Recombinant Human Ring Finger And Chy Zinc Finger Domain-Containing Protein 1 (RCHY1) Protein (GST)

Name: Recombinant Human Ring Finger And Chy Zinc Finger Domain-Containing Protein 1 (RCHY1) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-08787P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Ring Finger And Chy Zinc Finger Domain-Containing Protein 1 (RCHY1) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q96PM5
Target Symbol	RCHY1
Synonyms	Androgen receptor N terminal interacting protein; Androgen receptor N-terminal-interacting protein; ARNIP; CH-rich-interacting match with PLAG1; CHIMP; E3 ubiquitin-protein ligase Pirh2; hARNIP; hPirh2; p53 induced protein with a RING H2 domain; p53-induced RING-H2 protein; PIRH2E; PIRH2F; PRO1996; RCHY1; Ring finger and CHY zinc finger domain containing 1 E3 ubiquitin protein ligase; RING finger and CHY zinc finger domain-containing protein 1; RING finger protein 199; RNF199; ZCHY; ZFP 363; zinc finger CHY type; Zinc finger protein 363; ZN363_HUMAN; ZNF363
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MAATAREDGASGQERGQRGCEHYDRGCLLKAPCCDKLYTCRLCHDNNEDHQLDRFKVKEVQCINCEKIQHAQQTCEECSTLFGEYYCDICHLFDKDKKQYHCENCGICRIGPKEDFFHCLKCNLCLAMNLQGRHKCIENVSRQNCPICLEDIHTSRVVAHVLPCGHLLHRTCYEEMLKEGYRCPLCMHSALDMTRYWRQLDDEVAQTPMPSEYQNMTVDILCNDCNGRSTVQFHILGMKCKICESYNTAQAGGRRISLDQQ
Expression Range	1-261aa
Protein Length	Full Length
Mol. Weight	57.1kDa
Research Area	Cell Biology
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Mediates E3-dependent ubiquitination and proteasomal degradation of target proteins, including p53/TP53, P73, HDAC1 and CDKN1B. Preferentially acts on tetrameric p53/TP53. Monoubiquitinates the translesion DNA polymerase POLH. Contributes to the regulation of the cell cycle progression. Increases AR transcription factor activity.
Subcellular Location	Nucleus. Nucleus speckle. Cytoplasm.
Database References	HGNC: 17479 OMIM: 607680 KEGG: hsa:25898 STRING: 9606.ENSP00000321239 UniGene: PMID: 28258514 Data indicate cellular E3 ubiquitin ligase ring-finger and CHY zinc-finger domain-containing 1 (RCHY1) as an interacting partner of the viral SARS-unique domain (SUD) and papain-like protease (PL(pro)), and, as a consequence, the involvement of cellular p53 as antagonist of coronaviral replication. PMID: 27519799 p27 and its cognate ubiquitin ligases, Skp2/KPC/Pirh2, are specifically involved in determining the clinical profiles of lung carcinomas. PMID: 28601655 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. PMID: 27393961 The Hoxa2-mediated decay of RCHY1 involves both the 19S and 20S proteasome complexes PMID: 26496426 Tumor suppressor p63 regulates expression of ubiquitin ligase PIRH2. PMID: 26995965 Overexpression of Pirh2 decreased the replication of prototype foamy virus, whereas knockdown of Pirh2 with specific siRNA increased PFV replication. PMID: 25848801 Pirh2 has a physiologically relevant role in keratinocyte differentiation through the posttranslational modification of p63 protein. PMID: 23235527 suggested that the interaction of SCYL1BP1/Pirh2 could accelerate Pirh2 degradation through an ubiquitin-dependent pathway. SCYL1BP1 may function as an important tumor suppressor gene in HCC development PMID: 22570270 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. PMID: 22766706 low expression of human PIRH2 in lung, ovarian, and breast cancers correlates with decreased patients' survival PMID: 22125490 Data show that Pirh2 monoubiquitinates PolH at one of multiple lysine residues, and that monoubiquitination of PolH inhibits its ability to interact with PCNA and bypass UV-induced lesions, leading to decreased viability. PMID: 21791603 Pirh2 promotes the proteasomal turnover of TAp73, and thus targeting Pirh2 to restore TAp73-mediated growth suppression in p53-deficient tumors may be developed as a novel anti-cancer strategy. PMID: 21852228 