Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Myosin-3 (Muscle embryonic myosin heavy chain) (Myosin heavy chain 3) (Myosin heavy chain, fast skeletal muscle, embryonic) (SMHCE)

 MYH3_HUMAN              Reviewed;        1940 AA.
P11055; Q15492;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
07-JUL-2009, sequence version 3.
25-OCT-2017, entry version 172.
RecName: Full=Myosin-3;
AltName: Full=Muscle embryonic myosin heavy chain;
AltName: Full=Myosin heavy chain 3;
AltName: Full=Myosin heavy chain, fast skeletal muscle, embryonic;
AltName: Full=SMHCE;
Name=MYH3;
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 VARIANT THR-1192.
PubMed=2726495; DOI=10.1093/nar/17.9.3591;
Eller M.S., Stedman H.H., Sylvester J.E., Fertels S.H.,
Rubinstein N.A., Kelly A.M., Sarkar S.;
"Nucleotide sequence of full length human embryonic myosin heavy chain
cDNA.";
Nucleic Acids Res. 17:3591-3592(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 774-1940, AND VARIANT THR-1192.
PubMed=2806546; DOI=10.1016/0014-5793(89)81710-7;
Eller M.S., Stedman H.H., Sylvester J.E., Fertels S.H., Wu Q.-L.,
Raychowdhury M.K., Rubinstein N.A., Kelly A.M., Sarkar S.;
"Human embryonic myosin heavy chain cDNA. Interspecies sequence
conservation of the myosin rod, chromosomal locus and isoform specific
transcription of the gene.";
FEBS Lett. 256:21-28(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 856-1940, AND VARIANT THR-1192.
TISSUE=Skeletal muscle;
PubMed=1691980; DOI=10.1111/j.1432-1033.1990.tb15459.x;
Bober E., Buchberger-Seidl A., Braun T., Singh S., Goedde H.W.,
Arnold H.H.;
"Identification of three developmentally controlled isoforms of human
myosin heavy chains.";
Eur. J. Biochem. 189:55-65(1990).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 856-1940, AND VARIANT THR-1192.
PubMed=2771643; DOI=10.1093/nar/17.15.6167;
Karsch-Mizrachi I., Travis M., Blau H., Leinwand L.A.;
"Expression and DNA sequence analysis of a human embryonic skeletal
muscle myosin heavy chain gene.";
Nucleic Acids Res. 17:6167-6179(1989).
[6]
INVOLVEMENT IN DA2A, INVOLVEMENT IN DA2B, VARIANTS DA2A GLY-498;
SER-583; CYS-672; HIS-672 AND ASP-825, VARIANTS DA2B PHE-261; CYS-292;
LYS-375; TYR-517; VAL-769 AND GLU-838; LEU-841 DEL, VARIANT DA2A/DA2B
ILE-178, AND VARIANTS ALA-1622 AND VAL-1637.
PubMed=16642020; DOI=10.1038/ng1775;
Toydemir R.M., Rutherford A., Whitby F.G., Jorde L.B., Carey J.C.,
Bamshad M.J.;
"Mutations in embryonic myosin heavy chain (MYH3) cause Freeman-
Sheldon syndrome and Sheldon-Hall syndrome.";
Nat. Genet. 38:561-565(2006).
[7]
INVOLVEMENT IN DA8, TISSUE SPECIFICITY, VARIANTS DA8 SER-243 DEL;
ASN-1072 INS AND PRO-1075, AND CLASSIFICATION OF VARIANTS ALA-1622 AND
VAL-1637.
PubMed=25957469; DOI=10.1016/j.ajhg.2015.04.004;
University of Washington Center for Mendelian Genomics;
Chong J.X., Burrage L.C., Beck A.E., Marvin C.T., McMillin M.J.,
Shively K.M., Harrell T.M., Buckingham K.J., Bacino C.A., Jain M.,
Alanay Y., Berry S.A., Carey J.C., Gibbs R.A., Lee B.H., Krakow D.,
Shendure J., Nickerson D.A., Bamshad M.J.;
"Autosomal-dominant multiple pterygium syndrome is caused by mutations
in MYH3.";
Am. J. Hum. Genet. 96:841-849(2015).
