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Myristoylated alanine-rich C-kinase substrate (MARCKS) (Protein kinase C substrate, 80 kDa protein, light chain) (80K-L protein) (PKCSL)

 MARCS_HUMAN             Reviewed;         332 AA.
P29966; E1P560; Q2LA83; Q5TDB7;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
13-FEB-2019, entry version 170.
RecName: Full=Myristoylated alanine-rich C-kinase substrate;
Short=MARCKS;
AltName: Full=Protein kinase C substrate, 80 kDa protein, light chain;
Short=80K-L protein;
Short=PKCSL;
Name=MARCKS; Synonyms=MACS, PRKCSL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF
1-34.
PubMed=1860846;
Harlan D.M., Graff J.M., Stumpo D.J., Eddy R.L. Jr., Shows T.B.,
Boyle J.M., Blackshear P.J.;
"The human myristoylated alanine-rich C kinase substrate (MARCKS) gene
(MACS). Analysis of its gene product, promoter, and chromosomal
localization.";
J. Biol. Chem. 266:14399-14405(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1427823; DOI=10.1016/S0888-7543(05)80301-5;
Sakai K., Hirai M., Kudoh J., Minoshima S., Shimizu N.;
"Molecular cloning and chromosomal mapping of a cDNA encoding human
80K-L protein: major substrate for protein kinase C.";
Genomics 14:175-178(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-250 AND VAL-274.
NIEHS SNPs program;
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 189-322.
PubMed=1396720; DOI=10.1111/j.1432-1033.1992.tb17255.x;
Herget T., Brooks S.F., Broad S., Rozengurt E.;
"Relationship between the major protein kinase C substrates acidic 80-
kDa protein-kinase-C substrate (80K) and myristoylated alanine-rich C-
kinase substrate (MARCKS). Members of a gene family or equivalent
genes in different species.";
Eur. J. Biochem. 209:7-14(1992).
[8]
PHOSPHORYLATION AT SER-159; SER-163 AND SER-170.
PubMed=8557118; DOI=10.1016/0014-5793(95)01454-3;
Palmer R.H., Schonwasser D.C., Rahman D., Pappin D.J., Herget T.,
Parker P.J.;
"PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156
and serine 163.";
FEBS Lett. 378:281-285(1996).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-77; SER-101 AND
SER-170, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-46; SER-77;
SER-81; SER-118; THR-143; SER-145 AND THR-150, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-46; SER-101;
THR-150; SER-163; SER-167 AND SER-170, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-63; SER-77;
SER-81; SER-101; THR-150; SER-163 AND SER-170, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-101; THR-150 AND
SER-170, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-29; SER-101;
SER-135; SER-145; SER-147; SER-170 AND SER-314, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25255805; DOI=10.1038/ncomms5919;
Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U.,
Wright M.H., Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
"Global profiling of co- and post-translationally N-myristoylated
proteomes in human cells.";
Nat. Commun. 5:4919-4919(2014).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: MARCKS is the most prominent cellular substrate for
protein kinase C. This protein binds calmodulin, actin, and
synapsin. MARCKS is a filamentous (F) actin cross-linking protein.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
-!- PTM: Phosphorylation by PKC displaces MARCKS from the membrane. It
also inhibits the F-actin cross-linking activity.
{ECO:0000269|PubMed:8557118}.
-!- SIMILARITY: Belongs to the MARCKS family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/marcks/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MARCKSID50926ch6q21.html";
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EMBL; M68956; AAA59555.1; -; mRNA.
EMBL; M68955; AAA59554.1; -; Genomic_DNA.
EMBL; D10522; BAA01392.1; -; mRNA.
EMBL; DQ341274; ABC67467.1; -; Genomic_DNA.
EMBL; AL132660; CAI19942.1; -; Genomic_DNA.
EMBL; CH471051; EAW48258.1; -; Genomic_DNA.
EMBL; CH471051; EAW48259.1; -; Genomic_DNA.
EMBL; BC089040; AAH89040.1; -; mRNA.
CCDS; CCDS5101.1; -.
PIR; A38873; A38873.
RefSeq; NP_002347.5; NM_002356.6.
UniGene; Hs.519909; -.
UniGene; Hs.712658; -.
ProteinModelPortal; P29966; -.
BioGrid; 110257; 40.
ELM; P29966; -.
IntAct; P29966; 17.
MINT; P29966; -.
STRING; 9606.ENSP00000357624; -.
iPTMnet; P29966; -.
PhosphoSitePlus; P29966; -.
SwissPalm; P29966; -.
BioMuta; MARCKS; -.
DMDM; 76803798; -.
EPD; P29966; -.
jPOST; P29966; -.
MaxQB; P29966; -.
PaxDb; P29966; -.
PeptideAtlas; P29966; -.
PRIDE; P29966; -.
ProteomicsDB; 54612; -.
TopDownProteomics; P29966; -.
DNASU; 4082; -.
Ensembl; ENST00000612661; ENSP00000478061; ENSG00000277443.
GeneID; 4082; -.
KEGG; hsa:4082; -.
UCSC; uc032xir.2; human.
CTD; 4082; -.
DisGeNET; 4082; -.
EuPathDB; HostDB:ENSG00000277443.1; -.
GeneCards; MARCKS; -.
H-InvDB; HIX0006152; -.
HGNC; HGNC:6759; MARCKS.
HPA; CAB022062; -.
HPA; HPA054820; -.
HPA; HPA067595; -.
HPA; HPA069443; -.
MIM; 177061; gene.
neXtProt; NX_P29966; -.
OpenTargets; ENSG00000277443; -.
PharmGKB; PA30637; -.
eggNOG; ENOG410J04K; Eukaryota.
eggNOG; ENOG4111SZ0; LUCA.
GeneTree; ENSGT00730000111419; -.
HOGENOM; HOG000113482; -.
HOVERGEN; HBG081955; -.
InParanoid; P29966; -.
KO; K12561; -.
OMA; ARVGDFF; -.
OrthoDB; 1636177at2759; -.
TreeFam; TF332815; -.
Reactome; R-HSA-399997; Acetylcholine regulates insulin secretion.
SIGNOR; P29966; -.
ChiTaRS; MARCKS; human.
GeneWiki; MARCKS; -.
GenomeRNAi; 4082; -.
PRO; PR:P29966; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000277443; Expressed in 240 organ(s), highest expression level in forebrain.
Genevisible; P29966; HS.
GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
GO; GO:0032432; C:actin filament bundle; IEA:Ensembl.
GO; GO:0005938; C:cell cortex; IEA:Ensembl.
GO; GO:0005813; C:centrosome; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0042585; C:germinal vesicle; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0051015; F:actin filament binding; TAS:ProtInc.
GO; GO:0005516; F:calmodulin binding; TAS:ProtInc.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0005080; F:protein kinase C binding; IEA:Ensembl.
GO; GO:0051764; P:actin crosslink formation; IEA:Ensembl.
GO; GO:0051017; P:actin filament bundle assembly; IEA:Ensembl.
GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
InterPro; IPR002101; MARCKS.
PANTHER; PTHR14353; PTHR14353; 1.
Pfam; PF02063; MARCKS; 1.
PRINTS; PR00963; MARCKS.
PROSITE; PS00826; MARCKS_1; 1.
PROSITE; PS00827; MARCKS_2; 1.
1: Evidence at protein level;
Actin-binding; Calmodulin-binding; Complete proteome; Cytoplasm;
Cytoskeleton; Lipoprotein; Membrane; Myristate; Phosphoprotein;
Polymorphism; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:25255805}.
CHAIN 2 332 Myristoylated alanine-rich C-kinase
substrate.
/FTId=PRO_0000157148.
REGION 152 176 Calmodulin-binding (PSD).
MOD_RES 26 26 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 27 27 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 29 29 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 46 46 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 63 63 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 77 77 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 81 81 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 101 101 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 118 118 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 128 128 Phosphoserine.
{ECO:0000250|UniProtKB:P30009}.
MOD_RES 135 135 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 143 143 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 145 145 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 147 147 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 150 150 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 159 159 Phosphoserine; by PKC.
{ECO:0000269|PubMed:8557118}.
MOD_RES 163 163 Phosphoserine; by PKC.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000269|PubMed:8557118}.
MOD_RES 167 167 Phosphoserine; by PKC.
{ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:20068231}.
MOD_RES 170 170 Phosphoserine; by PKC.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:8557118}.
MOD_RES 262 262 Phosphoserine.
{ECO:0000250|UniProtKB:P26645}.
MOD_RES 314 314 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:25255805}.
VARIANT 250 250 P -> L (in dbSNP:rs45593337).
{ECO:0000269|Ref.3}.
/FTId=VAR_025825.
VARIANT 274 274 A -> V (in dbSNP:rs3734458).
{ECO:0000269|Ref.3}.
/FTId=VAR_025826.
CONFLICT 84 84 A -> S (in Ref. 2; BAA01392).
{ECO:0000305}.
CONFLICT 119 119 P -> A (in Ref. 2; BAA01392).
{ECO:0000305}.
CONFLICT 225 225 G -> R (in Ref. 7). {ECO:0000305}.
CONFLICT 234 234 P -> S (in Ref. 1; AAA59555).
{ECO:0000305}.
CONFLICT 235 235 Q -> E (in Ref. 7). {ECO:0000305}.
CONFLICT 287 308 PGAPPEQEAAPAEEPAAAAASS -> LVCPRRGGSPRGGAR
GRRSLNQ (in Ref. 1; AAA59555).
{ECO:0000305}.
SEQUENCE 332 AA; 31555 MW; 0AB247801EF8FCBF CRC64;
MGAQFSKTAA KGEAAAERPG EAAVASSPSK ANGQENGHVK VNGDASPAAA ESGAKEELQA
NGSAPAADKE EPAAAGSGAA SPSAAEKGEP AAAAAPEAGA SPVEKEAPAE GEAAEPGSPT
AAEGEAASAA SSTSSPKAED GATPSPSNET PKKKKKRFSF KKSFKLSGFS FKKNKKEAGE
GGEAEAPAAE GGKDEAAGGA AAAAAEAGAA SGEQAAAPGE EAAAGEEGAA GGDPQEAKPQ
EAAVAPEKPP ASDETKAAEE PSKVEEKKAE EAGASAAACE APSAAGPGAP PEQEAAPAEE
PAAAAASSAC AAPSQEAQPE CSPEAPPAEA AE


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EIAAB25423 Homo sapiens,Human,MacMARCKS,Mac-MARCKS,Macrophage myristoylated alanine-rich C kinase substrate,MARCKSL1,MARCKS-like protein 1,MARCKS-related protein,MLP,MRP
18-785-210260 MARCKS (Phospho-Ser158) - MARCKS; Protein kinase C substrate. 80 kDa protein. light chain; PKCSL; 80K-L protein Polyclonal 0.1 mg
18-785-210260 MARCKS (Phospho-Ser158) - MARCKS; Protein kinase C substrate. 80 kDa protein. light chain; PKCSL; 80K-L protein Polyclonal 0.05 mg
DL-MARCKS-Hu Human Myristoylated Alanine Rich Protein Kinase C Substrate (MARCKS) ELISA Kit 96T
18-785-210262 MARCKS (Ab-158) - MARCKS; Protein kinase C substrate. 80 kDa protein. light chain; PKCSL; 80K-L protein Polyclonal 0.05 mg
18-785-210262 MARCKS (Ab-158) - MARCKS; Protein kinase C substrate. 80 kDa protein. light chain; PKCSL; 80K-L protein Polyclonal 0.1 mg
18-785-210261 MARCKS (Ab-162) - MARCKS; Protein kinase C substrate. 80 kDa protein. light chain; PKCSL; 80K-L protein Polyclonal 0.1 mg
18-785-210261 MARCKS (Ab-162) - MARCKS; Protein kinase C substrate. 80 kDa protein. light chain; PKCSL; 80K-L protein Polyclonal 0.05 mg
E97688Hu ELISA Kit for Myristoylated Alanine Rich Protein Kinase C Substrate (MARCKS) 96T/Kit
MARCO MARCKS Gene myristoylated alanine-rich protein kinase C substrate
QY-E01553 Human Myristoylated Alanine Rich Protein Kinase C Substrate(MARCKS)ELISA Kit 96T
201-12-3018 Human Myristoylated Alanine Rich Protein Kinase C Substrate(MARCKS)ELISA Kit 96T
UB-E01553 Human Myristoylated Alanine Rich Protein Kinase C Substrate(MARCKS)ELISA Kit 96T
SEH688Hu ELISA Kit for Myristoylated Alanine Rich Protein Kinase C Substrate (MARCKS) Homo sapiens (Human) 96T
E97688Hu ELISA Kit for Myristoylated Alanine Rich Protein Kinase C Substrate (MARCKS) Organism: Homo sapiens (Human) 96T
CSB-EL013493RA Rat myristoylated alanine-rich protein kinase C substrate (MARCKS) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL013493BO Bovine myristoylated alanine-rich protein kinase C substrate (MARCKS) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
CSB-EL013493CH Chicken myristoylated alanine-rich protein kinase C substrate (MARCKS) ELISA kit, Species Chicken, Sample Type serum, plasma 96T
CSB-EL013493MO Mouse myristoylated alanine-rich protein kinase C substrate (MARCKS) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL013493HU Human myristoylated alanine-rich protein kinase C substrate (MARCKS) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL013493RA Rat Myristoylated alanine-rich C-kinase substrate(MARCKS) ELISA kit 96T

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