Recombinant Proteins

p53
LBP
CEA
HLA
TCL
TTC
NPM
MAF
Bax
BID

AHA1 Human

Activator of HSP90 ATPase-1 Human Recombinant

This product consists of the recombinant human AHA1 protein, which has been produced in E. coli. It is a single polypeptide chain that is not glycosylated and comprises 320 amino acids (residues 19-337). The molecular weight of this protein is 36.1 kDa.
Shipped with Ice Packs
Cat. No.
BT14018
Source
Escherichia Coli.
Appearance
This product appears as a clear and colorless solution that has been sterilized by filtration.

DnaJ E.Coli

DnaJ (HSP40) E.Coli Recombinant

Recombinant DnaJ, produced in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 376 amino acids and has a molecular weight of 41.1 kDa.
Shipped with Ice Packs
Cat. No.
BT14092
Source
Escherichia Coli.
Appearance
A clear and sterile solution.

DnaK E.coli

DnaK (HSP70) E.Coli Recombinant

This recombinant DnaK protein, expressed in E. coli, is a single polypeptide chain consisting of 638 amino acids. It is non-glycosylated and has a molecular weight of 69 kDa.
Shipped with Ice Packs
Cat. No.
BT15341
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

DnaK Human, His

DnaK Human Recombinant, His Tag

Recombinant human HSP70, expressed in E. coli, is a monomeric, non-glycosylated polypeptide chain encompassing amino acids 1-641. It includes an N-terminal 20-amino acid His-tag, resulting in a molecular weight of 72.2 kDa.
Shipped with Ice Packs
Cat. No.
BT15396
Source
Escherichia Coli.
Appearance
The product is a clear, colorless, and sterile-filtered solution.

GroES Human

GroES (HSP10) Human Recombinant

Recombinant GroES, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 102 amino acids with a molecular weight of 10 kDa.
Shipped with Ice Packs
Cat. No.
BT16190
Source
Escherichia Coli.
Appearance
Sterile, colorless solution.

GroES Human, His

GroES (HSP10) Human Recombinant, His Tag

GroES His Protein is a 12.0 kDa protein consisting of the full-length 111 amino acid sequence of human GroES plus a 10 amino acid N-terminal His-tag.
Shipped with Ice Packs
Cat. No.
BT16268
Source
E. coli

GrpE E.Coli

HSP-70 Cofactor (HSP24) E.Coli Recombinant

Recombinant GrpE, produced in E. coli, is a single, non-glycosylated polypeptide chain composed of 197 amino acids. It has a molecular weight of 21.8 kDa. The purification of GrpE is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT16353
Source
Escherichia Coli.
Appearance
A sterile, colorless solution that has been filtered.

hchA E.Coli

Chaperone Protein hchA E.Coli Recombinant

Produced in E. coli, hchA is a single, non-glycosylated polypeptide chain consisting of 303 amino acids (with the actual protein sequence spanning from amino acid 1 to 283). It has a molecular weight of 33.3kDa. The protein is expressed with a 20 amino acid His-tag attached to its N-terminus for purification purposes, which is carried out using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT16439
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized through filtration.

DNAJB4 Human

DnaJ (Hsp40) Homolog, Subfamily B, Member 4 Human Recombinant

This product consists of a recombinant human DNAJB4 protein produced in E. coli. It is a single, non-glycosylated polypeptide chain comprising 360 amino acids (amino acids 1-337), resulting in a molecular weight of 40 kDa. The protein includes a 23 amino acid His-tag attached to the N-terminus. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT14769
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

DNAJB6 Human

DnaJ (Hsp40) Homolog, Subfamily B, Member 6 Human Recombinant

Recombinant human DNAJB6, fused with a 23 amino acid His tag at its N-terminus, is produced in E. coli. It is a single, non-glycosylated polypeptide chain that contains 349 amino acids (amino acids 1-326) and has a molecular weight of 38.5 kDa. The purification of DNAJB6 is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT14823
Source
Escherichia Coli.
Appearance
A sterile filtered solution that is colorless.
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 .

© Copyright 2024 Thebiotek. All Rights Reserved.