-!- FUNCTION: Muscle contraction.
-!- SUBUNIT: Muscle myosin is a hexameric protein that consists of 2
heavy chain subunits (MHC), 2 alkali light chain subunits (MLC)
and 2 regulatory light chain subunits (MLC-2).
-!- SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments
of the myofibrils.
-!- TISSUE SPECIFICITY: Expressed in fetal bone, thymus, placenta,
heart, brain, and liver. {ECO:0000269|PubMed:25957469}.
-!- DEVELOPMENTAL STAGE: Abundantly present in fetal skeletal muscle
and not present or barely detectable in heart and adult skeletal
muscle.
-!- DOMAIN: The rodlike tail sequence is highly repetitive, showing
cycles of a 28-residue repeat pattern composed of 4 heptapeptides,
characteristic for alpha-helical coiled coils.
-!- DOMAIN: Limited proteolysis of myosin heavy chain produces 1 light
meromyosin (LMM) and 1 heavy meromyosin (HMM). HMM can be further
cleaved into 2 globular subfragments (S1) and 1 rod-shaped
subfragment (S2). {ECO:0000305}.
-!- DISEASE: Arthrogryposis, distal, 2A (DA2A) [MIM:193700]: A form of
distal arthrogryposis, a disease characterized by congenital joint
contractures that mainly involve two or more distal parts of the
limbs, in the absence of a primary neurological or muscle disease.
DA2A is characterized by contractures of the hands and feet,
oropharyngeal abnormalities, scoliosis, and a distinctive face
that includes a very small oral orifice, puckered lips, and an H-
shaped dimple of the chin. {ECO:0000269|PubMed:16642020}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Arthrogryposis, distal, 2B (DA2B) [MIM:601680]: A form of
distal arthrogryposis, a disease characterized by congenital joint
contractures that mainly involve two or more distal parts of the
limbs, in the absence of a primary neurological or muscle disease.
DA2B is characterized by contractures of the hands and feet, and a
distinctive face characterized by prominent nasolabial folds,
small mouth and downslanting palpebral fissures.
{ECO:0000269|PubMed:16642020}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Arthrogryposis, distal, 8 (DA8) [MIM:178110]: A form of
distal arthrogryposis, a disease characterized by congenital joint
contractures that mainly involve two or more distal parts of the
limbs, in the absence of a primary neurological or muscle disease.
{ECO:0000269|PubMed:25957469}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
superfamily. Myosin family. {ECO:0000305}.
-!- CAUTION: Represents a conventional myosin. This protein should not
be confused with the unconventional myosin-3 (MYO3).
{ECO:0000305}.
-!- CAUTION: Variants Ala-1622 and Val-1637 have been originally
reported as DA2B pathogenic mutations (PubMed:16642020). These
variants are now thought to be polymorphisms on the basis of
additional family information and frequencies in large databases
of control populations (PubMed:25957469).
{ECO:0000269|PubMed:16642020, ECO:0000303|PubMed:25957469}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X13988; CAA32167.1; -; mRNA.
EMBL; AC002347; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X13100; CAA31492.1; -; mRNA.
EMBL; X51593; CAA35942.1; -; mRNA.
EMBL; X15696; CAA33731.1; -; mRNA.
CCDS; CCDS11157.1; -.
PIR; S04090; S04090.
RefSeq; NP_002461.2; NM_002470.3.
RefSeq; XP_011522172.1; XM_011523870.2.
RefSeq; XP_011522173.1; XM_011523871.2.
UniGene; Hs.440895; -.
ProteinModelPortal; P11055; -.
SMR; P11055; -.
BioGrid; 110706; 13.
IntAct; P11055; 10.
MINT; MINT-2801002; -.
STRING; 9606.ENSP00000226209; -.
iPTMnet; P11055; -.
PhosphoSitePlus; P11055; -.
