Recombinant Proteins

p53
LBP
CEA
HLA
TCL
TTC
NPM
MAF
Bax
BID

PFDN1 Human

Prefoldin Subunit 1 Human Recombinant

PFDN1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 130 amino acids (14-122 a.a.) and having a molecular mass of 15kDa. The PFDN1 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5626
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

PFDN2 Human

Prefoldin Subunit 2 Human Recombinant

PFDN2 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 174 amino acids (1-154 a.a.) and having a molecular mass of 18.8kDa. The PFDN2 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5685
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

PFDN4 Human

Prefoldin Subunit 4 Recombinant Human

PFDN4 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 154 amino acids (1-134.a.a) and having a molecular mass of 17.4kDa.
PFDN4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5841
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

PFDN5 Human

Prefoldin Subunit 5 Human Recombinant

PFDN5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 174 amino acids (1-154 a.a.) and having a molecular mass of 19.5kDa.
PFDN5 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5886
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

PFDN6 Human

Prefoldin Subunit 6 Human Recombinant

PFDN6 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 149 amino acids (1-129a.a.) and having a molecular mass of 16.7 kDa.
PFDN6 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6141
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

VBP1 Human

Von Hippel-Lindau Binding Protein 1 Human Recombinant

VBP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (1-197 a.a) and having a molecular mass of 25kDa.
VBP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6196
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.
Definition and Classification

Prefoldin is a heterohexameric molecular chaperone found in both archaea and eukaryotes, including humans . It is composed of six subunits, typically two alpha and four beta subunits . Prefoldin functions as a co-chaperone, working in conjunction with chaperonins to assist in the proper folding of nascent proteins .

Biological Properties

Key Biological Properties: Prefoldin is essential for the correct folding of cytoskeletal proteins such as actin and tubulin . It operates in an ATP-independent manner, making it suitable for functioning under stress conditions .

Expression Patterns and Tissue Distribution: Prefoldin is ubiquitously expressed in various tissues, with significant roles in maintaining protein homeostasis . Its subunits are differentially expressed, and their levels can be influenced by cellular stress and other conditions .

Biological Functions

Primary Biological Functions: Prefoldin primarily assists in the folding of newly synthesized polypeptides, preventing their aggregation and ensuring proper protein function . It plays a crucial role in maintaining cellular protein homeostasis .

Role in Immune Responses and Pathogen Recognition: While prefoldin’s direct role in immune responses and pathogen recognition is not well-documented, its function in protein homeostasis indirectly supports immune cell function by ensuring the proper folding and function of immune-related proteins .

Modes of Action

Mechanisms with Other Molecules and Cells: Prefoldin binds to nascent, unfolded proteins and transports them to chaperonins for proper folding . It specifically interacts with the cytosolic chaperonin TCP-1 ring complex (TRiC)/chaperonin containing TCP-1 (CCT) to facilitate the folding of actin and tubulin .

Binding Partners and Downstream Signaling Cascades: Prefoldin forms complexes with other proteins to protect them from degradation and assist in their proper folding . It does not directly participate in downstream signaling cascades but supports the stability and function of proteins involved in these pathways .

Regulatory Mechanisms

Regulatory Mechanisms Controlling Expression and Activity: The expression of prefoldin subunits is regulated at the transcriptional level and can be influenced by cellular stress . Post-translational modifications, such as ubiquitination, also play a role in regulating the stability and activity of prefoldin subunits .

Transcriptional Regulation and Post-Translational Modifications: Prefoldin subunits can be protected from ubiquitin-mediated degradation by forming complexes with other subunits . This regulation ensures the proper balance and function of prefoldin within the cell .

Applications

In Biomedical Research: Prefoldin is studied for its role in protein folding and its implications in diseases caused by protein misfolding, such as neurodegenerative diseases .

Diagnostic Tools and Therapeutic Strategies: Abnormal expression of prefoldin subunits has been linked to various tumors, making it a potential biomarker for cancer diagnosis and prognosis . Its role in maintaining protein homeostasis also makes it a target for therapeutic strategies aimed at treating diseases related to protein misfolding .

Role in the Life Cycle

Throughout Development to Aging and Disease: Prefoldin is crucial throughout the life cycle, from development to aging . It ensures the proper folding and function of proteins necessary for cellular growth, differentiation, and maintenance . Dysregulation of prefoldin function can lead to diseases such as neurodegenerative disorders and cancer .

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