|Application ||WB, E|
|Antigen Region||273-301 aa|
|Other Names||Gem-associated protein 4, Gemin-4, Component of gems 4, p97, GEMIN4|
|Target/Specificity||This GEMIN4 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 273-301 amino acids from the N-terminal region of human GEMIN4.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||GEMIN4 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus.|
|Cellular Location||Cytoplasm. Nucleus. Nucleus, nucleolus. Nucleus, gem. Note=Localized in subnuclear structures next to coiled bodies, called gems, which are highly enriched in spliceosomal snRNPs and in the nucleolus EMBL; AF173856; AAF35283.1; -; mRNA EMBL; AC087392; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; AL080150; CAB45743.3; -; mRNA EMBL; AL080167; CAB45755.1; -; mRNA CCDS; CCDS45559.1; - PIR; T12535; T12535 RefSeq; NP_056536.2; NM_015721.2 UniGene; Hs.499620; - ProteinModelPortal; P57678; - SMR; P57678; - BioGrid; 119102; 93 CORUM; P57678; - IntAct; P57678; 76 MINT; P57678; - STRING; 9606.ENSP00000321706; - iPTMnet; P57678; - PhosphoSitePlus; P57678; - BioMuta; GEMIN4; - DMDM; 322510030; - EPD; P57678; - MaxQB; P57678; - PaxDb; P57678; - PeptideAtlas; P57678; - PRIDE; P57678; - ProteomicsDB; 57005; - DNASU; 50628; - Ensembl; ENST00000319004; ENSP00000321706; ENSG00000179409 GeneID; 50628; - KEGG; hsa:50628; - UCSC; uc002frs.2; human CTD; 50628; - DisGeNET; 50628; - EuPathDB; HostDB:ENSG00000179409.10; - GeneCards; GEMIN4; - H-InvDB; HIX0013389; - HGNC; HGNC:15717; GEMIN4 HPA; HPA065699; - HPA; HPA067891; - MIM; 606969; gene neXtProt; NX_P57678; - OpenTargets; ENSG00000179409; - eggNOG; ENOG410IET3; Eukaryota eggNOG; ENOG410XYXX; LUCA GeneTree; ENSGT00390000012296; - HOGENOM; HOG000143409; - HOVERGEN; HBG051720; - InParanoid; P57678; - KO; K13132; - OMA; LAWMECC; - OrthoDB; EOG091G010W; - PhylomeDB; P57678; - TreeFam; TF329445; - Reactome; R-HSA-191859; snRNP Assembly SIGNOR; P57678; - GeneWiki; GEMIN4; - GenomeRNAi; 50628; - PRO; PR:P57678; - Proteomes; UP000005640; Chromosome 17 Bgee; ENSG00000179409; - CleanEx; HS_GEMIN4; - ExpressionAtlas; P57678; baseline and differential Genevisible; P57678; HS GO; GO:0005737; C:cytoplasm; TAS:ProtInc GO; GO:0005829; C:cytosol; IDA:UniProtKB GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB GO; GO:0097504; C:Gemini of coiled bodies; IEA:UniProtKB-SubCell GO; GO:0016020; C:membrane; HDA:UniProtKB GO; GO:0016604; C:nuclear body; IDA:HPA GO; GO:0005730; C:nucleolus; TAS:ProtInc GO; GO:0005654; C:nucleoplasm; TAS:Reactome GO; GO:0030532; C:small nuclear ribonucleoprotein complex; TAS:ProtInc GO; GO:0032797; C:SMN complex; IDA:UniProtKB GO; GO:0034719; C:SMN-Sm protein complex; IDA:UniProtKB GO; GO:0051170; P:import into nucleus; TAS:Reactome GO; GO:0006364; P:rRNA processing; TAS:ProtInc GO; GO:0000387; P:spliceosomal snRNP assembly; IDA:UniProtKB InterPro; IPR033265; GEMIN4 PANTHER; PTHR15571; PTHR15571; 1 1: Evidence at protein level; Acetylation; Complete proteome; Cytoplasm; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Polymorphism; Reference proteome CHAIN 1 1058 Gem-associated protein 4 /FTId=PRO_0000087459 REGION 714 735 Leucine-zipper. MOD_RES 1 1 N-acetylmethionine MOD_RES 