BioMuta; MYH3; -.
DMDM; 251757455; -.
EPD; P11055; -.
MaxQB; P11055; -.
PaxDb; P11055; -.
PeptideAtlas; P11055; -.
PRIDE; P11055; -.
DNASU; 4621; -.
Ensembl; ENST00000583535; ENSP00000464317; ENSG00000109063.
GeneID; 4621; -.
KEGG; hsa:4621; -.
UCSC; uc002gmq.3; human.
CTD; 4621; -.
DisGeNET; 4621; -.
EuPathDB; HostDB:ENSG00000109063.14; -.
GeneCards; MYH3; -.
H-InvDB; HIX0039137; -.
HGNC; HGNC:7573; MYH3.
HPA; HPA021808; -.
MalaCards; MYH3; -.
MIM; 160720; gene.
MIM; 178110; phenotype.
MIM; 193700; phenotype.
MIM; 601680; phenotype.
neXtProt; NX_P11055; -.
OpenTargets; ENSG00000109063; -.
Orphanet; 1146; Digitotalar dysmorphism.
Orphanet; 2053; Freeman-Sheldon syndrome.
Orphanet; 1147; Sheldon-Hall syndrome.
PharmGKB; PA31370; -.
eggNOG; KOG0161; Eukaryota.
eggNOG; COG5022; LUCA.
GeneTree; ENSGT00760000118919; -.
HOGENOM; HOG000173959; -.
HOVERGEN; HBG004704; -.
InParanoid; P11055; -.
KO; K10352; -.
OMA; LGLQFQK; -.
OrthoDB; EOG091G07UM; -.
PhylomeDB; P11055; -.
TreeFam; TF314375; -.
Reactome; R-HSA-1445148; Translocation of GLUT4 to the plasma membrane.
Reactome; R-HSA-390522; Striated Muscle Contraction.
SIGNOR; P11055; -.
ChiTaRS; MYH3; human.
GeneWiki; MYH3; -.
GenomeRNAi; 4621; -.
PRO; PR:P11055; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000109063; -.
CleanEx; HS_MYH3; -.
Genevisible; P11055; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005859; C:muscle myosin complex; NAS:BHF-UCL.
GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
GO; GO:0030017; C:sarcomere; NAS:BHF-UCL.
GO; GO:0051015; F:actin filament binding; IMP:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042623; F:ATPase activity, coupled; IMP:BHF-UCL.
GO; GO:0005516; F:calmodulin binding; NAS:BHF-UCL.
GO; GO:0000146; F:microfilament motor activity; IMP:BHF-UCL.
GO; GO:0017018; F:myosin phosphatase activity; TAS:Reactome.
GO; GO:0030048; P:actin filament-based movement; NAS:UniProtKB.
GO; GO:0046034; P:ATP metabolic process; IMP:BHF-UCL.
GO; GO:0030326; P:embryonic limb morphogenesis; IC:BHF-UCL.
GO; GO:0060325; P:face morphogenesis; IC:BHF-UCL.
GO; GO:0030049; P:muscle filament sliding; TAS:Reactome.
GO; GO:0007517; P:muscle organ development; TAS:ProtInc.
GO; GO:0045214; P:sarcomere organization; NAS:BHF-UCL.
GO; GO:0003009; P:skeletal muscle contraction; IMP:BHF-UCL.
CDD; cd14913; MYSc_Myh3; 1.
Gene3D; 2.30.30.360; -; 1.
InterPro; IPR000048; IQ_motif_EF-hand-BS.
InterPro; IPR001609; Myosin_head_motor_dom.
InterPro; IPR004009; Myosin_N.
InterPro; IPR008989; Myosin_S1_N.
InterPro; IPR002928; Myosin_tail.
InterPro; IPR036000; MYSc_Myh3.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00063; Myosin_head; 1.
Pfam; PF02736; Myosin_N; 1.
Pfam; PF01576; Myosin_tail_1; 1.
PRINTS; PR00193; MYOSINHEAVY.
