Recombinant Proteins

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ISG15 Human

ISG15 Human Recombinant

ISG15 Human Recombinant protein, fused to an N-terminal Calmudulin Tag (151 a.a.) and produced in E. coli, is a single, non-glycosylated polypeptide chain. The total protein comprises 308 amino acids (157 a.a. without the tag) and has a molecular weight of 34 kDa.
Shipped with Ice Packs
Cat. No.
BT21309
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

OTUB1 Human

Ubiquitin Aldehyde Binding 1 Human Recombinant

Recombinant human OTUB1, expressed in E. coli, is a purified protein with a His-tag fused at its N-terminus. This non-glycosylated polypeptide chain consists of 291 amino acids (with the His-tag spanning residues 1-20 and the OTUB1 sequence from residues 21-291) and has a molecular weight of 33.4 kDa. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21417
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

OTUB2 Human

Ubiquitin Aldehyde Binding 2 Human Recombinant

The OTUB2 protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain with a molecular weight of 29.4 kDa. It comprises 254 amino acids, including a 20 amino acid His-tag at the N-terminus (1-234 a.a.). The protein undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21495
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

RPS27A Human

Ubiquitin Human Recombinant

This product consists of recombinant human Ubiquitin protein produced in E.coli. It has been purified using ion-exchange chromatography and contains 76 amino acids, resulting in a molecular weight of 8.6kDa.
Shipped with Ice Packs
Cat. No.
BT21599
Source
Escherichia Coli.
Appearance
Clear, sterile solution.

RPS27A Human, Biotin

Ubiquitin Biotinylated Human Recombinant

Recombinant Human RPS27A protein, biotinylated with NHS-biotin, is produced in E. coli. This single, non-glycosylated polypeptide chain consists of 76 amino acids and has a molecular weight of 8.6 kDa.
Shipped with Ice Packs
Cat. No.
BT21691
Source
Escherichia Coli.
Appearance
This product is a sterile-filtered, colorless liquid.

SUMO1 Human

SUMO1 Human Recombinant

This product contains the active form of human SUMO-I, specifically the amino acid region 1-97 of the Ubiquitin-like protein SMT3C precursor. The enzyme presents as a single polypeptide band at 11 kDa, consistent with its predicted molecular weight. The final enzyme fraction appears as a single polypeptide band at approximately 20 kDa on SDS-PAGE.
Shipped with Ice Packs
Cat. No.
BT21781
Source
Escherichia Coli.
Appearance
The product is a clear solution that has been sterilized through filtration.

SUMO1 Human His

Small Ubiquitin-Related Modifier 1 Human Recombinant, His Tag

Recombinant Human SUMO1, produced in E.coli, is a single, non-glycosylated polypeptide chain comprising 109 amino acids (1-101) with a molecular weight of 12.6 kDa. This SUMO1 variant is engineered with an 8 amino acid His-tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21851
Source
E.coli.
Appearance
A clear, colorless solution, sterilized by filtration.

SUMO2 Human

Small Ubiquitin-Related Modifier 2 Human Recombinant

Recombinant Human SUMO2 is a purified protein produced in E. coli bacteria. It is a single, non-glycosylated polypeptide chain containing 93 amino acids with a molecular weight of 10.6 kDa. The protein has been purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21928
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile solution.

SUMO3 Human

Small Ubiquitin-Related Modifier 3 Human Recombinant

Produced in E. coli, this SUMO3 protein is a single, non-glycosylated polypeptide chain consisting of 112 amino acids (1-92a.a.) with a molecular mass of 12.6kDa. Note that its molecular weight on SDS-PAGE will appear higher. This SUMO3 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.
BT22062
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

UBD Human

Ubiquitin-D Human Recombinant

Recombinant Human UBD, produced in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 188 amino acids (with amino acids 1-165 being of particular interest) and has a molecular weight of 20.9kDa. The UBD sequence is fused to a 23 amino acid His-tag at its N-terminus and is purified through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22148
Source
Escherichia Coli.
Appearance
A clear, sterile solution without any color.
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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