human Recombinant

Recombinant Human DNAJB8, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 252 amino acids (specifically, residues 1-232) and has a molecular weight of 27.8 kDa. This protein is engineered with a 20 amino acid His-tag fused to its N-terminus. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT14869
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

DNAJC12 Human

DnaJ (Hsp40) Homolog, Subfamily C, Member 12 Human Recombinant

This product is a recombinant human DNAJC12 protein produced in E. coli. It is a single polypeptide chain consisting of 222 amino acids (residues 1-198) with a molecular weight of 26 kDa. Note that the molecular weight observed on SDS-PAGE may be higher. The protein includes a 24 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT14924
Source
E.coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

DNAJC15 Human

DnaJ (Hsp40) Homolog, Subfamily C, Member 15 Human Recombinant

This product consists of the human DNAJC15 protein, manufactured in a lab using E. coli bacteria. It's a single chain of amino acids (the building blocks of proteins), with a specific sequence that corresponds to a portion of the naturally occurring DNAJC15 protein. This engineered protein is not glycosylated, meaning it lacks certain sugar modifications. It includes a 23 amino acid tag (His-tag) attached to aid in purification. The final purified product comes in a solution with a concentration of 0.25mg/ml.
Shipped with Ice Packs
Cat. No.
BT14986
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

DNAJC19 Human

DnaJ (Hsp40) Homolog, Subfamily C, Member 19 Human Recombinant

Recombinant human DNAJC19, expressed in E. coli, is a non-glycosylated polypeptide chain containing amino acids 19-116 of the DNAJC19 protein. A 37 amino acid His tag is fused to the N-terminus. This protein has a molecular mass of 15.1 kDa. The purity of this protein is greater than 90% as determined by SDS-PAGE. This protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15055
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

DnaK Lid Covering Substrate E.Coli

DnaK Lid Covering Substrate E.Coli Recombinant

This product consists of the recombinant DnaK Lid Covering Substrate domain, produced in E. coli, and is a single, non-glycosylated polypeptide chain comprising 132 amino acids. It has a molecular weight of 14.6 kDa.
Shipped with Ice Packs
Cat. No.
BT15473
Source
Escherichia Coli.
Appearance
The product is a sterile, colorless solution that has been filtered for clarity.

DsbE E.Coli

Thiol Disulfide Interchange Protein E.Coli Recombinant DsbE

Recombinant DsbE, expressed in E. coli, is a single, non-glycosylated polypeptide chain with a molecular weight of 18.1 kDa, comprising 161 amino acids. The purification of DsbE is achieved using standard chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15701
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

DNAJC24 Human

DnaJ (Hsp40) Homolog, Subfamily C, Member 24 Human Recombinant

Recombinant DNAJC24 Human, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 172 amino acids (1-149 a.a.) with a molecular weight of 19.5 kDa. This protein is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15133
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

DNAJC27 Human

DnaJ (Hsp40) Homolog, Subfamily C, Member 27 Human Recombinant

This recombinant DNAJC27 protein is produced in E. coli bacteria and corresponds to amino acids 1-273 of the human protein sequence. It is a single, non-glycosylated polypeptide chain with a molecular weight of 33.2 kDa. For purification purposes, a 23 amino acid His-tag is fused to the N-terminus of the protein. Purification is achieved using proprietary chromatographic techniques. The resulting protein is greater than 90% pure.
Shipped with Ice Packs
Cat. No.
BT15196
Source
E.coli.
Appearance
Clear, colorless solution, sterile-filtered.

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 with a molecular weight of 41.6 kDa.
Shipped with Ice Packs
Cat. No.
BT15249
Source
Escherichia Coli.
Appearance
Sterile filtered, colorless solution.

GROEL (27-573) Human

GroEL (HSP60) (27-573 a.a.) Human Recombinant

Recombinant human GROEL, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 572 amino acids (specifically, amino acids 27-573). It has a molecular mass of 60 kDa. This GROEL protein is fused to a 25 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15881
Source
Escherichia Coli.
Appearance
A clear, sterile 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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