SMART; SM00242; MYSc; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50096; IQ; 1.
PROSITE; PS51456; MYOSIN_MOTOR; 1.
1: Evidence at protein level;
Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil;
Complete proteome; Cytoplasm; Disease mutation; Methylation;
Motor protein; Muscle protein; Myosin; Nucleotide-binding;
Polymorphism; Reference proteome; Thick filament.
CHAIN 1 1940 Myosin-3.
/FTId=PRO_0000123394.
DOMAIN 86 779 Myosin motor.
DOMAIN 782 811 IQ. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
NP_BIND 179 186 ATP. {ECO:0000255}.
REGION 656 678 Actin-binding.
REGION 758 772 Actin-binding.
COILED 840 1933 {ECO:0000255}.
MOD_RES 130 130 N6,N6,N6-trimethyllysine. {ECO:0000255}.
VARIANT 178 178 T -> I (in DA2A and DA2B;
dbSNP:rs121913619).
{ECO:0000269|PubMed:16642020}.
/FTId=VAR_030370.
VARIANT 243 243 Missing (in DA8).
{ECO:0000269|PubMed:25957469}.
/FTId=VAR_074668.
VARIANT 261 261 S -> F (in DA2B).
{ECO:0000269|PubMed:16642020}.
/FTId=VAR_030371.
VARIANT 292 292 S -> C (in DA2B; dbSNP:rs139480342).
{ECO:0000269|PubMed:16642020}.
/FTId=VAR_030372.
VARIANT 375 375 E -> K (in DA2B; dbSNP:rs121913621).
{ECO:0000269|PubMed:16642020}.
/FTId=VAR_030373.
VARIANT 498 498 E -> G (in DA2A).
{ECO:0000269|PubMed:16642020}.
/FTId=VAR_030374.
VARIANT 517 517 D -> Y (in DA2B).
{ECO:0000269|PubMed:16642020}.
/FTId=VAR_030375.
VARIANT 583 583 Y -> S (in DA2A).
{ECO:0000269|PubMed:16642020}.
/FTId=VAR_030376.
VARIANT 672 672 R -> C (in DA2A; dbSNP:rs121913618).
{ECO:0000269|PubMed:16642020}.
/FTId=VAR_030377.
VARIANT 672 672 R -> H (in DA2A; dbSNP:rs121913617).
{ECO:0000269|PubMed:16642020}.
/FTId=VAR_030378.
VARIANT 769 769 G -> V (in DA2B).
{ECO:0000269|PubMed:16642020}.
/FTId=VAR_030379.
VARIANT 825 825 V -> D (in DA2A; dbSNP:rs121913620).
{ECO:0000269|PubMed:16642020}.
/FTId=VAR_030380.
VARIANT 838 838 K -> E (in DA2B).
{ECO:0000269|PubMed:16642020}.
/FTId=VAR_030381.
VARIANT 841 841 Missing (in DA2B).
{ECO:0000269|PubMed:16642020}.
/FTId=VAR_030382.
VARIANT 1003 1003 A -> V (in dbSNP:rs34088014).
/FTId=VAR_056173.
VARIANT 1072 1072 N -> NN (in DA8).
{ECO:0000269|PubMed:25957469}.
/FTId=VAR_074669.
VARIANT 1075 1075 Q -> P (in DA8; dbSNP:rs796051884).
{ECO:0000269|PubMed:25957469}.
/FTId=VAR_074670.
VARIANT 1137 1137 R -> C (in dbSNP:rs12941197).
/FTId=VAR_030196.
VARIANT 1192 1192 A -> T (in dbSNP:rs2285477).
{ECO:0000269|PubMed:1691980,
ECO:0000269|PubMed:2726495,
ECO:0000269|PubMed:2771643,
ECO:0000269|PubMed:2806546}.
/FTId=VAR_030197.
VARIANT 1313 1313 T -> I (in dbSNP:rs35230241).
/FTId=VAR_056174.
VARIANT 1622 1622 D -> A (polymorphism; originally found in
DA2B patients).
