Recombinant Proteins

p53
LBP
CEA
HLA
TCL
TTC
NPM
MAF
Bax
BID

ISG15 Human

ISG15 Human Recombinant

ISG15 Human Recombinant fused to N-terminal Calmudulin Tag (151 a.a.) produced in E.Coli is a single, non-glycosylated polypeptide chain containing a total of 308 amino acids (157 a.a. without tag) and having a molecular mass of 34 kDa.
Shipped with Ice Packs
Cat. No.
BT21309
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

OTUB1 Human

Ubiquitin Aldehyde Binding 1 Human Recombinant

OTUB1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 291 amino acids (1- 271 a.a.) and having a molecular mass of 33.4kDa.
The OTUB1 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21417
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

OTUB2 Human

Ubiquitin Aldehyde Binding 2 Human Recombinant

OTUB2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 254 amino acids (1-234 a.a.) and having a molecular mass of 29.4kDa.
OTUB2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21495
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

RPS27A Human

Ubiquitin Human Recombinant

Ubiquitin Human Recombinant expressed in E.coli and purified by ion-exchange chromatography, contains 76 amino acids and has an Mw of 8.6kDa.
Shipped with Ice Packs
Cat. No.
BT21599
Source
Escherichia Coli.
Appearance
Sterile Filtered solution.

RPS27A Human, Biotin

Ubiquitin Biotinylated Human Recombinant

Recombinant Human RPS27A protein biotinylated with NHS-biotin produced in E.Coli is a single, non-glycosylated polypeptide chain containing a total of 76 amino acids and having a molecular mass of 8.6 kDa.
Shipped with Ice Packs
Cat. No.
BT21691
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless liquid formulation.

SUMO1 Human

SUMO1 Human Recombinant

The active human SUMO-I (the 1-97 animo acid region of the Ubiquitin-like protein SMT3C precursor). The enzyme contains a single polypeptide band of 11 kDa. The predicted molecular weight of hSOMO I is 11 kDa. The The final fraction of enzyme contains single polypeptide band of approximately 20 kDa on SDS PAGE.
Shipped with Ice Packs
Cat. No.
BT21781
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

SUMO1 Human His

Small Ubiquitin-Related Modifier 1 Human Recombinant, His Tag

SUMO1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 109 amino acids (1-101) and having a molecular mass of 12.6 kDa.
SUMO1 is fused to a 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21851
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

UBL3 Human

Ubiquitin-Like 3 Human Recombinant

UBL3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 134 amino acids (1-114a.a) and having a molecular mass of 15.0kDa.
UBL3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22615
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

UBL4A Human

Ubiquitin-Like 4A Human Recombinant

UBL4A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (1-157 a.a.) and having a molecular mass of 18.8kDa.
UBL4A is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22696
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

UBL5 Human

Ubiquitin-Like 5 Human Recombinant

UBL5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 93 amino acids (1-73a.a) and having a molecular mass of 10.7kDa.
UBL3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22798
Source
Escherichia Coli.
Appearance
Sterile Filtered clear 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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