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ELISA Kit for Mouse E3 ubiquitin-protein ligase SIAH2

SKU : BHE13810215

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EIAAB SCIENCE INC, WUHAN

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Mfr.No.	E5526m
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. Promotes monoubiquitination of SNCA (By similarity). 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.
Specificity	Natural and recombinant Mouse E3 ubiquitin-protein ligase SIAH2
Subcellular Location	Cytoplasm Nucleus Predominantly cytoplasmic (By similarity). Partially nuclear.
Entryname	SIAH2_MOUSE
Platform	PF03145
Protein Name	E3 ubiquitin-protein ligase SIAH2
Sequence	50: MSRPSSTGPS ; ANKPCSKQPP ; PPQTPHAPSP ; AAPPAAATIS ; AAGPGSSAVP ; 100: AAAAVISGPG ; AGGGADPVSP ; QHHELTSLFE ; CPVCFDYVLP ; PILQCQAGHL ; 150: VCNQCRQKLS ; CCPTCRGALT ; PSIRNLAMEK ; VASAVLFPCK ; YATTGCSLTL ; 200: HHTEKPEHED ; ICEYRPYSCP ; CPGASCKWQG ; SLEAVMSHLM ; HAHKSITTLQ ; 250: GEDIVFLATD ; INLPGAVDWV ; MMQSCFGHHF ; MLVLEKQEKY ; EGHQQFFAIV ; 300: LLIGTRKQAE ; NFAYRLELNG ; NRRRLTWEAT ; PRSIHDGVAA ; AIMNSDCLVF ; 325: DTAIAHLFAD ; NGNLGINVTI ; STCCQ
Sequence Length	325
String	Q06986
Sub Unit	Homodimer. Interacts with UBE2E2. 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 UBE2I. Interacts with PEG10, which may inhibit its activity. Interacts with EGLN2 and SNCAIP (By similarity). Interacts with PEG3.

Uniprot	Q06986
Gene Name	Siah2
Immunogen Species	Mus musculus (Mouse)
Kegg	mmu:20439
Unigene	Mm.2847

Reference	1. "Isolation and characterisation of murine homologues of the Drosophila seven in absentia gene (sina)." Della N.G., Senior P.V., Bowtell D.D.L. Development117:1333-1343(1993) [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 strain: Swiss. 2. "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] strain: C57BL/6. tissue: Brain. 3. "Expression of Siah-2, a vertebrate homologue of Drosophila sina, in germ cells of the mouse ovary and testis." Della N.G., Bowtell D.D.L., Beck F. Cell Tissue Res.279:411-419(1995) [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: TISSUE SPECIFICITY 4. "Proteasomal regulation of nuclear receptor corepressor-mediated repression." Zhang J., Guenther M.G., Carthew R.W., Lazar M.A. Genes Dev.12:1775-1780(1998) [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 NCOR1 5. "Pw1/Peg3 is a potential cell death mediator and cooperates with Siah1a in p53-mediated apoptosis." Relaix F., Wei X., Li W., Pan J., Lin Y., Bowtell D.D., Sassoon D.A., Wu X. Proc. Natl. Acad. Sci. U.S.A.97:2105-2110(2000) [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 PEG3 6. "Alteration of the stability of Bag-1 protein in the control of olfactory neuronal apoptosis." Sourisseau T., Desbois C., Debure L., Bowtell D.D.L., Cato A.C.B., Schneikert J., Moyse E., Michel D. J. Cell Sci.114:1409-1416(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 BAG1 7. "Normal p53 function in primary cells deficient for Siah genes." Frew I.J., Dickins R.A., Cuddihy A.R., Del Rosario M., Reinhard C., O'Connell M.J., Bowtell D.D.L. Mol. Cell. Biol.22:8155-8164(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: INDUCTION 8. "Generation and analysis of Siah2 mutant mice." Frew I.J., Hammond V.E., Dickins R.A., Quinn J.M.W., Walkley C.R., Sims N.A., Schnall R., Della N.G., Holloway A.J., Digby M.R., Janes P.W., Tarlinton D.M., Purton L.E., Gillespie M.T., Bowtell D.D.L. Mol. Cell. Biol.23:9150-9161(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: FUNCTION 9. "The coiled-coil domain is the structural determinant for mammalian homologues of Drosophila Sina-mediated degradation of promyelocytic leukemia protein and other tripartite motif proteins by the proteasome." Fanelli M., Fantozzi A., De Luca P., Caprodossi S., Matsuzawa S., Lazar M.A., Pelicci P.G., Minucci S. J. Biol. Chem.279:5374-5379(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: FUNCTION IN DEGRADATION OF PML 10. "Regulation of the ring finger E3 ligase Siah2 by p38 MAPK." Khurana A., Nakayama K., Williams S., Davis R.J., Mustelin T., Ronai Z. J. Biol. Chem.281:35316-35326(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: PHOSPHORYLATION AT THR-24 AND SER-29;FUNCTION

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