{ECO:0000269|PubMed:16642020,
ECO:0000303|PubMed:25957469}.
/FTId=VAR_030383.
VARIANT 1637 1637 A -> V (polymorphism; originally found in
DA2B patients; dbSNP:rs34165480).
{ECO:0000269|PubMed:16642020,
ECO:0000303|PubMed:25957469}.
/FTId=VAR_030384.
CONFLICT 327 327 A -> R (in Ref. 1; CAA32167).
{ECO:0000305}.
CONFLICT 732 732 P -> L (in Ref. 1; CAA32167).
{ECO:0000305}.
CONFLICT 1331 1331 A -> G (in Ref. 4; CAA35942).
{ECO:0000305}.
CONFLICT 1391 1392 KK -> QE (in Ref. 1; CAA32167 and 3;
CAA31492). {ECO:0000305}.
CONFLICT 1608 1609 SR -> RA (in Ref. 4; CAA35942).
{ECO:0000305}.
CONFLICT 1663 1664 RG -> QT (in Ref. 3; CAA31492).
{ECO:0000305}.
SEQUENCE 1940 AA; 223905 MW; B7D6AF219E88E5C8 CRC64;
MSSDTEMEVF GIAAPFLRKS EKERIEAQNQ PFDAKTYCFV VDSKEEYAKG KIKSSQDGKV
TVETEDNRTL VVKPEDVYAM NPPKFDRIED MAMLTHLNEP AVLYNLKDRY TSWMIYTYSG
LFCVTVNPYK WLPVYNPEVV EGYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE
SGAGKTVNTK RVIQYFATIA ATGDLAKKKD SKMKGTLEDQ IISANPLLEA FGNAKTVRND
NSSRFGKFIR IHFGTTGKLA SADIETYLLE KSRVTFQLKA ERSYHIFYQI LSNKKPELIE
LLLITTNPYD YPFISQGEIL VASIDDAEEL LATDSAIDIL GFTPEEKSGL YKLTGAVMHY
GNMKFKQKQR EEQAEPDGTE VADKTAYLMG LNSSDLLKAL CFPRVKVGNE YVTKGQTVDQ
VHHAVNALSK SVYEKLFLWM VTRINQQLDT KLPRQHFIGV LDIAGFEIFE YNSLEQLCIN
FTNEKLQQFF NHHMFVLEQE EYKKEGIEWT FIDFGMDLAA CIELIEKPMG IFSILEEECM
FPKATDTSFK NKLYDQHLGK SNNFQKPKVV KGRAEAHFSL IHYAGTVDYS VSGWLEKNKD
PLNETVVGLY QKSSNRLLAH LYATFATADA DSGKKKVAKK KGSSFQTVSA LFRENLNKLM
SNLRTTHPHF VRCIIPNETK TPGAMEHSLV LHQLRCNGVL EGIRICRKGF PNRILYGDFK
QRYRVLNASA IPEGQFIDSK KACEKLLASI DIDHTQYKFG HTKVFFKAGL LGTLEEMRDD
RLAKLITRTQ AVCRGFLMRV EFQKMVQRRE SIFCIQYNIR SFMNVKHWPW MKLFFKIKPL
LKSAETEKEM ATMKEEFQKT KDELAKSEAK RKELEEKLVT LVQEKNDLQL QVQAESENLL
DAEERCDQLI KAKFQLEAKI KEVTERAEDE EEINAELTAK KRKLEDECSE LKKDIDDLEL
TLAKVEKEKH ATENKVKNLT EELSGLDETI AKLTREKKAL QEAHQQALDD LQAEEDKVNS
LNKTKSKLEQ QVEDLESSLE QEKKLRVDLE RNKRKLEGDL KLAQESILDL ENDKQQLDER
LKKKDFEYCQ LQSKVEDEQT LGLQFQKKIK ELQARIEELE EEIEAERATR AKTEKQRSDY
ARELEELSER LEEAGGVTST QIELNKKREA EFLKLRRDLE EATLQHEAMV AALRKKHADS
VAELGEQIDN LQRVKQKLEK EKSEFKLEID DLSSSMESVS KSKANLEKIC RTLEDQLSEA
RGKNEEIQRS LSELTTQKSR LQTEAGELSR QLEEKESIVS QLSRSKQAFT QQTEELKRQL
EEENKAKNAL AHALQSSRHD CDLLREQYEE EQEGKAELQR ALSKANSEVA QWRTKYETDA
IQRTEELEEA KKKLAQRLQD SEEQVEAVNA KCASLEKTKQ RLQGEVEDLM VDVERANSLA
