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Sterol regulatory element-binding protein cleavage-activating protein (SCAP) (SREBP cleavage-activating protein)

 SCAP_MOUSE              Reviewed;        1276 AA.
Q6GQT6; Q6A0A6; Q6NS67; Q7TNG7; Q80UI6;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
19-JUL-2004, sequence version 1.
12-SEP-2018, entry version 139.
RecName: Full=Sterol regulatory element-binding protein cleavage-activating protein;
Short=SCAP;
Short=SREBP cleavage-activating protein;
Name=Scap {ECO:0000312|MGI:MGI:2135958};
Synonyms=Kiaa0199 {ECO:0000312|EMBL:BAD32190.1};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000312|EMBL:BAD32190.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Fetal brain {ECO:0000312|EMBL:BAD32190.1};
PubMed=15368895; DOI=10.1093/dnares/11.3.205;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 11:205-218(2004).
[2] {ECO:0000312|EMBL:BAE27338.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE27338.1};
TISSUE=Embryonic heart {ECO:0000312|EMBL:BAE27338.1}, and
Macrophage {ECO:0000312|EMBL:BAE29431.1};
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3] {ECO:0000312|EMBL:AAH72633.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH72633.1}, and
FVB/N {ECO:0000312|EMBL:AAH55472.1};
TISSUE=Brain {ECO:0000312|EMBL:AAH72633.1},
Colon {ECO:0000312|EMBL:AAH55472.1}, and
Mammary gland {ECO:0000312|EMBL:AAH51066.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4] {ECO:0000305}
FUNCTION, AND MUTAGENESIS OF ASP-443.
PubMed=9854040; DOI=10.1172/JCI5341;
Korn B.S., Shimomura I., Bashmakov Y., Hammer R.E., Horton J.D.,
Goldstein J.L., Brown M.S.;
"Blunted feedback suppression of SREBP processing by dietary
cholesterol in transgenic mice expressing sterol-resistant
SCAP(D443N).";
J. Clin. Invest. 102:2050-2060(1998).
[5] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=11358865; DOI=10.1101/gad.891301;
Matsuda M., Korn B.S., Hammer R.E., Moon Y.-A., Komuro R.,
Horton J.D., Goldstein J.L., Brown M.S., Shimomura I.;
"SREBP cleavage-activating protein (SCAP) is required for increased
lipid synthesis in liver induced by cholesterol deprivation and
insulin elevation.";
Genes Dev. 15:1206-1216(2001).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-821 AND SER-934, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-821; SER-843 AND
SER-850, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1048, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[9]
UBIQUITINATION AT LYS-454 AND LYS-466, AND MUTAGENESIS OF LYS-454 AND
LYS-466.
PubMed=29068315; DOI=10.7554/eLife.28766;
Zhang L., Rajbhandari P., Priest C., Sandhu J., Wu X., Temel R.,
Castrillo A., de Aguiar Vallim T.Q., Sallam T., Tontonoz P.;
"Inhibition of cholesterol biosynthesis through RNF145-dependent
ubiquitination of SCAP.";
Elife 6:0-0(2017).
-!- FUNCTION: Escort protein required for cholesterol as well as lipid
homeostasis. Regulates export of the SCAP/SREBF complex from the
ER upon low cholesterol. Formation of a ternary complex with INSIG
at high sterol concentrations leads to masking of an ER-export
signal in SCAP and retention of the complex in the ER. Low sterol
concentrations trigger release of INSIG, a conformational change
in the SSC domain of SCAP, unmasking of the ER export signal,
recruitment into COPII-coated vesicles, transport to the Golgi
complex, proteolytic cleavage of SREBF in the Golgi, release of
the transcription factor fragment of SREBF from the membrane, its
import into the nucleus and up-regulation of LDLR, INSIG1 and the
mevalonate pathway. {ECO:0000250|UniProtKB:P97260,
ECO:0000269|PubMed:11358865, ECO:0000269|PubMed:9854040}.
-!- SUBUNIT: Membrane region forms a homotetramer. Forms a stable
complex with SREBF1/SREBP1 or SREBF2/SREBP2 through its C-terminal
cytoplasmic domain. Forms a ternary complex with INSIG1 or INSIG2
through its transmembrane domains at high sterol concentrations.