identified a novel Pirh2-interacting protein, AIG1, by yeast two-hybrid screening and confirmed its interaction with p53 both in vitro and in vivo PMID: 21622095 Our results suggest that Pirh2 mediates the degradation of p27(Kip1) and participates in cell proliferation in human hepatocellular carcinoma PMID: 21236467 This comprehensive analysis of the Pirh2 and Mdm2 RING domains provides structural and mechanistic insight into p53 regulation by its E3 ligases. PMID: 21084285 MDM2, MDMX, Pirh2 and COP1 might inhibit p53 activity synergistically in vivo. PMID: 20333547 SCYL1-BP1 can be ubiquitinated and degraded by Pirh2 but not by MDM2, which suggests that SCYL1-BP1 can be regulated by Pirh2. PMID: 20598683 low level of expression of hPirh2 was found both at transcriptional and translational level in human hepatocellular carcinoma (HCC) when compared to non-cancerous tissue. The protein shows no ubiquitin protein ligase activity. PMID: 20452352 found that DNA polymerase eta is recruited by Pirh2 and degraded by 20S proteasome in a ubiquitin-independent manner. PMID: 20008555 increased expression of PIRH2 was correlated with poor survival in patients with hepatocellular carcinoma; PIRH2 is a novel prognostic marker for hepatocellular carcinoma PMID: 19551892 expression of measles virus antigens in non-small cell lung carcinoma is associated with expression of Pirh2. The presence of Pirh2 itself was associated with improved survival. PMID: 19895323 cloning and characterization of an androgen receptor N-terminal-interacting protein with ubiquitin-protein ligase activity [androgen-receptor N-terminal-interacting protein; hARNIP] PMID: 12200228 This protein is a p53-induced ubiquitin-protein ligase which promotes p53 degradation. PMID: 12654245 These results are consistent with the hypothesis that increased Pirh2 expression affects lung tumorigenesis by reducing p53 activity. PMID: 15547185 Human PIRH2 as a key modulator of AR function, opening a new direction for targeted therapy in aggressive human prostate cancer. PMID: 16914734 Study evaluated Pirh2, MDM2, p53 and p21 expression after DNA damage using cancer cell lines with wildtype, mutant and null p53 and found that unlike MDM2, Pirh2 expression was not affected by wildtype p53 in the cancer cells. PMID: 16934800 phosphorylation of Pirh2 may act as a fine-tuning to maintain the balance of p53-Pirh2 autoregulatory feedback loop, which facilitates the tight regulation of p53 stability and tumor suppression PMID: 17568776 PIRH2 functions as a regulator for COP I complex. PMID: 17721809 Given the importance of Pirh2 in regulating p53 stability, its interaction with PLAGL2 may provide valuable therapeutic targets in treating Pirh2-overexpression malignancies. PMID: 17950244 Pirh2 acts as a negative regulator of p27(Kip1) function by promoting ubiquitin-dependent proteasomal degradation PMID: 18006823 The authors show that Pirh2-p53 interaction is dependent on the C-terminal zinc binding module of Pirh2, which binds to the tetramerization domain of p53. PMID: 19043414 The RCHY1 protein was displayed an unexpected role in regulating the organization of the network of K8/18 keratin filaments. PMID: 19282868 Pirh2 overexpression may have an important role in the development and maintenance of head and neck squamous cell carcinoma at least partially through p27 degradation PMID: 19445020 Pirh2 ubiquitin ligase has two novel isoforms that negatively regulate p53 independent of RING finger domains PMID: 19483087 Pirh2 (ZNF363), a gene regulated by p53, encodes a RING-H2 domain-containing protein with intrinsic ubiquitin-protein ligase activity. Pirh2 protein physically interacts with p53 and promotes ubiquitination and degradation of p53 independently of Mdm2. PMID: 12654245

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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