PSMB1 Human

Proteasome Subunit Beta Type 1 Human Recombinant

Recombinant human PSMB1, with a 37 amino acid His Tag fused at its N-terminal, is produced in E. coli. This single, non-glycosylated polypeptide chain consists of 250 amino acids (30-241) and has a molecular weight of 27.7 kDa. Purification of PSMB1 is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5689
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

PSMB5 Human

Proteasome Subunit Beta Type 5 Human Recombinant

Recombinant human PSMB5, expressed in E. coli, is fused with a 36 amino acid His tag at its N-terminus. This single, non-glycosylated polypeptide chain comprises 241 amino acids (60-263 a.a.) and exhibits a molecular mass of 26.7 kDa. Purification of PSMB5 is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6536
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

PSMB6 Human

Proteasome Subunit Beta Type 6 Human Recombinant

Recombinantly produced in E.coli, PSMB6 Human Recombinant is a single, non-glycosylated polypeptide chain. This protein consists of 226 amino acids (residues 35-239) and has a molecular weight of 24.2 kDa. For purification purposes, PSMB6 is tagged with a 21 amino acid His-tag at its N-terminus and subsequently purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6677
Source
Escherichia Coli.
Appearance
The product is a sterile-filtered solution with a colorless appearance.

PSMA7 Human

Proteasome Subunit Alpha Type 7 Human Recombinant

PSMA7 Human Recombinant, tagged with N-terminal His-Tag, is produced in E. coli. This protein is a single, non-glycosylated polypeptide chain containing 268 amino acids (residues 1-248), with a molecular weight of 30 kDa. The recombinant PSMA7 is purified using standard chromatography techniques following its expression in E. coli.
Shipped with Ice Packs
Cat. No.
BT5505
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

PSMB4 Human

Proteasome Subunit Beta Type 4 Human Recombinant

Recombinant Human PSMB4, produced in E. coli, is a single, non-glycosylated polypeptide chain encompassing amino acids 46-264 (240 a.a.) and possessing a molecular weight of 26.6 kDa. This protein is expressed with an N-terminal 21 amino acid His-tag and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6459
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

PSMB7 Human

Proteasome Subunit Beta Type 7 Human Recombinant

Recombinant human PSMB7 protein has been expressed in E. coli bacteria and purified to a high degree. This protein represents a single polypeptide chain of 255 amino acids, encompassing amino acids 44 to 277 of the full-length PSMB7 protein. It has a molecular weight of 27.6 kDa, but may appear larger on SDS-PAGE due to the presence of a 21 amino acid His-tag at the N-terminus. This His-tag allows for easy purification using affinity chromatography techniques. This recombinant PSMB7 protein is not glycosylated, meaning it lacks the sugar modifications typically found on proteins produced in eukaryotic cells.
Shipped with Ice Packs
Cat. No.
BT6866
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

PSME3 Human

Proteasome Activator Subunit 3 Human Recombinant

Recombinant human PSME3, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 274 amino acids, including a 20-amino acid His-tag at the N-terminus, resulting in a molecular weight of 31.7 kDa. The protein is purified using proprietary chromatographic techniques to ensure high purity.
Shipped with Ice Packs
Cat. No.
BT7655
Source
E.coli.
Appearance
Clear, colorless solution sterilized by filtration.

PSMF1 Human

Proteasome Inhibitor Subunit 1 Human Recombinant

Recombinant human PSMF1, expressed in E. coli, is a single-chain polypeptide that lacks glycosylation. It comprises 291 amino acids (residues 1-271) and has a molecular weight of 31.9 kDa. A 20-amino acid His-tag is fused to the N-terminus of PSMF1 to facilitate purification using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT7736
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

PSMG2 Human

Proteasome Assembly Chaperone 2 Human Recombinant

Recombinant human PSMG2, expressed in E. coli, is a non-glycosylated polypeptide chain. It comprises 287 amino acids, specifically encompassing amino acids 1 to 264, resulting in a molecular weight of 31.8 kDa. A 23 amino acid His-tag is fused to the N-terminus of PSMG2. The purification process involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7791
Source
Escherichia Coli.
Appearance
A clear and sterile solution.