Interacts with the SEC23/SEC24 complex in a SAR1-GTP-dependent
manner through an ER export signal in its third cytoplasmic loop.
Binds cholesterol through its SSC domain. Component of SCAP/SREBP
complex composed of SREBF2, SCAP and RNF139; the complex hampers
the interaction between SCAP and SEC24B, thereby reducing SREBF2
proteolytic processing. Interacts with RNF139; the interaction
inhibits the interaction of SCAP with SEC24B and hampering the ER
to Golgi transport of the SCAP/SREBP complex (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:P97260}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P97260}. Golgi apparatus membrane
{ECO:0000250|UniProtKB:P97260}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P97260}. Cytoplasmic vesicle, COPII-coated
vesicle membrane {ECO:0000250|UniProtKB:P97260}; Multi-pass
membrane protein {ECO:0000250|UniProtKB:P97260}. Note=Moves from
the endoplasmic reticulum to the Golgi in the absence of sterols.
{ECO:0000250|UniProtKB:P97260}.
-!- DOMAIN: Cholesterol bound to SSC domain of SCAP or oxysterol bound
to INSIG1/2 leads to masking of an ER export signal on SCAP
possibly by moving the signal further away from the ER membrane.
{ECO:0000250|UniProtKB:P97260}.
-!- PTM: Ubiquitinated at Lys-454 and Lys-466. RNF145 triggers
ubiquitination of SCAP, likely inhibiting SCAP:SREBPF2 complex
transport to the Golgi apparatus and the subsequent
processing/maturation of SREBPF2. {ECO:0000269|PubMed:29068315}.
-!- DISRUPTION PHENOTYPE: Mice lacking Scap in their liver show an 80%
reduction in cholesterol and fatty acid synthesis in the liver as
well as a lack of regulation of target gene expression in response
to cholesterol deprivation or insulin elevation. Mice expressing
dominant negative mutant Scap in their liver show higher levels of
mature Srebf1 and Srebf2 as well as transcripts encoding proteins
involved in uptake and synthesis of cholesterol and fatty acids.
They show an 1.6-fold increase in liver size as well as a six-fold
increase in cholesterol and a nine-fold increase in triglyceride
content of the liver. Their plasma levels of cholesterol and
triglycerides are reduced by 50%. They show reduced down-
regulation of mature Srebf1/2 when fed a high cholesterol diet.
{ECO:0000269|PubMed:11358865}.
-!- SIMILARITY: Belongs to the WD repeat SCAP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD32190.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AK172912; BAD32190.1; ALT_INIT; Transcribed_RNA.
EMBL; AK146658; BAE27338.1; -; mRNA.
EMBL; AK150275; BAE29431.1; -; mRNA.
EMBL; AK152478; BAE31252.1; -; mRNA.
EMBL; AK153330; BAE31909.1; -; mRNA.
EMBL; BC051066; AAH51066.1; -; mRNA.
EMBL; BC055472; AAH55472.1; -; mRNA.
EMBL; BC069955; AAH69955.1; -; mRNA.
EMBL; BC070437; AAH70437.1; -; mRNA.
EMBL; BC072633; AAH72633.1; -; mRNA.
CCDS; CCDS23564.1; -.
RefSeq; NP_001001144.2; NM_001001144.3.
RefSeq; NP_001096632.1; NM_001103162.2.
RefSeq; XP_006512146.1; XM_006512083.2.
RefSeq; XP_006512147.1; XM_006512084.3.
RefSeq; XP_006512148.1; XM_006512085.3.
UniGene; Mm.288741; -.
ProteinModelPortal; Q6GQT6; -.
SMR; Q6GQT6; -.
BioGrid; 231694; 2.
DIP; DIP-61666N; -.
IntAct; Q6GQT6; 1.
STRING; 10090.ENSMUSP00000095953; -.
iPTMnet; Q6GQT6; -.
PhosphoSitePlus; Q6GQT6; -.
SwissPalm; Q6GQT6; -.
MaxQB; Q6GQT6; -.
PaxDb; Q6GQT6; -.
PeptideAtlas; Q6GQT6; -.
PRIDE; Q6GQT6; -.
Ensembl; ENSMUST00000098350; ENSMUSP00000095953; ENSMUSG00000032485.
GeneID; 235623; -.
KEGG; mmu:235623; -.
UCSC; uc009rtw.3; mouse.
CTD; 22937; -.
MGI; MGI:2135958; Scap.
eggNOG; KOG1933; Eukaryota.
eggNOG; ENOG410XR54; LUCA.
GeneTree; ENSGT00910000144151; -.
HOGENOM; HOG000230538; -.
HOVERGEN; HBG019538; -.
InParanoid; Q6GQT6; -.
OMA; GNFWQND; -.
OrthoDB; EOG091G04AA; -.
PhylomeDB; Q6GQT6; -.
TreeFam; TF315236; -.
Reactome; R-MMU-1655829; Regulation of cholesterol biosynthesis by SREBP (SREBF).
ChiTaRS; Scap; mouse.
PRO; PR:Q6GQT6; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032485; Expressed in 272 organ(s), highest expression level in primary oocyte.
CleanEx; MM_SCAP; -.
ExpressionAtlas; Q6GQT6; baseline and differential.
Genevisible; Q6GQT6; MM.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0015485; F:cholesterol binding; TAS:MGI.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0008203; P:cholesterol metabolic process; IDA:MGI.
GO; GO:0045540; P:regulation of cholesterol biosynthetic process; IMP:MGI.
GO; GO:0042304; P:regulation of fatty acid biosynthetic process; IMP:MGI.
GO; GO:0019217; P:regulation of fatty acid metabolic process; IDA:MGI.
GO; GO:0001666; P:response to hypoxia; IMP:MGI.
GO; GO:0032868; P:response to insulin; IMP:MGI.
GO; GO:0032933; P:SREBP signaling pathway; ISO:MGI.
Gene3D; 2.130.10.10; -; 2.
InterPro; IPR030225; SCAP.
InterPro; IPR000731; SSD.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
PANTHER; PTHR10796:SF127; PTHR10796:SF127; 1.
Pfam; PF12349; Sterol-sensing; 1.
Pfam; PF00400; WD40; 1.
SMART; SM00320; WD40; 6.
SUPFAM; SSF50978; SSF50978; 3.
PROSITE; PS50156; SSD; 1.
PROSITE; PS00678; WD_REPEATS_1; 1.
PROSITE; PS50082; WD_REPEATS_2; 1.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
Cholesterol metabolism; Complete proteome; Cytoplasmic vesicle;
Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Isopeptide bond;
Lipid metabolism; Membrane; Methylation; Phosphoprotein;
Reference proteome; Repeat; Steroid metabolism; Sterol metabolism;
Transmembrane; Transmembrane helix; Ubl conjugation; WD repeat.
CHAIN 1 1276 Sterol regulatory element-binding protein
cleavage-activating protein.
/FTId=PRO_0000315870.
TOPO_DOM 1 18 Cytoplasmic.
{ECO:0000250|UniProtKB:P97260}.
TRANSMEM 19 39 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 40 279 Lumenal. {ECO:0000250|UniProtKB:P97260}.
TRANSMEM 280 300 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 301 312 Cytoplasmic.
{ECO:0000250|UniProtKB:P97260}.
TRANSMEM 313 333 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 334 344 Lumenal. {ECO:0000250|UniProtKB:P97260}.
TRANSMEM 345 365 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 366 401 Cytoplasmic.
{ECO:0000250|UniProtKB:P97260}.
TRANSMEM 402 422 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 423 423 Lumenal. {ECO:0000250|UniProtKB:P97260}.
TRANSMEM 424 444 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 445 518 Cytoplasmic.
{ECO:0000250|UniProtKB:P97260}.
TRANSMEM 519 539 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 540 707 Lumenal. {ECO:0000250|UniProtKB:P97260}.
TRANSMEM 708 728 Helical; Name=8. {ECO:0000255}.
TOPO_DOM 729 1276 Cytoplasmic.
{ECO:0000250|UniProtKB:P97260}.
DOMAIN 284 442 SSD. {ECO:0000255|PROSITE-
ProRule:PRU00199}.
REPEAT 771 811 WD 1. {ECO:0000255}.
REPEAT 949 999 WD 2. {ECO:0000255}.
REPEAT 1002 1039 WD 3. {ECO:0000255}.
