OTUB1 Human

Ubiquitin Aldehyde Binding 1 Human Recombinant
Cat. No.
BT21417
Source
Escherichia Coli.
Synonyms
Ubiquitin thioesterase OTUB1, Otubain-1, OTU domain-containing ubiquitin aldehyde-binding protein 1, Ubiquitin-specific-processing protease OTUB1, Deubiquitinating enzyme OTUB1, OTUB1, OTB1, OTU1, HSPC263, MGC4584, FLJ20113, FLJ40710, MGC111158.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

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.

Product Specs

Introduction
Otubain 1 (OTUB1), a member of the ovarian tumor (OUT) superfamily of putative cysteine proteases, plays a crucial role in regulating immune responses by suppressing cytokine gene transcription. This function is mediated through its interaction with a ubiquitin protease and an E3 ubiquitin ligase. OTUB1 exhibits high specificity as a ubiquitin isopeptidase, selectively cleaving ubiquitin from branched polyubiquitin chains while leaving ubiquitinated substrates untouched. Its precise mechanism of action suggests involvement in specific ubiquitin-dependent pathways, potentially by controlling polyubiquitin chain elongation. By removing conjugated ubiquitin from proteins in vitro, OTUB1 acts as a hydrolase, thereby potentially influencing protein turnover rates and preventing degradation. Furthermore, OTUB1 plays a critical role in T-cell anergy, a state of T-cell unresponsiveness to antigen re-challenge. This regulatory function is exerted through its interaction with RNF128/GRAIL, an indispensable factor for inducing CD4 T-cell anergy.
Description
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.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The OTUB1 protein is supplied in a solution containing 20 mM Tris buffer at pH 8.0 and 10% glycerol.
Stability
For short-term storage (up to 4 weeks), the OTUB1 solution should be kept at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is advisable for long-term storage. Repeated freezing and thawing should be avoided.
Purity
The purity of the OTUB1 protein is greater than 95%, as determined by SDS-PAGE analysis.
Synonyms
Ubiquitin thioesterase OTUB1, Otubain-1, OTU domain-containing ubiquitin aldehyde-binding protein 1, Ubiquitin-specific-processing protease OTUB1, Deubiquitinating enzyme OTUB1, OTUB1, OTB1, OTU1, HSPC263, MGC4584, FLJ20113, FLJ40710, MGC111158.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAAEEPQQQK QEPLGSDSEG VNCLAYDEAI MAQQDRIQQE IAVQNPLVSE RLELSVLYKE YAEDDNIYQQ KIKDLHKKYS YIRKTRPDGN CFYRAFGFSH LEALLDDSKE LQRFKAVSAK SKEDLVSQGF TEFTIEDFHN TFMDLIEQVE KQTSVADLLA SFNDQSTSDY LVVYLRLLTS GYLQRESKFF EHFIEGGRTV KEFCQQEVEP MCKESDHIHI IALAQALSVS IQVEYMDRGE GGTTNPHIFP EGSEPKVYLL YRPGHYDILY K.

Product Science Overview

Structure and Function

OTUB1 is a highly specific ubiquitin iso-peptidase, meaning it can cleave ubiquitin from branched poly-ubiquitin chains but not from ubiquitinated substrates . This specificity plays a crucial role in regulating protein turnover by preventing the degradation of proteins. OTUB1 achieves this by removing ‘Lys-48’-linked conjugated ubiquitin from proteins .

Biological Role

OTUB1 is involved in several important biological processes:

  1. Regulation of T-cell Anergy: OTUB1 interacts with RNF128/GRAIL, a crucial inductor of CD4 T-cell anergy. This interaction is vital for the immune system as it renders T-cells unresponsive to antigen rechallenge .
  2. Deubiquitination: OTUB1 mediates the deubiquitination of ‘Lys-48’-linked polyubiquitin chains, which is essential for maintaining protein stability and function .
  3. Interaction with Other Proteins: OTUB1 interacts with other ubiquitin proteases and E3 ubiquitin ligases, influencing various ubiquitin-dependent pathways .
Recombinant Production

Recombinant human OTUB1 protein is typically expressed in E. coli cells using an N-terminal His tag . This recombinant protein is used in various research applications, including studying protein-protein interactions, enzyme activity assays, and understanding the mechanisms of deubiquitination.

Clinical Relevance

Mutations or dysregulation of OTUB1 have been associated with diseases such as diabetic retinopathy and microvascular complications of diabetes . Understanding the function and regulation of OTUB1 can provide insights into these conditions and potentially lead to therapeutic interventions.

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