Anti-UBR2 Picoband™ Antibody (monoclonal, 2G10)
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Application
| WB |
|---|---|
| Primary Accession | Q8IWV8 |
| Host | Mouse |
| Isotype | Mouse IgG2a |
| Reactivity | Human |
| Clonality | Monoclonal |
| Format | Lyophilized |
| Description | Anti-UBR2 Picoband™ Antibody (monoclonal, 2G10) . Tested in WB applications. This antibody reacts with Human. |
| Reconstitution | Add 0.2ml of distilled water will yield a concentration of 500ug/ml. |
| Gene ID | 23304 |
|---|---|
| Other Names | E3 ubiquitin-protein ligase UBR2, 2.3.2.27, N-recognin-2, RING-type E3 ubiquitin transferase UBR2, Ubiquitin-protein ligase E3-alpha-2, Ubiquitin-protein ligase E3-alpha-II, UBR2, C6orf133, KIAA0349 |
| Calculated MW | 200538 Da |
| Application Details | Western blot, 0.25-0.5 µg/ml, Human |
| Source | Eukaryota |
| Contents | Each vial contains 4mg Trehalose, 0.9mg NaCl and 0.2mg Na2HPO4. |
| Clone Names | Clone: 2G10 |
| Immunogen | E.coli-derived human UBR2 recombinant protein (Position: Q10-A664). |
| Purification | Immunogen affinity purified. |
| Storage | Store at -20˚C for one year from date of receipt. After reconstitution, at 4˚C for one month. It can also be aliquotted and stored frozen at -20˚C for six months. Avoid repeated freeze-thaw cycles. |
For Research Use Only. Not For Use In Diagnostic Procedures.
| Name | UBR2 |
|---|---|
| Synonyms | C6orf133, KIAA0349 |
| Function | E3 ubiquitin-protein ligase which is a component of the N-end rule pathway (PubMed:15548684, PubMed:20835242, PubMed:28392261). Recognizes and binds to proteins bearing specific N-terminal residues (N-degrons) that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation (PubMed:20835242, PubMed:28392261). Recognizes both type-1 and type-2 N-degrons, containing positively charged amino acids (Arg, Lys and His) and bulky and hydrophobic amino acids, respectively (PubMed:20835242, PubMed:28392261). Does not ubiquitinate proteins that are acetylated at the N-terminus (PubMed:20835242). In contrast, it strongly binds methylated N-degrons (PubMed:28392261). Plays a critical role in chromatin inactivation and chromosome-wide transcriptional silencing during meiosis via ubiquitination of histone H2A (By similarity). Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth (PubMed:20298436). Required for spermatogenesis, promotes, with Tex19.1, SPO11-dependent recombination foci to accumulate and drive robust homologous chromosome synapsis (By similarity). Polyubiquitinates LINE-1 retrotransposon encoded, LIRE1, which induces degradation, inhibiting LINE-1 retrotransposon mobilization (By similarity). Catalyzes ubiquitination and degradation of the N-terminal part of NLRP1 following NLRP1 activation by pathogens and other damage-associated signals: ubiquitination promotes degradation of the N-terminal part and subsequent release of the cleaved C-terminal part of NLRP1, which polymerizes and forms the NLRP1 inflammasome followed by host cell pyroptosis (By similarity). Plays a role in T-cell receptor signaling by inducing 'Lys-63'-linked ubiquitination of lymphocyte cell-specific kinase LCK (PubMed:38225265). This activity is regulated by DUSP22, which induces 'Lys-48'-linked ubiquitination of UBR2, leading to its proteasomal degradation by SCF E3 ubiquitin-protein ligase complex (PubMed:38225265). |
| Cellular Location | Nucleus {ECO:0000250|UniProtKB:Q6WKZ8}. Chromosome {ECO:0000250|UniProtKB:Q6WKZ8}. Note=Associated with chromatin during meiosis. {ECO:0000250|UniProtKB:Q6WKZ8} |
| Tissue Location | Broadly expressed, with highest levels in skeletal muscle, kidney and pancreas. Present in acinar cells of the pancreas (at protein level). |
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
E3 ubiquitin-protein ligase UBR2 is an enzyme that in humans is encoded by the UBR2 gene. It is mapped to 6p21.1. This gene encodes an E3 ubiquitin ligase of the N-end rule proteolytic pathway that targets proteins with destabilizing N-terminal residues for polyubiquitylation and proteasome-mediated degradation. Alternative splicing results in multiple transcript variants.
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