PSMA1 Human

Proteasome Subunit Alpha Type 1 Human Recombinant

Recombinant human PSMA1, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 286 amino acids (residues 1-263) with a molecular weight of 32.0 kDa. This protein is expressed with a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5039
Source
E.coli.
Appearance
A sterile, filtered solution without color.

PSMB2 Human

Proteasome Subunit Beta Type 2 Human Recombinant

Recombinant human PSMB2, produced in E. coli, is a single, non-glycosylated polypeptide chain composed of 221 amino acids (residues 1-201), resulting in a molecular weight of 24.9 kDa. The protein features a 20-amino acid His-tag fused to its N-terminus and undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5845
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

PSMB3 Human

Proteasome Subunit Beta Type 3 Human Recombinant

Recombinantly produced in E. coli, PSMB3 Human is a single, non-glycosylated polypeptide chain comprising 225 amino acids (specifically, residues 1 to 205) and exhibiting a molecular mass of 25.1 kDa. This protein is engineered with a 20 amino acid His-tag fused to its N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5933
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.

PSMB8 Human

Proteasome Subunit Beta Type 8 Human Recombinant

Recombinant human PSMB8 protein was expressed in E. coli and purified to yield a single, non-glycosylated polypeptide chain. The protein contains 229 amino acids (residues 73-276) and has a molecular weight of 25.4 kDa. For purification and detection purposes, a 25 amino acid His-tag is present at the N-terminus.
Shipped with Ice Packs
Cat. No.
BT6951
Source
Escherichia Coli.
Appearance
Clear, colorless and sterile-filtered solution.

PSMB9 Human

Proteasome Subunit Beta Type 9 Human Recombinant

PSMB9, expressed in E. coli, is a single, non-glycosylated polypeptide chain containing 220 amino acids (amino acids 21-219). This protein has a molecular weight of 23.5 kDa. PSMB9 is fused to a 21 amino acid His-tag at its N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7049
Source
Escherichia Coli.
Appearance
Sterile filtered solution, colorless.

PSMD10 Human

Gankyrin Human Recombinant

Recombinant human PSMD10, produced in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 226 amino acids, resulting in a molecular weight of 24.4 kDa.
Shipped with Ice Packs
Cat. No.
BT7110
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

PSMD11 Human

Proteasome 26S Subunit, Non-ATPase 11 Human Recombinant

Recombinant human PSMD11, expressed in E.coli, is a single, non-glycosylated polypeptide chain. It consists of 442 amino acids (1-422a.a), resulting in a molecular weight of 49.6kDa. The protein includes a 20 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7176
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized by filtration.

PSMD13 Human

Proteasome 26S Subunit, Non-ATPase 13 Human Recombinant

Recombinant human PSMD13, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 399 amino acids (residues 1-376) and has a molecular weight of 45.3 kDa. This protein includes a 23 amino acid His-tag fused to the N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT7273
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

PSMA6 Human

Proteasome Subunit Alpha Type 6 Human Recombinant

Recombinant human PSMA6, expressed in E. coli, is a single, non-glycosylated polypeptide chain with a molecular weight of 29.9 kDa. It comprises 270 amino acids, including a 24 amino acid His-tag fused to the N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5411
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

PSMA8 Human

Proteasome Subunit Alpha Type 8 Human Recombinant

Recombinant PSMA8 Human, produced in E.coli, is a single, non-glycosylated polypeptide chain consisting of 270 amino acids (residues 1-250) with a molecular weight of 30kDa. This protein is fused to a 20 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5607
Source
E.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 .

© Copyright 2024 Thebiotek. All Rights Reserved.