Recombinant Proteins

p53
LBP
CEA
HLA
TCL
TTC
NPM
MAF
Bax
BID

UBLCP1 Human

Ubiquitin-Like Domain Containing CTD Phosphatase 1 Human Recombinant

UBLCP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 341 amino acids (1-318 a.a) and having a molecular mass of 39.2kDa.
UBLCP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22889
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

UBQLN2 Human

Ubiquilin 2 Human Recombinant

UBQLN2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 647 amino acids (1-624 a.a) and having a molecular mass of 68.1kDa. UBQLN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22977
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

UFM1 Human

Ubiquitin-Fold Modifier 1 Human Recombinant

UFM1 Human Recombinant fused with a20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing103 amino acids (1-83 a.a) and having a molecular mass of 11.1kDa. The UFM1 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23053
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

URM1 Human

Ubiquitin Related Modifier 1 Human Recombinant

URM1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 121 amino acids (1-101 a.a.) and having a molecular mass of 13.5kDa.
URM1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23131
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

USP14 Human

Ubiquitin Specific Peptidase 14 Human Recombinant

USP14 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 517 amino acids (1-494 a.a) and having a molecular mass of 58.5kDa. USP14 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23268
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

USP15 Human

Ubiquitin Specific Peptidase 15 Human Recombinant

USP15 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 258 amino acids (1-235) and having a molecular mass of 29.5kDa.
USP15 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23332
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

USP46 Human

Ubiquitin Specific Peptidase 46 Human Recombinant

USP46 Human Recombinant produced in E. coli is. a single polypeptide chain containing 389 amino acids (1-366) and having a molecular mass of 44.8kDa. USP46 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23395
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

SUMO2 Human

Small Ubiquitin-Related Modifier 2 Human Recombinant

SUMO2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 93 amino acids and having a molecular mass of 10.6 kDa.
The SUMO-2 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21928
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

SUMO3 Human

Small Ubiquitin-Related Modifier 3 Human Recombinant

SUMO3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 112 amino acids (1-92a.a.) and having a molecular mass of 12.6kDa (molecular weight on SDS-PAGE will appear higher).
SUMO3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22062
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

UBD Human

Ubiquitin-D Human Recombinant

UBD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-165 a.a.) and having a molecular mass of 20.9kDa.
UBD is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT22148
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless 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 .

© Copyright 2024 Thebiotek. All Rights Reserved.