84 84 Phosphothreonine MOD_RES 86 86 Phosphoserine MOD_RES 205 205 Phosphoserine VARIANT 182 182 F -> L (in dbSNP:rs34604548) /FTId=VAR_056891 VARIANT 502 502 I -> V (in dbSNP:rs34616851) /FTId=VAR_056892 VARIANT 579 579 A -> G (in dbSNP:rs910925) /FTId=VAR_024317 VARIANT 684 684 R -> Q (in dbSNP:rs3744741) /FTId=VAR_021971 VARIANT 739 739 I -> T (in dbSNP:rs1062923) /FTId=VAR_056893 VARIANT 749 749 P -> L (in dbSNP:rs8078660) /FTId=VAR_056894 VARIANT 782 782 F -> L (in dbSNP:rs34452716) /FTId=VAR_056895 VARIANT 824 824 V -> F (in dbSNP:rs34936176) /FTId=VAR_056896 VARIANT 913 913 V -> I (in dbSNP:rs34610323) /FTId=VAR_056897 VARIANT 1033 1033 R -> C (in dbSNP:rs7813) /FTId=VAR_020390 CONFLICT 163 163 V -> I (in Ref. 1; AAF35283) CONFLICT 450 450 Q -> E (in Ref. 1; AAF35283 and 3; CAB45743). CONFLICT 593 593 E -> V (in Ref. 1; AAF35283 and 3; CAB45743). CONFLICT 713 713 Q -> P (in Ref. 1; AAF35283) CONFLICT 929 929 D -> N (in Ref. 1; AAF35283 and 3; CAB45755/CAB45743). SEQUENCE 1058 AA; 120037 MW; ACEC60EC19EF5081 CRC64; MDLGPLNICE EMTILHGGFL LAEQLFHPKA LAELTKSDWE RVGRPIVEAL REISSAAAHS QPFAWKKKAL IIIWAKVLQP HPVTPSDTET RWQEDLFFSV GNMIPTINHT ILFELLKSLE ASGLFIQLLM ALPTTICHAE LERFLEHVTV DTSAEDVAFF LDVWWEVMKH KGHPQDPLLS QFSAMAHKYL PALDEFPHPP KRLRSDPDAC PTMPLLAMLL RGLTQIQSRI LGPGRKCCAL ANLADMLTVF ALTEDDPQEV SATVYLDKLA TVISVWNSDT QNPYHQQALA EKVKEAERDV SLTSLAKLPS ETIFVGCEFL HHLLREWGEE LQAVLRSSQG TSYDSYRLCD SLTSFSQNAT LYLNRTSLSK EDRQVVSELA ECVRDFLRKT STVLKNRALE DITASIAMAV IQQKMDRHME VCYIFASEKK WAFSDEWVAC LGSNRALFRQ PDLVLRLLET VIDVSTADRA IPESQIRQVI HLILECYADL SLPGKNKVLA GILRSWGRKG LSEKLLAYVE GFQEDLNTTF NQLTQSASEQ GLAKAVASVA RLVIVHPEVT VKKMCSLAVV NLGTHKFLAQ ILTAFPALRF VEEQGPNSSA TFMVSCLKET VWMKFSTPKE EKQFLELLNC LMSPVKPQGI PVAALLEPDE VLKEFVLPFL RLDVEEVDLS LRIFIQTLEA NACREEYWLQ TCSPFPLLFS LCQLLDRFSK YWQLPKEKRC LSLDRKDLAI HILELLCEIV SANAETFSPD VWIKSLSWLH RKLEQLDWTV GLRLKSFFEG HFKCEVPATL FEICKLSEDE WTSQAHPGYG AGTGLLAWME CCCVSSGISE RMLSLLVVDV GNPEEVRLFS KGFLVALVQV MPWCSPQEWQ RLHQLTRRLL EKQLLHVPYS LEYIQFVPLL NLKPFAQELQ LSVLFLRTFQ FLCSHSCRDW LPLEGWNHVV KLLCGSLTRL LDSVRAIQAA GPWVQGPEQD LTQEALFVYT QVFCHALHIM AMLHPEVCEP LYVLALETLT CYETLSKTNP SVSSLLQRAH EQRFLKSIAE GIGPEERRQT LLQKMSSF|
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Provided below are standard protocols that you may find useful for product applications.
The product of this gene is part of a large complex localized to the cytoplasm, nucleoli, and to discrete nuclear bodies called Gemini bodies (gems). The complex functions in spliceosomal snRNP assembly in the cytoplasm, and regenerates spliceosomes required for pre-mRNA splicing in the nucleus. The encoded protein directly interacts with a DEAD box protein and several spliceosome core proteins. Alternatively spliced transcript variants have been described, but their biological validity has not been determined.
Kim, J.S., et al. Mol. Carcinog. 49(10):913-921(2010)
Wilker, E.H., et al. Environ. Health Perspect. 118(7):943-948(2010)
Boni, V., et al. Pharmacogenomics J. (2010) In press :
Clague, J., et al. Mol. Carcinog. 49(2):183-189(2010)
Ye, Y., et al. Cancer Prev Res (Phila) 1(6):460-469(2008)
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