AALDKKQRNF DKVLAEWKTK CEESQAELEA SLKESRSLST ELFKLKNAYE EALDQLETVK
RENKNLEQEI ADLTEQIAEN GKTIHELEKS RKQIELEKAD IQLALEEAEA ALEHEEAKIL
RIQLELTQVK SEIDRKIAEK DEEIEQLKRN YQRTVETMQS ALDAEVRSRN EAIRLKKKME
GDLNEIEIQL SHANRQAAET LKHLRSVQGQ LKDTQLHLDD ALRGQEDLKE QLAIVERRAN
LLQAEVEELR ATLEQTERAR KLAEQELLDS NERVQLLHTQ NTSLIHTKKK LETDLMQLQS
EVEDASRDAR NAEEKAKKAI TDAAMMAEEL KKEQDTSAHL ERMKKNLEQT VKDLQHRLDE
AEQLALKGGK KQIQKLETRI RELEFELEGE QKKNTESVKG LRKYERRVKE LTYQSEEDRK
NVLRLQDLVD KLQVKVKSYK RQAEEADEQA NAHLTKFRKA QHELEEAEER ADIAESQVNK
LRAKTRDFTS SRMVVHESEE


Related products :

Catalog number Product name Quantity
EIAAB25968 Homo sapiens,Human,Muscle embryonic myosin heavy chain,MYH3,Myosin heavy chain 3,Myosin heavy chain, fast skeletal muscle, embryonic,Myosin-3,SMHCE
EIAAB25969 Myh3,Myosin heavy chain 3,Myosin heavy chain, fast skeletal muscle, embryonic,Myosin-3,Rat,Rattus norvegicus
EIAAB25971 Chicken,Gallus gallus,MYH3,Myosin heavy chain 3,Myosin heavy chain, fast skeletal muscle, embryonic,Myosin-3
E0755h ELISA Homo sapiens,Human,MYH2,MyHC-2a,MyHC-IIa,MYHSA2,Myosin heavy chain 2,Myosin heavy chain 2a,Myosin heavy chain IIa,Myosin heavy chain, skeletal muscle, adult 2,Myosin-2 96T
E0755h ELISA kit Homo sapiens,Human,MYH2,MyHC-2a,MyHC-IIa,MYHSA2,Myosin heavy chain 2,Myosin heavy chain 2a,Myosin heavy chain IIa,Myosin heavy chain, skeletal muscle, adult 2,Myosin-2 96T
U0755h CLIA Homo sapiens,Human,MYH2,MyHC-2a,MyHC-IIa,MYHSA2,Myosin heavy chain 2,Myosin heavy chain 2a,Myosin heavy chain IIa,Myosin heavy chain, skeletal muscle, adult 2,Myosin-2 96T
EIAAB25977 Homo sapiens,Human,MYH4,MyHC-2b,MyHC-IIb,Myosin heavy chain 2b,Myosin heavy chain 4,Myosin heavy chain IIb,Myosin heavy chain, skeletal muscle, fetal,Myosin-4
EIAAB25976 MYH4,MyHC-2b,Myosin heavy chain 2b,Myosin heavy chain 4,Myosin heavy chain, skeletal muscle, juvenile,Myosin-4,Oryctolagus cuniculus,Rabbit
U0161b CLIA Bos taurus,Bovine,MYH1,MyHC-2x,Myosin heavy chain 1,Myosin heavy chain 2x,Myosin heavy chain, skeletal muscle, adult 1,Myosin-1 96T
U0161m CLIA Mouse,Mus musculus,Myh1,MyHC-2x,Myosin heavy chain 1,Myosin heavy chain 2x,Myosin heavy chain, skeletal muscle, adult 1,Myosin-1 96T
