Recombinant Proteins

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USP15 Human

Ubiquitin Specific Peptidase 15 Human Recombinant

Recombinant human USP15, expressed in E.coli, is a single, non-glycosylated polypeptide chain. It consists of 258 amino acids (residues 1-235) and has a molecular weight of 29.5 kDa. This protein includes a 23 amino acid His-tag fused at the N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23332
Source
Escherichia Coli.
Appearance
The product appears as a clear, colorless solution that has been sterilized by filtration.

USP46 Human

Ubiquitin Specific Peptidase 46 Human Recombinant

Recombinant human USP46 protein has been produced in E. coli. The protein consists of a single polypeptide chain of 389 amino acids, encompassing residues 1 to 366 of the USP46 sequence, with a molecular weight of 44.8 kDa. A 23-amino acid His-tag is fused to the N-terminus of the protein to facilitate purification using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT23395
Source
Escherichia Coli.
Appearance
Clear solution that has been sterilized by filtration.
Definition and Classification

Ubiquitin is a small regulatory protein, approximately 8.6 kDa in size, found ubiquitously in eukaryotic cells . It consists of 76 amino acids and is highly conserved across species . Ubiquitin is encoded by four genes in the human genome: UBB, UBC, UBA52, and RPS27A . The primary function of ubiquitin is to tag proteins for degradation via the proteasome, a process known as ubiquitination .

Biological Properties

Key Biological Properties: Ubiquitin is a globular protein that is highly stable and resistant to denaturation . It can withstand a wide range of pH and temperatures .

Expression Patterns: Ubiquitin is expressed in all eukaryotic cells and is involved in various cellular processes .

Tissue Distribution: Ubiquitin is found in the cell-surface membrane, cytoplasm, and nucleus of eukaryotic cells .

Biological Functions

Primary Biological Functions: The main function of ubiquitin is to label improperly folded, unwanted, or damaged proteins for proteasomal degradation . It also plays a role in altering the cellular location, structural conformation, or biological function of target proteins .

Role in Immune Responses and Pathogen Recognition: Ubiquitin is involved in the regulation of immune responses and pathogen recognition by modulating the activity of immune-related proteins .

Modes of Action

Ubiquitin exerts its effects through a process called ubiquitination, which involves three main steps: activation, conjugation, and ligation . These steps are performed by ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s), and ubiquitin ligases (E3s), respectively . Ubiquitin can mark proteins for degradation, alter their cellular location, affect their activity, and promote or prevent protein interactions .

Regulatory Mechanisms

Transcriptional Regulation: The expression of ubiquitin is tightly regulated at the transcriptional level to ensure proper cellular function .

Post-Translational Modifications: Ubiquitin itself can undergo various post-translational modifications, such as phosphorylation, which can affect its function and interactions with other proteins .

Applications

Biomedical Research: Ubiquitin is widely used in biomedical research to study protein degradation, signal transduction, and other cellular processes .

Diagnostic Tools: Ubiquitin-based assays are used to detect and quantify protein ubiquitination in various diseases .

Therapeutic Strategies: Targeting the ubiquitin-proteasome system has been explored as a therapeutic strategy for treating cancer and other diseases .

Role in the Life Cycle

Ubiquitin plays a crucial role throughout the life cycle, from development to aging and disease . During cell growth and proliferation, ubiquitin-mediated degradation is essential for maintaining genome integrity and ensuring proper cell cycle progression . Dysregulation of ubiquitin pathways can lead to various diseases, including cancer .

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