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

Tropomyosin alpha-1 chain (Alpha-tropomyosin) (Tropomyosin-1)

 TPM1_CHICK              Reviewed;         284 AA.
P04268; P02559; P08942; P18441; P18442; P49436; P49438; P49439;
Q540N4;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 2.
23-MAY-2018, entry version 139.
RecName: Full=Tropomyosin alpha-1 chain;
AltName: Full=Alpha-tropomyosin;
AltName: Full=Tropomyosin-1;
Name=TPM1;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
PROTEIN SEQUENCE (ISOFORM 1), AND ACETYLATION AT MET-1.
PubMed=3997866;
Lau S.Y.M., Sanders C., Smillie L.B.;
"Amino acid sequence of chicken gizzard gamma-tropomyosin.";
J. Biol. Chem. 260:7257-7263(1985).
[2]
NUCLEOTIDE SEQUENCE (ISOFORM 1).
PubMed=3671073; DOI=10.1093/nar/15.19.8105;
Gooding C., Reinach F.C., Macleod A.R.;
"Complete nucleotide sequence of the fast-twitch isoform of chicken
skeletal muscle alpha-tropomyosin.";
Nucleic Acids Res. 15:8105-8105(1987).
[3]
NUCLEOTIDE SEQUENCE (ISOFORMS 1; 2; 4; 5; 6 AND 7).
PubMed=1748294; DOI=10.1016/0378-1119(91)90323-4;
Lemonnier M., Balvay L., Mouly V., Libri D., Fiszman M.Y.;
"The chicken gene encoding the alpha isoform of tropomyosin of fast-
twitch muscle fibers: organization, expression and identification of
the major proteins synthesized.";
Gene 107:229-240(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4).
TISSUE=Body wall;
PubMed=7820856; DOI=10.1002/cm.970290104;
Fanning A.S., Wolenski J.S., Mooseker M.S., Izant J.G.;
"Differential regulation of skeletal muscle myosin-II and brush border
myosin-I enzymology and mechanochemistry by bacterially produced
tropomyosin isoforms.";
Cell Motil. Cytoskeleton 29:29-45(1994).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Heart, and Skeletal muscle;
Denz C.R., Zajdel R.W., Dube S., Dube D.K.;
"Identification, characterization, and expression of a novel alpha-
tropomyosin isoform in cardiac tissues in developing chicken.";
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Red jungle fowl;
PubMed=15592404; DOI=10.1038/nature03154;
Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C.,
Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E.,
Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W.,
Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A., Kremitzki C.,
Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E.,
Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J.,
Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M.,
Paton B., Smith J., Morrice D., Daniels L., Tempest H.G.,
Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V.,
Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J.,
van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J.,
Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H.,
Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S.,
Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J.,
Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H.,
Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C.,
Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C.,
Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P.,
King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S.,
Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S.,
Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S.,
Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z.,
Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J.,
Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z.,
Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J.,
Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G.,
Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D.,
Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G.,
Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A.,
Mardis E.R., Wilson R.K.;
"Sequence and comparative analysis of the chicken genome provide
unique perspectives on vertebrate evolution.";
Nature 432:695-716(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 24-284 (ISOFORM 1).
PubMed=7128591;
McLeod A.R.;
"Distinct alpha-tropomyosin mRNA sequences in chicken skeletal
muscle.";
Eur. J. Biochem. 126:293-297(1982).
[8]
NUCLEOTIDE SEQUENCE OF 189-213 (ISOFORM 4).
TISSUE=Muscle;
PubMed=2762137; DOI=10.1093/nar/17.13.5400;
Lemonnier M., Libri D., Fiszman M.Y.;
"Chick alpha tropomyosin gene contains three sets of mutually
exclusive alternatively spliced exons.";
Nucleic Acids Res. 17:5400-5400(1989).
[9]
INTERACTION WITH HRG.
PubMed=15313924; DOI=10.1158/0008-5472.CAN-04-0440;
Donate F., Juarez J.C., Guan X., Shipulina N.V., Plunkett M.L.,
Tel-Tsur Z., Shaw D.E., Morgan W.T., Mazar A.P.;
"Peptides derived from the histidine-proline domain of the histidine-
proline-rich glycoprotein bind to tropomyosin and have antiangiogenic
and antitumor activities.";
Cancer Res. 64:5812-5817(2004).
[10]
INTERACTION WITH HRG.
PubMed=15269838; DOI=10.1267/THRO04080403;
Guan X., Juarez J.C., Qi X., Shipulina N.V., Shaw D.E., Morgan W.T.,
McCrae K.R., Mazar A.P., Donate F.;
"Histidine-proline rich glycoprotein (HPRG) binds and transduces anti-
angiogenic signals through cell surface tropomyosin on endothelial
cells.";
Thromb. Haemost. 92:403-412(2004).
[11]
SUBUNIT.
PubMed=23832280; DOI=10.1007/s10974-013-9353-x;
Janco M., Suphamungmee W., Li X., Lehman W., Lehrer S.S., Geeves M.A.;
"Polymorphism in tropomyosin structure and function.";
J. Muscle Res. Cell Motil. 34:177-187(2013).
[12]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-81.
PubMed=11438684; DOI=10.1073/pnas.131219198;
Brown J.H., Kim K.H., Jun G., Greenfield N.J., Dominguez R.,
Volkmann N., Hitchcock-DeGregori S.E., Cohen C.;
"Deciphering the design of the tropomyosin molecule.";
Proc. Natl. Acad. Sci. U.S.A. 98:8496-8501(2001).
-!- FUNCTION: Binds to actin filaments in muscle and non-muscle cells.
Plays a central role, in association with the troponin complex, in
the calcium dependent regulation of vertebrate striated muscle
contraction. Smooth muscle contraction is regulated by interaction
with caldesmon. In non-muscle cells is implicated in stabilizing
cytoskeleton actin filaments. {ECO:0000250|UniProtKB:P09493}.
