Recombinant Proteins

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Ubiquitin G76A Human

Ubiquitin G76A Human Recombinant

This product contains recombinant human ubiquitin with a glycine-to-alanine mutation at position 76 (G76A). This mutation inhibits ubiquitin hydrolases, effectively preventing the removal of ubiquitin from conjugated proteins. The ubiquitin G76A protein is produced in E. coli and purified using ion-exchange chromatography.
Shipped with Ice Packs
Cat. No.
BT22221
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

Ubiquitin K48R Human

Ubiquitin K48R Human Recombinant

Recombinant human ubiquitin K48R is designed to limit polyubiquitin chain formation and reduce conjugation rates. By substituting Lys48 with Arg48, this variant alters the ubiquitination process. Produced in E.coli and purified using proprietary chromatographic methods, it offers high purity for research applications.
Shipped with Ice Packs
Cat. No.
BT22299
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

UBL5 Human

Ubiquitin-Like 5 Human Recombinant

Recombinant Human UBL5, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 93 amino acids (1-73a.a) and has a molecular mass of 10.7 kDa. This UBL3 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.
BT22798
Source
Escherichia Coli.
Appearance
A clear, sterile filtered solution.

UBLCP1 Human

Ubiquitin-Like Domain Containing CTD Phosphatase 1 Human Recombinant

Recombinant human UBLCP1, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It encompasses amino acids 1-318, with an additional 23 amino acid His-tag at the N-terminus, resulting in a molecular weight of 39.2kDa. The protein has been purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22889
Source
Escherichia Coli.
Appearance
Clear solution, sterile filtered.

UBQLN2 Human

Ubiquilin 2 Human Recombinant

Recombinant UBQLN2 protein, produced in E. coli bacteria, is a purified protein consisting of a single polypeptide chain that is not glycosylated (does not contain sugar modifications). It encompasses 647 amino acids, representing amino acids 1 through 624 of the full-length human UBQLN2 protein. The recombinant protein has a molecular weight of 68.1 kDa and includes a 23-amino acid His-tag attached to its N-terminus. This His-tag facilitates purification using specialized chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22977
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

UFM1 Human

Ubiquitin-Fold Modifier 1 Human Recombinant

Recombinant human UFM1, with a 20 amino acid His tag at the N-terminus, is produced in E. coli. This non-glycosylated polypeptide chain consists of 103 amino acids (1-83 a.a), resulting in a molecular mass of 11.1 kDa. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23053
Source
Escherichia Coli.
Appearance
A sterile, colorless solution.

URM1 Human

Ubiquitin Related Modifier 1 Human Recombinant

The URM1 protein, expressed in E. coli, is a single polypeptide chain without any glycosylation. It consists of 121 amino acids, with amino acids 1 to 101 representing the URM1 sequence, resulting in a molecular weight of 13.5 kDa. A 20 amino acid His-tag is fused to the N-terminus of URM1 to facilitate purification, which is carried out using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT23131
Source
Escherichia Coli.
Appearance
The product is a clear, colorless solution that has been sterilized by filtration.

UBL3 Human

Ubiquitin-Like 3 Human Recombinant

Recombinant human UBL3, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 134 amino acids (residues 1-114) with a molecular weight of 15.0 kDa. The protein includes a 20 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22615
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

UBL4A Human

Ubiquitin-Like 4A Human Recombinant

Recombinant human UBL4A protein was produced in E. coli bacteria. This protein is a single chain with 165 amino acids (specifically amino acids 1 to 157 of the human UBL4A sequence) and a molecular weight of 18.8 kDa. It is not glycosylated, meaning it does not have sugars attached. For purification and detection purposes, the UBL4A protein has an 8 amino acid His-tag attached to its C-terminus. The protein was purified using proprietary chromatographic techniques to ensure high purity.
Shipped with Ice Packs
Cat. No.
BT22696
Source
Escherichia Coli.
Appearance
Clear and colorless solution that has been sterilized by filtration.

USP14 Human

Ubiquitin Specific Peptidase 14 Human Recombinant

Recombinant human USP14, expressed in E. coli, is a non-glycosylated polypeptide chain containing 494 amino acids (residues 1-494). This 58.5 kDa protein includes a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23268
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.
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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