Recombinant Proteins

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HSPH1 Human

Heat Shock Protein 105 Human Recombinant

Recombinant HSPH1, expressed in E.Coli, is a single, non-glycosylated polypeptide chain comprising 894 amino acids. With a molecular weight of 100.9kDa, HSP105 Alpha is engineered to include a 36 amino acid His tag and is purified using standard chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19132
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

SERPINH1 Human

Heat Shock 47kDa Human Recombinant

Recombinant Human HSP47, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 439 amino acids (residues 18-418). With a molecular weight of 48.9 kDa, this recombinant protein is fused to a 38 amino acid His Tag at its N-terminus and purified using standard chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19231
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

SKP E. Coli

Chaperone Protein SKP E.Coli Recombinant

Recombinant E. coli-produced SKP is a single, non-glycosylated polypeptide chain consisting of 162 amino acids (specifically, residues 21-161). With a molecular weight of 17.9 kDa, the SKP protein is fused to a 21 amino acid His-Tag at its N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19317
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

ST13 Human

HSP70 Interacting Protein Human Recombinant

Recombinant Human ST13, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 369 amino acids (specifically, amino acids 12 to 369), resulting in a molecular weight of 41.3 kDa. The purification of recombinant human ST13 is achieved through standard chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT19395
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

STUB1 Human

STIP1 Homology and U-Box Containing Protein 1 Human Recombinant

Recombinant human STUB1, expressed in E. coli, is a non-glycosylated polypeptide chain consisting of 303 amino acids. With a molecular weight of 34.8 kDa, it is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19460
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

DnaJ Human

DnaJ (HSP40) Human Recombinant

DnaJ Human Recombinant protein is produced in E.Coli. It is a single, non-glycosylated polypeptide chain containing amino acids 1-340 and fused to a 20 aa His tag at the N-terminus, resulting in a total of 360 amino acids. The molecular mass of the protein is 40.2 kDa.
Purification of the DnaJ protein is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT14390
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

DNAJB11 Human

DnaJ (Hsp40) Homolog, Subfamily B, Member 11 Human Recombinant

Produced in E. coli, our DNAJB11 is a single, non-glycosylated polypeptide chain. It comprises 357 amino acids (specifically, residues 23 to 358) and has a molecular weight of 40.5 kDa. For purification, we've added a 21 amino acid His-tag at the N-terminus and employed proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT14643
Source
Escherichia Coli.
Appearance
The product is a sterile, filtered solution that is colorless.

DNAJB2 Human

DnaJ (Hsp40) homolog, subfamily B, member 2 Human Recombinant

Recombinant DNAJB2, of human origin, is produced in E. coli. This protein construct includes a 23 amino acid His tag at the N-terminus. It exists as a single, non-glycosylated polypeptide chain with a total of 300 amino acids (residues 1-277) and a molecular weight of 33kDa. Purification of DNAJB2 is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT14701
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

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 comprising amino acids 385-546. It consists of 163 amino acids and has a molecular weight of 17.7 kDa.
Shipped with Ice Packs
Cat. No.
BT15537
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

Dnak SBD C-terminus E.Coli

Dnak Substrate Binding Domain C-terminal E.Coli Recombinant

This product consists of the recombinant C-terminal DnaK Substrate Binding Domain, produced in E. coli. It is a single, non-glycosylated polypeptide chain composed of 255 amino acids, with a molecular weight of 27.7 kDa.
Shipped with Ice Packs
Cat. No.
BT15627
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.
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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