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ELISA Kit for Human E3 ubiquitin-protein ligase SIAH2

SKU : BHE13809504

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EIAAB SCIENCE INC, WUHAN

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Mfr.No.	E5526h
Alternative Names	RING-type E3 ubiquitin transferase SIAH2 ; Seven in absentia homolog 2 ; Siah-2
Categories	Elisa
Function	E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates E3 ubiquitin ligase activity either through direct binding to substrates or by functioning as the essential RING domain subunit of larger E3 complexes. Triggers the ubiquitin-mediated degradation of many substrates, including proteins involved in transcription regulation (POU2AF1, PML, NCOR1), a cell surface receptor (DCC), an antiapoptotic protein (BAG1), and a protein involved in synaptic vesicle function in neurons (SYP). It is thereby involved in apoptosis, tumor suppression, cell cycle, transcription and signaling processes. Has some overlapping function with SIAH1. Triggers the ubiquitin-mediated degradation of TRAF2, whereas SIAH1 can not. Promotes monoubiquitination of SNCA.
Specificity	Natural and recombinant Human E3 ubiquitin-protein ligase SIAH2
Subcellular Location	Cytoplasm Nucleus Predominantly cytoplasmic (Probable). Partially nuclear.
Detection Range	78-5000pg/mL
Entryname	SIAH2_HUMAN
Method Type	Sandwich
Platform	PF03145
Protein Name	E3 ubiquitin-protein ligase SIAH2
Sensitivity	25pg/mL
Sequence	50: MSRPSSTGPS ; ANKPCSKQPP ; PQPQHTPSPA ; APPAAATISA ; AGPGSSAVPA ; 100: AAAVISGPGG ; GGGAGPVSPQ ; HHELTSLFEC ; PVCFDYVLPP ; ILQCQAGHLV ; 150: CNQCRQKLSC ; CPTCRGALTP ; SIRNLAMEKV ; ASAVLFPCKY ; ATTGCSLTLH ; 200: HTEKPEHEDI ; CEYRPYSCPC ; PGASCKWQGS ; LEAVMSHLMH ; AHKSITTLQG ; 250: EDIVFLATDI ; NLPGAVDWVM ; MQSCFGHHFM ; LVLEKQEKYE ; GHQQFFAIVL ; 300: LIGTRKQAEN ; FAYRLELNGN ; RRRLTWEATP ; RSIHDGVAAA ; IMNSDCLVFD ; 324: TAIAHLFADN ; GNLGINVTIS ; TCCP
Sequence Length	324
String	O43255
Sub Unit	Homodimer. Interacts with UBE2E2. Interacts with PEG3 (By similarity). Interacts with VAV1, without mediating its ubiquitin-mediated degradation. Interacts with CACYBP/SIP. Probable component of some large E3 complex possibly composed of UBE2D1, SIAH2, CACYBP/SIP, SKP1, APC and TBL1X. Interacts with PEG10, which may inhibit its activity. Interacts with EGLN2 and SNCAIP.

Uniprot	O43255
Gene Name	SIAH2
Immunogen Species	Homo Sapiens (Human)
Kegg	hsa:6478
Unigene	Hs.477959

Reference	1. "Characterization of human homologs of the Drosophila seven in absentia (sina) gene." Hu G., Chung Y.-L., Glover T., Valentine V., Look A.T., Fearon E.R. Genomics46:103-111(1997) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA];TISSUE SPECIFICITY 2. "hSiah2 is a new Vav binding protein which inhibits Vav-mediated signaling pathways." Germani A., Romero F., Houlard M., Camonis J., Gisselbrecht S., Fischer S., Varin-Blank N. Mol. Cell. Biol.19:3798-3807(1999) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA];INTERACTION WITH VAV1 3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res.14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] tissue: Brain. 4. "Mammalian homologs of seven in absentia regulate DCC via the ubiquitin-proteasome pathway." Hu G., Zhang S., Vidal M., Baer J.L., Xu T., Fearon E.R. Genes Dev.11:2701-2714(1997) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION IN DEGRADATION OF DCC;INTERACTION WITH UBE2I 5. "Regulation of BOB.1/OBF.1 stability by SIAH." Boehm J., He Y., Greiner A., Staudt L., Wirth T. EMBO J.20:4153-4162(2001) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION IN DEGRADATION OF POU2AF1 6. "Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses." Matsuzawa S., Reed J.C. Mol. Cell7:915-926(2001) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH CACYBP 7. "Stress-induced decrease in TRAF2 stability is mediated by Siah2." Habelhah H., Frew I.J., Laine A., Janes P.W., Relaix F., Sassoon D., Bowtell D.D.L., Ronai Z. EMBO J.21:5756-5765(2002) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION IN DEGRADATION OF TRAF2 8. "Involvement of PEG10 in human hepatocellular carcinogenesis through interaction with SIAH1." Okabe H., Satoh S., Furukawa Y., Kato T., Hasegawa S., Nakajima Y., Yamaoka Y., Nakamura Y. Cancer Res.63:3043-3048(2003) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH PEG10 9. "Characterization of different isoforms of the HIF prolyl hydroxylase PHD1 generated by alternative initiation." Tian Y.M., Mole D.R., Ratcliffe P.J., Gleadle J.M. Biochem. J.397:179-186(2006) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH EGLN2 10. "Synphilin-1A inhibits seven in absentia homolog (SIAH) and modulates alpha-synuclein monoubiquitylation and inclusion formation." Szargel R., Rott R., Eyal A., Haskin J., Shani V., Balan L., Wolosker H., Engelender S. J. Biol. Chem.284:11706-11716(2009) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;INTERACTION WITH SNCAIP;SUBCELLULAR LOCATION;ENZYME REGULATION 11. "Mutual regulation between SIAH2 and DYRK2 controls hypoxic and genotoxic signaling pathways." Perez M., Garcia-Limones C., Zapico I., Marina A., Schmitz M.L., Munoz E., Calzado M.A. J. Mol. Cell Biol.4:316-330(2012) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;INTERACTION WITH DYRK2;SUBCELLULAR LOCATION;PHOSPHORYLATION AT SER-16; THR-26; SER-28; SER-68 AND THR-119;MUTAGENESIS OF SER-16; THR-26; SER-28; SER-68 AND THR-119;IDENTIFICATION BY MASS SPECTROMETRY

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