PSMG3 Human

Proteasome Assembly Chaperone 3 Human Recombinant

Recombinant human PSMG3, expressed in E. coli, is a purified protein with a 20 amino acid His tag at the N-terminus. This single, non-glycosylated polypeptide chain consists of 142 amino acids (residues 1-122), resulting in a molecular weight of 15.2kDa. Purification of PSMG3 is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7865
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile filtered.
Definition and Classification

Proteasomes are large protein complexes found in eukaryotic cells, archaea, and some bacteria. They are responsible for degrading unneeded or damaged proteins by proteolysis, a chemical reaction that breaks peptide bonds . Proteasomes are classified into two main types: the 20S core particle and the 26S proteasome, which includes the 20S core particle capped with regulatory particles .

Biological Properties

Key Biological Properties: Proteasomes are essential for maintaining cellular homeostasis by regulating the concentration of specific proteins and degrading misfolded proteins . They are involved in various cellular processes, including the cell cycle, gene expression regulation, and responses to oxidative stress .

Expression Patterns and Tissue Distribution: Proteasomes are ubiquitously expressed in all eukaryotic cells and are found in both the nucleus and cytoplasm . Their expression levels can vary depending on the cell type and physiological conditions .

Biological Functions

Primary Biological Functions: The primary function of proteasomes is to degrade ubiquitin-tagged proteins, thereby regulating protein turnover and quality control within the cell . This process is crucial for removing damaged or misfolded proteins and preventing their accumulation .

Role in Immune Responses and Pathogen Recognition: Proteasomes play a vital role in the immune system by generating peptide fragments presented on major histocompatibility complex (MHC) class I molecules, which are recognized by cytotoxic T cells . This process is essential for the immune system to identify and eliminate infected or malignant cells .

Modes of Action

Mechanisms with Other Molecules and Cells: Proteasomes interact with various molecules, including ubiquitin, which tags proteins for degradation . The 19S regulatory particle recognizes these ubiquitin-tagged proteins and directs them to the 20S core particle for degradation .

Binding Partners and Downstream Signaling Cascades: Proteasomes are involved in multiple signaling pathways by degrading key regulatory proteins, such as transcription factors and cyclins . This degradation process can activate or inhibit downstream signaling cascades, thereby influencing various cellular functions .

Regulatory Mechanisms

Regulatory Mechanisms Controlling Expression and Activity: Proteasome activity is tightly regulated at multiple levels, including transcriptional regulation, post-translational modifications, and changes in complex composition . For example, the expression of proteasome subunits can be upregulated in response to cellular stress .

Transcriptional Regulation and Post-Translational Modifications: Proteasome subunits are regulated at the transcriptional level by various transcription factors . Additionally, post-translational modifications, such as phosphorylation and ubiquitination, can modulate proteasome activity and stability .

Applications

Biomedical Research: Proteasomes are extensively studied in biomedical research for their role in protein homeostasis and disease pathogenesis . They are used as models to understand protein degradation mechanisms and develop therapeutic strategies .

Diagnostic Tools and Therapeutic Strategies: Proteasome inhibitors, such as bortezomib, are used as therapeutic agents in treating multiple myeloma and other cancers . These inhibitors block proteasome activity, leading to the accumulation of toxic proteins and inducing cell death in cancer cells .

Role in the Life Cycle

Role Throughout the Life Cycle: Proteasomes are involved in various stages of the life cycle, from development to aging and disease . During development, they regulate the degradation of key proteins involved in cell differentiation and growth . In aging, proteasome activity declines, leading to the accumulation of damaged proteins and contributing to age-related diseases .

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