Pirh21 (7B9) Mouse mAb
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Application
| WB, IHC-P, IF, FC, ICC |
|---|---|
| Primary Accession | Q96PM5 |
| Reactivity | Rat, Human |
| Host | Mouse |
| Clonality | Monoclonal Antibody |
| Isotype | IgG1 |
| Conjugate | Unconjugated |
| Immunogen | Purified recombinant fragment of human Pirh2 expressed in E. Coli. |
| Purification | Ascitic Fluid |
| Calculated MW | 30110 Da |
| Gene ID | 25898 |
|---|---|
| Other Names | ARNIP; CHIMP; RNF199; RCHY1 |
| Dilution | WB~~1:1000 IHC-P~~1:50~200 IF~~1:50~200 FC~~1:10~50 ICC~~N/A |
| Format | Liquid in Purified antibody in PBS with 0.05% sodium azide. |
| Storage | Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles. |
For Research Use Only. Not For Use In Diagnostic Procedures.
| Name | RCHY1 |
|---|---|
| Function | E3 ubiquitin-protein ligase that mediates ubiquitination of target proteins, including p53/TP53, TP73, HDAC1 and CDKN1B (PubMed:16914734, PubMed:17721809, PubMed:18006823, PubMed:19043414, PubMed:19483087, PubMed:21994467). Mediates ubiquitination and degradation of p53/TP53; preferentially acts on tetrameric p53/TP53 (PubMed:19043414, PubMed:19483087). Catalyzes monoubiquitinates the translesion DNA polymerase POLH (PubMed:21791603). Involved in the ribosome-associated quality control (RQC) pathway, which mediates the extraction of incompletely synthesized nascent chains from stalled ribosomes: RCHY1 acts downstream of NEMF and recognizes CAT tails associated with stalled nascent chains, leading to their ubiquitination and degradation (PubMed:33909987). |
| Cellular Location | Nucleus. Nucleus speckle. Cytoplasm |
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
Swiss-Prot Acc.Q96PM5.Pirh 2 (P53 induced RING-H2 protein), also known as RCHY1, it forms dimers through its N- and C-terminus in cells. The Pirh2 has ubiquitin-protein ligase activity and it binds with p53 and promotes the ubiquitin-mediated proteosomal degradation of p53. The Pirh2 is oncogenic because loss of p53 function contributes directly to malignant tumor development. Pirh2 expression decreases the level of p53, and a decrease of endogenous Pirh2 expression increases p53 levels. Pirh2 is therefore considered, together with MDM2, to act as a negative regulator of p53 function.
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