E0755b ELISA kit Bos taurus,Bovine,MYH2,MyHC-2a,Myosin heavy chain 2,Myosin heavy chain 2a,Myosin heavy chain, skeletal muscle, adult 2,Myosin-2 96T
E0161b ELISA kit Bos taurus,Bovine,MYH1,MyHC-2x,Myosin heavy chain 1,Myosin heavy chain 2x,Myosin heavy chain, skeletal muscle, adult 1,Myosin-1 96T
E0755b ELISA Bos taurus,Bovine,MYH2,MyHC-2a,Myosin heavy chain 2,Myosin heavy chain 2a,Myosin heavy chain, skeletal muscle, adult 2,Myosin-2 96T
E0161b ELISA Bos taurus,Bovine,MYH1,MyHC-2x,Myosin heavy chain 1,Myosin heavy chain 2x,Myosin heavy chain, skeletal muscle, adult 1,Myosin-1 96T
E0161m ELISA Mouse,Mus musculus,Myh1,MyHC-2x,Myosin heavy chain 1,Myosin heavy chain 2x,Myosin heavy chain, skeletal muscle, adult 1,Myosin-1 96T
E0161m ELISA kit Mouse,Mus musculus,Myh1,MyHC-2x,Myosin heavy chain 1,Myosin heavy chain 2x,Myosin heavy chain, skeletal muscle, adult 1,Myosin-1 96T
U0755b CLIA Bos taurus,Bovine,MYH2,MyHC-2a,Myosin heavy chain 2,Myosin heavy chain 2a,Myosin heavy chain, skeletal muscle, adult 2,Myosin-2 96T
U0161h CLIA Homo sapiens,Human,MYH1,MyHC-2x,MyHC-IIx_d,Myosin heavy chain 1,Myosin heavy chain 2x,Myosin heavy chain IIx_d,Myosin heavy chain, skeletal muscle, adult 1,Myosin-1 96T
E0161h ELISA kit Homo sapiens,Human,MYH1,MyHC-2x,MyHC-IIx_d,Myosin heavy chain 1,Myosin heavy chain 2x,Myosin heavy chain IIx_d,Myosin heavy chain, skeletal muscle, adult 1,Myosin-1 96T
E0161h ELISA Homo sapiens,Human,MYH1,MyHC-2x,MyHC-IIx_d,Myosin heavy chain 1,Myosin heavy chain 2x,Myosin heavy chain IIx_d,Myosin heavy chain, skeletal muscle, adult 1,Myosin-1 96T
E0755p ELISA kit MYH2,MyHC-2a,Myosin heavy chain 2,Myosin heavy chain 2a,Myosin heavy chain, skeletal muscle, adult 2,Myosin-2,Pig,Sus scrofa 96T
E0755p ELISA MYH2,MyHC-2a,Myosin heavy chain 2,Myosin heavy chain 2a,Myosin heavy chain, skeletal muscle, adult 2,Myosin-2,Pig,Sus scrofa 96T
U0755p CLIA MYH2,MyHC-2a,Myosin heavy chain 2,Myosin heavy chain 2a,Myosin heavy chain, skeletal muscle, adult 2,Myosin-2,Pig,Sus scrofa 96T
U0161p CLIA MYH1,MyHC-2x,Myosin heavy chain 1,Myosin heavy chain 2x,Myosin heavy chain, skeletal muscle, adult 1,Myosin-1,Pig,Sus scrofa 96T
E0161p ELISA kit MYH1,MyHC-2x,Myosin heavy chain 1,Myosin heavy chain 2x,Myosin heavy chain, skeletal muscle, adult 1,Myosin-1,Pig,Sus scrofa 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur