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ELISA Kit for Human Histone acetyltransferase p300

SKU : BHE13803372

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EIAAB SCIENCE INC, WUHAN

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Mfr.No.	E15334h
Alternative Names	E1A-associated protein p300 ; P300
Categories	Elisa
Function	Functions as histone acetyltransferase and regulates transcription via chromatin remodeling. Acetylates all four core histones in nucleosomes. Histone acetylation gives an epigenetic tag for transcriptional activation. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. Mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes. Acetylates the 'Lys-131' residue of ALX1 and acts as its coactivator in the presence of CREBBP. Acts as a TFAP2A-mediated transcriptional coactivator in presence of CITED2. Plays a role as a coactivator of NEUROD1-dependent transcription of the secretin and p21 genes and controls terminal differentiation of cells in the intestinal epithelium. Promotes cardiac myocyte enlargement.
Specificity	Natural and recombinant Human Histone acetyltransferase p300
Subcellular Location	Cytoplasm Nucleus In the presence of ALX1 relocalizes from the cytoplasm to the nucleus. Co-localizes with ROCK2 in the nucleus.
Detection Range	78-5000pg/mL
Entryname	EP300_HUMAN
Method Type	Sandwich
Platform	PF00439
Protein Name	Histone acetyltransferase p300
Sensitivity	39.4pg/mL
Sequence	50: MAENVVEPGP ; PSAKRPKLSS ; PALSASASDG ; TDFGSLFDLE ; HDLPDELINS ; 100: TELGLTNGGD ; INQLQTSLGM ; VQDAASKHKQ ; LSELLRSGSS ; PNLNMGVGGP ; 150: GQVMASQAQQ ; SSPGLGLINS ; MVKSPMTQAG ; LTSPNMGMGT ; SGPNQGPTQS ; 200: TGMMNSPVNQ ; PAMGMNTGMN ; AGMNPGMLAA ; GNGQGIMPNQ ; VMNGSIGAGR ; 250: GRQNMQYPNP ; GMGSAGNLLT ; EPLQQGSPQM ; GGQTGLRGPQ ; PLKMGMMNNP ; 300: NPYGSPYTQN ; PGQQIGASGL ; GLQIQTKTVL ; SNNLSPFAMD ; KKAVPGGGMP ; 350: NMGQQPAPQV ; QQPGLVTPVA ; QGMGSGAHTA ; DPEKRKLIQQ ; QLVLLLHAHK ; 400: CQRREQANGE ; VRQCNLPHCR ; TMKNVLNHMT ; HCQSGKSCQV ; AHCASSRQII ; 450: SHWKNCTRHD ; CPVCLPLKNA ; GDKRNQQPIL ; TGAPVGLGNP ; SSLGVGQQSA ; 500: PNLSTVSQID ; PSSIERAYAA ; LGLPYQVNQM ; PTQPQVQAKN ; QQNQQPGQSP ; 550: QGMRPMSNMS ; ASPMGVNGGV ; GVQTPSLLSD ; SMLHSAINSQ ; NPMMSENASV ; 600: PSLGPMPTAA ; QPSTTGIRKQ ; WHEDITQDLR ; NHLVHKLVQA ; IFPTPDPAAL ; 650: KDRRMENLVA ; YARKVEGDMY ; ESANNRAEYY ; HLLAEKIYKI ; QKELEEKRRT ; 700: RLQKQNMLPN ; AAGMVPVSMN ; PGPNMGQPQP ; GMTSNGPLPD ; PSMIRGSVPN ; 750: QMMPRITPQS ; GLNQFGQMSM ; AQPPIVPRQT ; PPLQHHGQLA ; QPGALNPPMG ; 800: YGPRMQQPSN ; QGQFLPQTQF ; PSQGMNVTNI ; PLAPSSGQAP ; VSQAQMSSSS ; 850: CPVNSPIMPP ; GSQGSHIHCP ; QLPQPALHQN ; SPSPVPSRTP ; TPHHTPPSIG ; 900: AQQPPATTIP ; APVPTPPAMP ; PGPQSQALHP ; PPRQTPTPPT ; TQLPQQVQPS ; 950: LPAAPSADQP ; QQQPRSQQST ; AASVPTPTAP ; LLPPQPATPL ; SQPAVSIEGQ ; 1000: VSNPPSTSST ; EVNSQAIAEK ; QPSQEVKMEA ; KMEVDQPEPA ; DTQPEDISES ; 1050: KVEDCKMEST ; ETEERSTELK ; TEIKEEEDQP ; STSATQSSPA ; PGQSKKKIFK ; 1100: PEELRQALMP ; TLEALYRQDP ; ESLPFRQPVD ; PQLLGIPDYF ; DIVKSPMDLS ; 1150: TIKRKLDTGQ ; YQEPWQYVDD ; IWLMFNNAWL ; YNRKTSRVYK ; YCSKLSEVFE ; 1200: QEIDPVMQSL ; GYCCGRKLEF ; SPQTLCCYGK ; QLCTIPRDAT ; YYSYQNRYHF ; 1250: CEKCFNEIQG ; ESVSLGDDPS ; QPQTTINKEQ ; FSKRKNDTLD ; PELFVECTEC ; 1300: GRKMHQICVL ; HHEIIWPAGF ; VCDGCLKKSA ; RTRKENKFSA ; KRLPSTRLGT ; 1350: FLENRVNDFL ; RRQNHPESGE ; VTVRVVHASD ; KTVEVKPGMK ; ARFVDSGEMA ; 1400: ESFPYRTKAL ; FAFEEIDGVD ; LCFFGMHVQE ; YGSDCPPPNQ ; RRVYISYLDS ; 1450: VHFFRPKCLR ; TAVYHEILIG ; YLEYVKKLGY ; TTGHIWACPP ; SEGDDYIFHC ; 1500: HPPDQKIPKP ; KRLQEWYKKM ; LDKAVSERIV ; HDYKDIFKQA ; TEDRLTSAKE ; 1550: LPYFEGDFWP ; NVLEESIKEL ; EQEEEERKRE ; ENTSNESTDV ; TKGDSKNAKK ; 1600: KNNKKTSKNK ; SSLSRGNKKK ; PGMPNVSNDL ; SQKLYATMEK ; HKEVFFVIRL ; 1650: IAGPAANSLP ; PIVDPDPLIP ; CDLMDGRDAF ; LTLARDKHLE ; FSSLRRAQWS ; 1700: TMCMLVELHT ; QSQDRFVYTC ; NECKHHVETR ; WHCTVCEDYD ; LCITCYNTKN ; 1750: HDHKMEKLGL ; GLDDESNNQQ ; AAATQSPGDS ; RRLSIQRCIQ ; SLVHACQCRN ; 1800: ANCSLPSCQK ; MKRVVQHTKG ; CKRKTNGGCP ; ICKQLIALCC ; YHAKHCQENK ; 1850: CPVPFCLNIK ; QKLRQQQLQH ; RLQQAQMLRR ; RMASMQRTGV ; VGQQQGLPSP ; 1900: TPATPTTPTG ; QQPTTPQTPQ ; PTSQPQPTPP ; NSMPPYLPRT ; QAAGPVSQGK ; 1950: AAGQVTPPTP ; PQTAQPPLPG ; PPPAAVEMAM ; QIQRAAETQR ; QMAHVQIFQR ; 2000: PIQHQMPPMT ; PMAPMGMNPP ; PMTRGPSGHL ; EPGMGPTGMQ ; QQPPWSQGGL ; 2050: PQPQQLQSGM ; PRPAMMSVAQ ; HGQPLNMAPQ ; PGLGQVGISP ; LKPGTVSQQA ; 2100: LQNLLRTLRS ; PSSPLQQQQV ; LSILHANPQL ; LAAFIKQRAA ; KYANSNPQPI ; 2150: PGQPGMPQGQ ; PGLQPPTMPG ; QQGVHSNPAM ; QNMNPMQAGV ; QRAGLPQQQP ; 2200: QQQLQPPMGG ; MSPQAQQMNM ; NHNTMPSQFR ; DILRRQQMMQ ; QQQQQGAGPG ; 2250: IGPGMANHNQ ; FQQPQGVGYP ; PQQQQRMQHH ; MQQMQQGNMG ; QIGQLPQALG ; 2300: AEAGASLQAY ; QQRLLQQQMG ; SPVQPNPMSP ; QQHMLPNQAQ ; SPHLQGQQIP ; 2350: NSLSNQVRSP ; QPVPSPRPQS ; QPPHSSPSPR ; MQPQPSPHHV ; SPQTSSPHPG ; 2400: LVAAQANPME ; QGHFASPDQN ; SMLSQLASNP ; GMANLHGASA ; TDLGLSTDNS ; 2414: DLNSNLSQST ; LDIH
Sequence Length	2414
String	Q09472
Sub Unit	Interacts with phosphorylated CREB1 (By similarity). Interacts with HIF1A; the interaction is stimulated in response to hypoxia and inhibited by CITED2. Interacts (via N-terminus) with TFAP2A (via N-terminus); the interaction requires CITED2. Interacts (via CH1 domain) with CITED2 (via C-terminus). Interacts with CITED1 (unphosphorylated form preferentially and via C-terminus). Interacts with ESR1; the interaction is estrogen-dependent and enhanced by CITED1. Interacts with DTX1, EID1, ELF3, FEN1, LEF1, NCOA1, NCOA6, NR3C1, PCAF, PELP1, PRDM6, SP1, SP3, SPIB, SRY, TCF7L2, TP53, SATB1, SRCAP, TTC5, JMY and TRERF1. The TAZ-type 1 domain interacts with HIF1A. Probably part of a complex with HIF1A and CREBBP. Part of a complex containing CARM1 and NCOA2/GRIP1. Interacts with ING4 and this interaction may be indirect. Interacts with ING5. Interacts with the C-terminal region of CITED4. Interacts with HTLV-1 Tax and p30II. Interacts with and acetylates HIV-1 Tat. Non-sumoylated EP300 preferentially interacts with SENP3. Interacts with SS18L1/CREST. Interacts with ALX1 (via homeobox domain). Interacts with NEUROD1; the interaction is inhibited by NR0B2. Interacts with TCF3. Interacts (via CREB-binding domain) with MYOCD (via C-terminus) (By similarity). Binds to HIPK2 (By similarity). Interacts with ROCK2 and PPARG. Forms a complex made of CDK9, CCNT1/cyclin-T1, EP300 and GATA4 that stimulates hypertrophy in cardiomyocytes.

Uniprot	Q09472
Gene Name	EP300
Immunogen Species	Homo Sapiens (Human)
Kegg	hsa:2033
Unigene	Hs.517517

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SKU	Supplier No.	Size	Your price	Quantity
BHE13803372	E15334h	96T	$736		Add to Cart

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