Recombinant Proteins

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PFDN4 Human

Prefoldin Subunit 4 Recombinant Human

Produced in E. coli, the recombinant PFDN4 protein is a single, non-glycosylated polypeptide chain consisting of 154 amino acids. The sequence encompasses amino acids 1 to 134, along with an N-terminal 20-amino acid His-tag. With a molecular weight of 17.4 kDa, PFDN4 undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5841
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized by filtration.

PFDN5 Human

Prefoldin Subunit 5 Human Recombinant

Recombinant Human PFDN5, produced in E. coli, is a single, non-glycosylated polypeptide chain. This protein consists of 174 amino acids, with amino acids 1-154 representing the PFDN5 sequence. The recombinant protein has a molecular mass of 19.5 kDa and includes a 20 amino acid His-tag fused at the N-terminus to facilitate purification by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5886
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

PFDN6 Human

Prefoldin Subunit 6 Human Recombinant

Recombinant PFDN6, expressed in E. coli, is a single, non-glycosylated polypeptide chain with a molecular weight of 16.7 kDa. This protein consists of 149 amino acids, including a 20 amino acid His-tag fused at the N-terminus. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6141
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

PFDN1 Human

Prefoldin Subunit 1 Human Recombinant

Recombinant human PFDN1, expressed in E. coli, is a non-glycosylated polypeptide chain with a His tag (20 amino acids) at its N-terminus. This protein, with a molecular weight of 15kDa, consists of 130 amino acids (residues 14-122). The purification process involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5626
Source
Escherichia Coli.
Appearance
A clear, colorless solution, sterilized by filtration.

PFDN2 Human

Prefoldin Subunit 2 Human Recombinant

Recombinant human PFDN2, expressed in E. coli, is a purified protein with a 20 amino acid His tag added to the N-terminus. This single, non-glycosylated polypeptide chain consists of 174 amino acids (residues 1-154), resulting in a molecular weight of 18.8 kDa. The purification process employs proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5685
Source
Escherichia Coli.
Appearance
A colorless solution that has been sterilized through filtration.

VBP1 Human

Von Hippel-Lindau Binding Protein 1 Human Recombinant

Recombinant human VBP1, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 220 amino acids (residues 1-197) and has a molecular weight of 25 kDa. The protein includes a 23-amino acid His-tag fused at the N-terminus. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6196
Source
Escherichia Coli.
Appearance
Sterile, 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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