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The protein encoded by RCHY1 has ubiquitin ligase activity. Additionally we are shipping Ring Finger and CHY Zinc Finger Domain Containing 1, E3 Ubiquitin Protein Ligase Proteins (5) and many more products for this protein.
Showing 10 out of 53 products:
Human Polyclonal RCHY1 Primary Antibody for IP, WB - ABIN250699
Koivusalo, Mialon, Pitkänen, Westermarck, Hietanen: Activation of p53 in cervical cancer cells by human papillomavirus E6 RNA interference is transient, but can be sustained by inhibiting endogenous nuclear export-dependent p53 antagonists. in Cancer research 2006
Show all 9 references for 250699
Human Monoclonal RCHY1 Primary Antibody for EIA, FACS - ABIN1108844
Zheng, Ning, Yang: PLAGL2 controls the stability of Pirh2, an E3 ubiquitin ligase for p53. in Biochemical and biophysical research communications 2007
Show all 5 references for 1108844
Human Monoclonal RCHY1 Primary Antibody for ELISA, WB - ABIN393831
Yan, Zhang, Di, Shi, Rao, Huo: A newly identified Pirh2 substrate SCYL1-BP1 can bind to MDM2 and accelerate MDM2 self-ubiquitination. in FEBS letters 2010
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Human Monoclonal RCHY1 Primary Antibody for ICC, FACS - ABIN1724723
Duan, Gao, Druhan, Zhu, Morrison, Otterson, Villalona-Calero: Expression of Pirh2, a newly identified ubiquitin protein ligase, in lung cancer. in Journal of the National Cancer Institute 2004
Show all 2 references for 1724723
Cow (Bovine) Polyclonal RCHY1 Primary Antibody for WB - ABIN2775660
Maruyama, Miyajima, Bohgaki, Tsukiyama, Shigemura, Nonomura, Hatakeyama: Ubiquitylation of epsilon-COP by PIRH2 and regulation of the secretion of PSA. in Molecular and cellular biochemistry 2007
This study showed that ORF3 (show ASZ1 Antibodies) protein of porcine circovirus type 2 interacted competitively with p53 tumor suppressor protein (show TP53 Antibodies) in binding to porcine Pirh2.
Results show that the PCV2 ORF3 (show ASZ1 Antibodies) protein specifically interacts with pPirh2 and inhibits its stabilization; this may lead to increasing p53 (show TP53 Antibodies) expression, resulting in apoptosis.
Findings indicate that PIRH2 has central roles in the ubiquitylation of Chk2 (show CHEK2 Antibodies) and its turnover and in the regulation of its function.
This study provides evidence that the ubiquitination of p73 (show ARHGAP24 Antibodies) mediated by Pirh2 represents an important pathway for controlling the suppressive function of p73 (show ARHGAP24 Antibodies)
these data reveal the in vivo roles of Pirh2 in the regulation of p53 and c-Myc stability and support its role as a tumor suppressor
Data show that Pirh2 monoubiquitinates PolH (show POLH Antibodies) at one of multiple lysine residues, and that monoubiquitination of PolH (show POLH Antibodies) inhibits its ability to interact with PCNA (show PCNA Antibodies) and bypass UV-induced lesions, leading to decreased viability.
cloning and characterization of an androgen receptor N-terminal-interacting protein with ubiquitin-protein ligase (show UBE2K Antibodies) activity [androgen-receptor N-terminal-interacting protein; mARNIP]
Pirh2 (Zfp363), a gene regulated by p53 (show TP53 Antibodies), encodes a RING-H2 domain-containing protein with intrinsic ubiquitin-protein ligase (show UBE2K Antibodies) activity. Pirh2 physically interacts with p53 (show TP53 Antibodies) and promotes ubiquitination and degradation of p53 (show TP53 Antibodies) independently of Mdm2 (show MDM2 Antibodies).
These results are consistent with the hypothesis that increased Pirh2 expression affects lung tumorigenesis by reducing p53 (show TP53 Antibodies) activity.
Pirh2 acts as a negative regulator of p27(Kip1 (show CDKN1B Antibodies)) function by promoting ubiquitin-dependent proteasomal degradation
Decrease of PIRH2 expression in the breast cancer cell line MDA-MB-231 resulted in reduced tumor cell growth via the inhibition of cell proliferation and the interruption of cell cycle transition.
The Hoxa2 (show HOXA2 Antibodies)-mediated decay of RCHY1 involves both the 19S and 20S proteasome (show PSMA5 Antibodies) complexes
Tumor suppressor p63 (show RPE65 Antibodies) regulates expression of ubiquitin ligase PIRH2.
Overexpression of Pirh2 decreased the replication of prototype foamy virus, whereas knockdown of Pirh2 with specific siRNA increased PFV replication.
Pirh2 has a physiologically relevant role in keratinocyte differentiation through the posttranslational modification of p63 (show RPE65 Antibodies) protein.
suggested that the interaction of SCYL1BP1 (show GORAB Antibodies)/Pirh2 could accelerate Pirh2 degradation through an ubiquitin-dependent pathway. SCYL1BP1 (show GORAB Antibodies) may function as an important tumor suppressor gene in HCC (show FAM126A Antibodies) development
Compared to full-length PIRH2A, PIRH2E lacks amino acids 235-261, while PIRH2F is missing C-terminal amino acids 227-261 and both isoforms harbor the RING domain.
low expression of human PIRH2 in lung, ovarian, and breast cancers correlates with decreased patients' survival
The protein encoded by this gene has ubiquitin ligase activity. It mediates E3-dependent ubiquitination and proteasomal degradation of target proteins, including TP53, HDAC1 and CDKN1B, thus regulating their levels and cell cycle progression. Alternatively spliced transcript variants encoding different isoforms have been described for this gene.
CH-rich interacting match with PLAG1
, E3 ubiquitin-protein ligase Pirh2
, RING finger and CHY zinc finger domain-containing protein 1
, RING finger protein 199
, androgen-receptor N-terminal-interacting protein
, p53-induced protein with a RING-H2 domain
, zinc finger protein 363
, CH-rich-interacting match with PLAG1
, androgen receptor N-terminal-interacting protein
, ring finger and CHY zinc finger domain containing 1