PSMG4 Human

Proteasome Assembly Chaperone 4 Human Recombinant

This product consists of the recombinant human PSMG4 protein, expressed in E. coli. It is a single, non-glycosylated polypeptide chain composed of 143 amino acids, with the first 123 amino acids corresponding to the native PSMG4 sequence. The protein has a molecular weight of 15.9 kDa. For purification and detection purposes, a 20 amino acid His-tag is fused to the N-terminus of the protein. The purification process utilizes proprietary chromatographic techniques to ensure high purity.
Shipped with Ice Packs
Cat. No.
BT7953
Source
E.coli.
Appearance
The product is a clear, colorless solution that has been sterilized through filtration.

PSMA2 Human

Proteasome Subunit Alpha Type 2 Human Recombinant

PSMA2 Human Recombinant, produced in E.Coli, is a single, non-glycosylated polypeptide chain. It consists of 254 amino acids (with the active protein spanning 1-234 a.a.) and has a molecular weight of 28kDa. A 20 amino acid His-tag is attached to the N-terminus of PSMA2, and it undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5119
Source
Escherichia Coli.
Appearance
A clear, sterile solution without any color.

PSMA3 Human

Proteasome Subunit Alpha Type 3 Human Recombinant

Recombinant human PSMA3, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 275 amino acids (residues 1-255) with a molecular weight of 30.6 kDa. This protein features a 20 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5214
Source
E.coli.
Appearance
Clear, colorless solution, sterile filtered.

PSMA4 Human

Proteasome Subunit Alpha Type 4 Human Recombinant

Recombinant human PSMA4, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 285 amino acids (residues 1-261), resulting in a molecular weight of 32 kDa. This protein is engineered with a 24 amino acid His-tag at the N-terminus and purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT5279
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

PSMA5 Human

Proteasome Subunit Alpha Type 5 Human Recombinant

Recombinant human PSMA5, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 277 amino acids (residues 1-241) with a molecular weight of 30.5 kDa. The protein features a 36 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5342
Source
E.coli.
Appearance
Clear, colorless solution, sterile-filtered.

PSMB10 Human

Proteasome Beta Type 10 Human Recombinant

Recombinant Human PSMB10, produced in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 255 amino acids (40-273 a.a.), has a molecular weight of 26.9 kDa, and includes a 21 amino acid His-tag at the N-terminus. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5793
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

PSMD5 Human

Proteasome 26S Subunit, Non-ATPase 5 Human Recombinant

Recombinant human PSMD5, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 529 amino acids (specifically, residues 1-504). With a molecular weight of 58.9 kDa, this protein is fused to a 25 amino acid His-tag at its N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7356
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

PSMD9 Human

Proteasome 26S Subunit, Non-ATPase 9 Human Recombinant

This product consists of the human PSMD9 protein, recombinantly produced in E. coli bacteria. It is a single polypeptide chain containing 246 amino acids, with a molecular weight of 27.1 kDa. This non-glycosylated protein is purified to a high degree and includes a 23 amino acid His-tag at the N-terminus for various applications.
Shipped with Ice Packs
Cat. No.
BT7415
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

PSME1 Human

Proteasome Activator Subunit 1 Human Recombinant

Produced in E. coli, our recombinant PSME1 is a single, non-glycosylated polypeptide chain consisting of 269 amino acids (1-249a.a.) with a molecular weight of 30.8 kDa. This protein features a 20 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7505
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

PSME2 Human

Proteasome Activator Subunit 2 Human Recombinant

Recombinant human PSME2, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 259 amino acids (residues 1-239). It has a molecular weight of 29.5 kDa. This protein includes a 20 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT7591
Source
E.coli.
Appearance
A clear, sterile 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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