PSMB2 Human

Proteasome Subunit Beta Type 2 Human Recombinant

PSMB2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 221 amino acids (1-201) and having a molecular mass of 24.9kDa.
PSMB2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5845
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

PSMB3 Human

Proteasome Subunit Beta Type 3 Human Recombinant

PSMB3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids (1-205 a.a.) and having a molecular mass of 25.1kDa.
PSMB3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5933
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

PSMB4 Human

Proteasome Subunit Beta Type 4 Human Recombinant

PSMB4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 240 amino acids (46-264 a.a.) and having a molecular mass of 26.6kDa.
PSMB4 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6459
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

PSMB5 Human

Proteasome Subunit Beta Type 5 Human Recombinant

PSMB5 Human Recombinant fused with a 36 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 241 amino acids (60-263 a.a.) and having a molecular mass of 26.7kDa. The PSMB5 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6536
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

PSMB6 Human

Proteasome Subunit Beta Type 6 Human Recombinant

PSMB6 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 226 amino acids (35-239) and having a molecular mass of 24.2kDa.
PSMB6 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6677
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

PSMB7 Human

Proteasome Subunit Beta Type 7 Human Recombinant

PSMB7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 255 amino acids (44-277) and having a molecular mass of 27.6kDa (Molecular size on SDS-PAGE will appear higher).
PSMB7 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6866
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

PSMB8 Human

Proteasome Subunit Beta Type 8 Human Recombinant

PSMB8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 229 amino acids (73-276 a.a.) and having a molecular mass of 25.4kDa. PSMB8 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6951
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

PSMB9 Human

Proteasome Subunit Beta Type 9 Human Recombinant

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

PSMD10 Human

Gankyrin Human Recombinant

PSMD10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 226 amino acids and having a molecular mass of 24.4 kDa.
Shipped with Ice Packs
Cat. No.
BT7110
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

PSMD11 Human

Proteasome 26S Subunit, Non-ATPase 11 Human Recombinant

PSMD11 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 442 amino acids (1-422a.a) and having a molecular mass of 49.6kDa. PSMD11 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7176
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.
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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