REPEAT 1074 1111 WD 4. {ECO:0000255}.
REPEAT 1114 1152 WD 5. {ECO:0000255}.
REPEAT 1155 1192 WD 6. {ECO:0000255}.
REPEAT 1194 1232 WD 7. {ECO:0000255}.
REGION 447 452 ER export signal.
{ECO:0000250|UniProtKB:P97260}.
REGION 731 1276 Interaction with SREBF2.
{ECO:0000250|UniProtKB:P97260}.
MOD_RES 821 821 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 837 837 Phosphoserine.
{ECO:0000250|UniProtKB:Q12770}.
MOD_RES 843 843 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 850 850 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 905 905 Phosphoserine.
{ECO:0000250|UniProtKB:Q12770}.
MOD_RES 934 934 Phosphoserine.
{ECO:0000244|PubMed:17242355}.
MOD_RES 1048 1048 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
CARBOHYD 263 263 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 590 590 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 641 641 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CROSSLNK 454 454 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:29068315}.
CROSSLNK 466 466 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:29068315}.
MUTAGEN 443 443 D->N: Higher level of processed SREBF1
and SREBF2 when expressed in liver.
{ECO:0000269|PubMed:9854040}.
MUTAGEN 454 454 K->R: Loss of ubiquitination; when
asociated with R-466.
{ECO:0000269|PubMed:29068315}.
MUTAGEN 466 466 K->R: Loss of ubiquitination; when
asociated with R-454.
{ECO:0000269|PubMed:29068315}.
CONFLICT 247 247 Missing (in Ref. 1; BAD32190).
{ECO:0000305}.
CONFLICT 619 619 P -> L (in Ref. 3; AAH70437).
{ECO:0000305}.
SEQUENCE 1276 AA; 139611 MW; 4EE7DDCEEB6F3331 CRC64;
MTLTERLREK ISQAFYNHGL LCASYPIPII LFTGLCILAC CYPLLKLPLP GTGPVEFSTP
VKGYSPPPAD SDHKQGEPSE QPEWYVGAPV AYIQQIFVKS SVSPWHRNLL AVDVFRSPLS
RAFQLVEEIR NHVLRDSSGT KSLEEVCLQV TDLLPGLRKL RSLLPEHGCL LLSPGNFWQN
DWERFHADPD IIGTIHQHEP KTLQTSATLK DLLFGVPGKY SGVSLYTRKR MVSYTITLVF
QRYHAKFLSS LRARLMLLHP SPNCSLRAEN LVHVHFKEEI GIAELIPLVT TYIILFAYIY
FSTRKIDMVK SKWGLALAAV VTVLSSLLMS VGLCTLFGLT PTLNGGEIFP YLVVVIGLEN
VLVLTKSVVS TPVDLEVKLR IAQGLSSESW SIMKNAATEL GIILIGYFTL VPAIQEFCLF
AVVGLVSDFF LQMLFFTTVL SIDIRRMELA DLNKRLPPES CLPSAKPVGR PARYERQQAV
RPSTPHTITL QPSSFRNLRL PKRLRVIYFL ARTRLAQRLI MAGTVVWIGI LVYTDPAGLR
TYLAAQVTEQ SPLGEGSLGP MPVPSGVLPA SHPDPAFSIF PPDAPKLPEN QTLPGELPEH
AGPAEGVHDS RAPEVTWGPE DEELWRKLSF RHWPTLFNYY NITLAKRYIS LLPVIPVTLH
LNPREALEGR HPQDGRSAWA PQEPLPAGLW ESGPKGPGGT QTHGDITLYK VAALGLAAGI
VLVLLLLCLY RVLCPRNYGQ PGGGPGRRRR GELPCDDYGY APPETEIVPL VLRGHLMDIE
CLASDGMLLV SCCLAGQVCV WDAQTGDCLT RIPRPGPRRD SCGGGAFETQ ENWERLSDGG
KASPEEPGDS PPLRRRPRGP PPPSLFGDQP DLTCLIDTNF SVQLPPEPTQ PEPRHRVGCG
RSRDSGYDFS RLVQRVYQEE GLAAMRMPAL RPPSPGPPLP QASQEEGTAP EKGSPPLAWT
PSTAGSIWSL ELQGNLIVVG RSSGRLEVWD AIEGVLCCSN EEISSGITAL VFLDRRIVAA
RLNGSLDFFS LETHTSLSPL QFRGTPGRGS SPSSSVYSSS NTVTCHRTHT VPCAHQKPIT
ALRAAAGRLV TGSQDHTLRV FRLDDSCCLF TLKGHSGAIT AVYIDQTMVL ASGGQDGAIC
LWDVLTGSRV SQTFAHRGDV TSLTCTASCV ISSGLDDFIS IWDRSTGIKL YSIQQDLGCG
ASLGVISDNL LVTGGQGCVS FWDLNYGDLL QTVYLGKNSE AQPARQILVL DNAAIVCNFG
SELSLVYVPS VLEKLD


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EIAAB37515 Rat,Rattus norvegicus,SCAP,Scap,SREBP cleavage-activating protein,Sterol regulatory element-binding protein cleavage-activating protein
EIAAB37519 Bos taurus,Bovine,SCAP,SCAP,SREBP cleavage-activating protein,Sterol regulatory element-binding protein cleavage-activating protein
EIAAB37517 Pig,SCAP,SCAP,SREBP cleavage-activating protein,Sterol regulatory element-binding protein cleavage-activating protein,Sus scrofa
H3302 Sterol regulatory element-binding protein cleavage-activating protein (SCAP), Rat, ELISA Kit 96T
H3301 Sterol regulatory element-binding protein cleavage-activating protein (SCAP), Pig, ELISA Kit 96T
CSB-EL020758RA Rat Sterol regulatory element-binding protein cleavage-activating protein(SCAP) ELISA kit 96T
CSB-EL020758RA Rat Sterol regulatory element-binding protein cleavage-activating protein(SCAP) ELISA kit SpeciesRat 96T
CSB-EL020758PI Pig Sterol regulatory element-binding protein cleavage-activating protein(SCAP) ELISA kit SpeciesPig 96T
H3300 Sterol regulatory element-binding protein cleavage-activating protein (SCAP), Mouse, ELISA Kit 96T
H3299 Sterol regulatory element-binding protein cleavage-activating protein (SCAP), Human, ELISA Kit 96T
CSB-EL020758HU Human Sterol regulatory element-binding protein cleavage-activating protein(SCAP) ELISA kit 96T
CSB-EL020758BO Bovine Sterol regulatory element-binding protein cleavage-activating protein(SCAP) ELISA kit 96T
H3298 Sterol regulatory element-binding protein cleavage-activating protein (SCAP), Bovine, ELISA Kit 96T
CSB-EL020758MO Mouse Sterol regulatory element-binding protein cleavage-activating protein(SCAP) ELISA kit 96T
SCAP_RAT ELISA Kit FOR Sterol regulatory element-binding protein cleavage-activating protein; organism: Rat; gene name: Scap 96T
CSB-EL020758BO Bovine Sterol regulatory element-binding protein cleavage-activating protein(SCAP) ELISA kit SpeciesBovine 96T
CSB-EL020758MO Mouse Sterol regulatory element-binding protein cleavage-activating protein(SCAP) ELISA kit SpeciesMouse 96T
CSB-EL020758HU Human Sterol regulatory element-binding protein cleavage-activating protein(SCAP) ELISA kit SpeciesHuman 96T
SCAP_MOUSE ELISA Kit FOR Sterol regulatory element-binding protein cleavage-activating protein; organism: Mouse; gene name: Scap 96T
SCAP_PIG Pig ELISA Kit FOR Sterol regulatory element-binding protein cleavage-activating protein 96T
EIAAB39839 ADD1,Adipocyte determination- and differentiation-dependent factor 1,Rat,Rattus norvegicus,Srebf1,Srebp1,SREBP-1,Sterol regulatory element-binding protein 1,Sterol regulatory element-binding transcrip
EIAAB39841 Mouse,Mus musculus,Srebf2,Srebp2,SREBP-2,Sterol regulatory element-binding protein 2,Sterol regulatory element-binding transcription factor 2
EIAAB39837 Mouse,Mus musculus,Srebf1,Srebp1,SREBP-1,Sterol regulatory element-binding protein 1,Sterol regulatory element-binding transcription factor 1


 

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