Pirh2 Antibody (YA4435)
(Synonyms: ARNIP; CHIMP; RNF199; RCHY1)
Based on 1 Customer Validation
Pirh2 Antibody (YA4435) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to Pirh2.
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Host:
Mouse
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Isotype:
IgG1
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Application:
WB, IHC-P, ICC/IF, FC, ELISA
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Reactivity :
Human, Rat
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Formulation:
Supplied in PBS with 0.05% sodium azide.
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
WB
WB: Western Blot
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IHC-P
IHC-P: Immunohistochemistry-Paraffin
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
FC
FC: Flow Cytometry
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ELISA
ELISA: Enzyme Linked Immunosorbent Assay
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|---|---|---|---|---|---|
| Dilution Ratio | 1:500-1:2000 | 1:200-1:1000 | 1:200-1:1000 | 1:200-1:400 | 1:10000 |
Product Details
Pirh2 Antibody (YA4435) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to Pirh2.
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Host Mouse
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Clonality Monoclonal
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Species ReactivityHuman, Rat
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Observed Molecular WeightObserved band size: 30 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 30 kDa
Purified recombinant fragment of human Pirh2 full(aa 1-261).
affinity purified.
Non-conjugated
Unmodified
IgG1
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS with 0.05% sodium azide.
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Concentration
Batch-dependent, Please check the COA for the concentration of each lot. Check Lot Concentration
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
Pirh2 is an E3 ubiquitin-protein ligase that mediates ubiquitination of target proteins, including p53/TP53, TP73, HDAC1 and CDKN1B. Mediates ubiquitination and degradation of p53/TP53; preferentially acts on tetrameric p53/TP53. Catalyzes monoubiquitinates the translesion DNA polymerase POLH. 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; Has no E3 ubiquitin-protein ligase activity[1][2][3][4][5][6][7][8].
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Subcellular Localization
Nucleus; Nucleus speckle; Cytoplasm
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Expression
Induction:Up-regulated during the S phase of the cell cycle (PubMed:18006823) . Expressed at low levels during G phase (PubMed:18006823) ; Down-regulated in hepatocellular carcinoma -
Isoforms & Post-Translational Modification
Q96PM5 has 8 isomers: Q96PM5-1: 30110 Da (predicted); Q96PM5-2: 28983 Da (predicted); Q96PM5-3: 20720 Da (predicted); Q96PM5-4: 21697 Da (predicted); Q96PM5-5: 8494 Da (predicted); Q96PM5-6: 27676 Da (predicted); Q96PM5-7: 25337 Da (predicted); Q96PM5-8: 24210 Da (predicted).
Subject to ubiquitination and proteasomal degradation. Interaction with PLAGL2 or KAT5 enhances protein stability -
Subunit
Monomer and homodimer. Interacts with AR, MDM2, KAT5, PLAG1, PLAGL2, COPE, UBE2D2 and GORAB/NTKLBP1
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SwissProt ID
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Synonyms
ARNIP; CHIMP; RNF199; RCHY1
Documentation
References
[1]. Logan IR, et al. Human PIRH2 enhances androgen receptor signaling through inhibition of histone deacetylase 1 and is overexpressed in prostate cancer. Mol Cell Biol. 2006 Sep;26(17):6502-10. [Content Brief]
[2]. Maruyama S, et al. Ubiquitylation of epsilon-COP by PIRH2 and regulation of the secretion of PSA. Mol Cell Biochem. 2008 Jan;307(1-2):73-82. [Content Brief]
[3]. Hattori T, et al. Pirh2 promotes ubiquitin-dependent degradation of the cyclin-dependent kinase inhibitor p27Kip1. Cancer Res. 2007 Nov 15;67(22):10789-95. [Content Brief]
[4]. Sheng Y, et al. Molecular basis of Pirh2-mediated p53 ubiquitylation. Nat Struct Mol Biol. 2008 Dec;15(12):1334-42. [Content Brief]
[5]. Corcoran CA, et al. Identification and characterization of two novel isoforms of Pirh2 ubiquitin ligase that negatively regulate p53 independent of RING finger domains. J Biol Chem. 2009 Aug 14;284(33):21955-21970. [Content Brief]
[6]. Wu H, et al. Pirh2, a ubiquitin E3 ligase, inhibits p73 transcriptional activity by promoting its ubiquitination. Mol Cancer Res. 2011 Dec;9(12):1780-90. [Content Brief]
[7]. Jung YS, et al. Pirh2 E3 ubiquitin ligase monoubiquitinates DNA polymerase eta to suppress translesion DNA synthesis. Mol Cell Biol. 2011 Oct;31(19):3997-4006. [Content Brief]
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