NewEast Biosciences pioneered the research and development of the antibodies for GTPases and mutated Oncogene ten years ago. GTPases involve (1) signal transduction in response to activation of cell surface receptors, including transmembrane receptors such as those mediating taste, smell and vision, (2) protein biosynthesis at the ribosome, (3) regulation of cell differentiation, proliferation, division and movement, (4) translocation of proteins through membranes, (5) transport of vesicles within the cell, and vesicle-mediated secretion and uptake, through GTPase control of vesicle coat assembly. An oncogene is a gene that has the potential to cause cancer.
We offer three unique categories of antibodies, which (1) recognize only the active configuration of GTPase (not the inactive one), (2) mutated Oncogene (not mild type) and (3) have super affinity for cAMP and cGMP (no acetylation required). We have over one thousand peer reviewed articles cited our products.
$349.00
Cat.#: N262646 |
Product Name: Anti-OTUB1 Rabbit Monoclonal Antibody |
Synonyms: OTUB1; OTB1; OTU1; HSPC263; Ubiquitin thioesterase OTUB1; Deubiquitinating enzyme OTUB1; OTU domain-containing ubiquitin aldehyde-binding protein 1; Otubain-1; hOTU1; Ubiquitin-specific-processing protease OTUB1 |
UNIPROT ID: Q96FW1 |
Background: Hydrolase that can specifically remove ‘Lys-48’-linked conjugated ubiquitin from proteins and plays an important regulatory role at the level of protein turnover by preventing degradation. Regulator of T-cell anergy, a phenomenon that occurs when T-cells are rendered unresponsive to antigen rechallenge and no longer respond to their cognate antigen. Acts via its interaction with RNF128/GRAIL, a crucial inductor of CD4 T-cell anergy. Isoform 1 destabilizes RNF128, leading to prevent anergy. In contrast, isoform 2 stabilizes RNF128 and promotes anergy. Surprisingly, it regulates RNF128-mediated ubiquitination, but does not deubiquitinate polyubiquitinated RNF128. Deubiquitinates estrogen receptor alpha (ESR1). Mediates deubiquitination of ‘Lys-48’-linked polyubiquitin chains, but not ‘Lys-63’-linked polyubiquitin chains. Not able to cleave di-ubiquitin. Also capable of removing NEDD8 from NEDD8 conjugates, but with a much lower preference compared to ‘Lys-48’-linked ubiquitin.Plays a key non-catalytic role in DNA repair regulation by inhibiting activity of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of ‘Lys-63’-linked histone H2A and H2AX at DNA damage sites. Inhibits RNF168 independently of ubiquitin thioesterase activity by binding and inhibiting UBE2N/UBC13, the E2 partner of RNF168, thereby limiting spreading of ‘Lys-63’-linked histone H2A and H2AX marks. Inhibition occurs by binding to free ubiquitin: free ubiquitin acts as an allosteric regulator that increases affinity for UBE2N/UBC13 and disrupts interaction with UBE2V1. The OTUB1-UBE2N/UBC13-free ubiquitin complex adopts a configuration that mimics a cleaved ‘Lys48’-linked di-ubiquitin chain.MiscellaneousIn the structure described by PubMed:18954305, the His-265 active site of the catalytic triad is located too far to interact directly with the active site Cys-91. A possible explanation is that OTUB1 is in inactive conformation in absence of ubiquitin and a conformation change may move His-265 in the proximity of Cys-91 in presence of ubiquitin substrate. |
Immunogen: A synthetic peptide of human OTUB1 |
Applications: WB,IP |
Recommended Dilutions: WB: 1/500-1/1000 IP: 1/20 |
Host Species: Rabbit |
Clonality: Rabbit Monoclonal |
Clone ID: R04-6I3 |
MW: Calculated MW: 31 kDa; Observed MW: 31 kDa |
Isotype: IgG |
Purification: Affinity Purified |
Species Reactivity: Human,Mouse,Rat |
Conjugation: Unconjugated |
Modification: Unmodified |
Constituents: PBS (without Mg2+ and Ca2+), pH 7.3 containing 50% glycerol, 0.5% BSA and 0.02% sodium azide |
Research Areas: Epigenetics and Nuclear Signaling |
Storage & Shipping: Store at -20°C. Avoid repeated freezing and thawing |
Western blot analysis of OTUB1 in K562, rat Brain, C6, 3T3, Hela lysates using OTUB1 antibody. |