OTUB2 Antibody
Ubiquitin thioesterase OTUB2, Deubiquitinating enzyme OTUB2, OTU domain-containing ubiquitin aldehyde-binding protein 2, Otubain-2, Ubiquitin-specific-processing protease OTUB2, OTUB2, C14orf137, OTB2, OTU2.
Description
Product Specs
OTUB2, or Ubiquitin thioesterase OTUB2, is part of the peptidase C65 family. This hydrolase enzyme can deubiquitinate proteins in vitro, suggesting a regulatory role in protein turnover by preventing degradation.
The solution is at a concentration of 1mg/ml in a buffer of PBS at pH 7.4, with 10% Glycerol and 0.02% Sodium Azide.
The OTUB2 antibody has undergone testing by both ELISA and Western blot to ensure its specificity and reactivity. However, due to variations in applications, it is recommended to titrate the reagent for each specific use to achieve optimal results.
Ubiquitin thioesterase OTUB2, Deubiquitinating enzyme OTUB2, OTU domain-containing ubiquitin aldehyde-binding protein 2, Otubain-2, Ubiquitin-specific-processing protease OTUB2, OTUB2, C14orf137, OTB2, OTU2.
OTUB2 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
PAT1F8AT.
Anti-human OTUB2 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human OTUB2 protein 1-234 amino acids purified from E. coli.
Mouse IgG1 heavy chain and k light chain.
Product Science Overview
Mouse Anti Human Ubiquitin Aldehyde Binding 2 (OTUB2) is a deubiquitinase enzyme that plays a crucial role in the regulation of protein stability through the ubiquitin-proteasome system (UPS). Ubiquitination is a post-translational modification process where ubiquitin molecules are attached to substrate proteins, marking them for degradation or altering their function. Deubiquitinases (DUBs) like OTUB2 remove ubiquitin from proteins, thereby regulating their stability and function.
The preparation of Mouse Anti Human Ubiquitin Aldehyde Binding 2 involves several steps:
- Gene Cloning: The gene encoding OTUB2 is cloned into an appropriate expression vector.
- Expression: The vector is introduced into a suitable host cell, such as E. coli or mammalian cells, to express the OTUB2 protein.
- Purification: The expressed OTUB2 protein is purified using techniques such as affinity chromatography, which exploits the protein’s specific binding properties.
- Characterization: The purified protein is characterized using methods like SDS-PAGE and Western blotting to confirm its identity and purity.
For large-scale production of OTUB2, the following methods are typically employed:
- Fermentation: Large-scale fermentation processes are used to culture the host cells expressing OTUB2. This involves optimizing growth conditions to maximize protein yield.
- Downstream Processing: After fermentation, the cells are harvested, and the OTUB2 protein is extracted and purified using industrial-scale chromatography techniques.
- Quality Control: Rigorous quality control measures are implemented to ensure the consistency and purity of the produced OTUB2 protein. This includes testing for contaminants and verifying the protein’s activity.
OTUB2 functions by binding to ubiquitinated substrates and catalyzing the removal of ubiquitin molecules. This process involves several key steps:
- Substrate Recognition: OTUB2 recognizes and binds to specific ubiquitinated substrates through its ubiquitin-binding domains.
- Catalysis: The enzyme’s catalytic domain cleaves the isopeptide bond between ubiquitin and the substrate protein, releasing free ubiquitin.
- Regulation: OTUB2 activity is regulated by various factors, including post-translational modifications and interactions with other proteins.
OTUB2 has been implicated in various cellular processes, including cell cycle regulation, DNA repair, and signal transduction. Dysregulation of OTUB2 activity has been linked to several diseases, particularly cancer. For instance, elevated levels of OTUB2 have been associated with poor prognosis and increased metastasis in colon cancer .