-!- SUBUNIT: Homodimer (PubMed:23832280). Heterodimer of an alpha
(TPM1, TPM3 or TPM4) and a beta (TPM2) chain (By similarity).
Interacts with HRG (via the HRR domain); the interaction
contributes to the antiangiogenic properties of the
histidine/proline-rich region (HRR) of HRG (PubMed:15269838,
PubMed:15313924). {ECO:0000250|UniProtKB:P04692,
ECO:0000269|PubMed:15269838, ECO:0000269|PubMed:15313924}.
-!- INTERACTION:
Q99LM3:Smtnl1 (xeno); NbExp=3; IntAct=EBI-8073544, EBI-8073484;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:P04692}. Note=Associates with F-actin
stress fibers. {ECO:0000250|UniProtKB:P04692}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=Fast-twitch skeletal muscle, CTm7;
IsoId=P04268-1; Sequence=Displayed;
Name=2; Synonyms=Smooth muscle;
IsoId=P04268-2; Sequence=VSP_006588, VSP_006590;
Name=4; Synonyms=Fibroblast F1;
IsoId=P04268-4; Sequence=VSP_006589, VSP_006590;
Name=5; Synonyms=Fibroblast F2;
IsoId=P04268-5; Sequence=VSP_006590;
Name=6; Synonyms=Brain major;
IsoId=P04268-6; Sequence=VSP_006587, VSP_006591;
Name=7; Synonyms=Brain minor;
IsoId=P04268-7; Sequence=VSP_006591;
-!- DOMAIN: The molecule is in a coiled coil structure that is formed
by 2 polypeptide chains. The sequence exhibits a prominent seven-
residues periodicity.
-!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M32441; AAA48610.1; -; mRNA.
EMBL; X57991; CAA41056.1; -; Genomic_DNA.
EMBL; X57993; CAA41056.1; JOINED; Genomic_DNA.
EMBL; X57994; CAA41056.1; JOINED; Genomic_DNA.
EMBL; X57995; CAA41056.1; JOINED; Genomic_DNA.
EMBL; M69144; AAA48577.1; -; Genomic_DNA.
EMBL; M69140; AAA48577.1; JOINED; Genomic_DNA.
EMBL; M69142; AAA48577.1; JOINED; Genomic_DNA.
EMBL; M69143; AAA48577.1; JOINED; Genomic_DNA.
EMBL; X16090; CAA34217.1; ALT_SEQ; Genomic_DNA.
EMBL; X57991; CAA41059.1; -; Genomic_DNA.
EMBL; X57993; CAA41059.1; JOINED; Genomic_DNA.
EMBL; X57994; CAA41059.1; JOINED; Genomic_DNA.
EMBL; X57996; CAA41059.1; JOINED; Genomic_DNA.
EMBL; X57991; CAA41058.1; -; Genomic_DNA.
EMBL; X57993; CAA41058.1; JOINED; Genomic_DNA.
EMBL; X57994; CAA41058.1; JOINED; Genomic_DNA.
EMBL; X57996; CAA41058.1; JOINED; Genomic_DNA.
EMBL; X57991; CAA41057.1; -; Genomic_DNA.
EMBL; X57993; CAA41057.1; JOINED; Genomic_DNA.
EMBL; X57994; CAA41057.1; JOINED; Genomic_DNA.
EMBL; X57996; CAA41057.1; JOINED; Genomic_DNA.
EMBL; M36336; AAA65120.1; -; mRNA.
EMBL; M36337; AAA65121.1; -; mRNA.
EMBL; AY150210; AAN75276.1; -; mRNA.
EMBL; AADN02040437; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AADN02040438; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; J00910; AAA49113.1; -; mRNA.
PIR; S24399; TMCHA.
PIR; S24400; TMCHS2.
PIR; S24401; S24401.
PIR; S24402; S24402.
RefSeq; NP_990732.1; NM_205401.1. [P04268-4]
RefSeq; XP_015134260.1; XM_015278774.1. [P04268-1]
RefSeq; XP_015134264.1; XM_015278778.1. [P04268-5]
RefSeq; XP_015134271.1; XM_015278785.1. [P04268-7]
UniGene; Gga.4108; -.
PDB; 1IC2; X-ray; 2.00 A; A/B/C/D=1-80.
PDB; 3MTU; X-ray; 2.10 A; A/B/C/D=1-29, E/F=257-284.
PDB; 3MUD; X-ray; 2.20 A; A/B=246-257, C/D=1-29.
PDB; 3U1A; X-ray; 2.00 A; A/B/C/D=1-81.
PDB; 3U1C; X-ray; 1.80 A; A/B=1-98.
PDBsum; 1IC2; -.
PDBsum; 3MTU; -.
PDBsum; 3MUD; -.
PDBsum; 3U1A; -.
PDBsum; 3U1C; -.
ProteinModelPortal; P04268; -.
SMR; P04268; -.
IntAct; P04268; 1.
MINT; P04268; -.
iPTMnet; P04268; -.
PRIDE; P04268; -.
Ensembl; ENSGALT00000005572; ENSGALP00000005562; ENSGALG00000003521. [P04268-1]
Ensembl; ENSGALT00000039589; ENSGALP00000038799; ENSGALG00000003521. [P04268-4]
Ensembl; ENSGALT00000060647; ENSGALP00000051797; ENSGALG00000003521. [P04268-5]
GeneID; 396366; -.
KEGG; gga:396366; -.
CTD; 7168; -.
GeneTree; ENSGT00550000074494; -.
HOVERGEN; HBG107404; -.
InParanoid; P04268; -.
KO; K10373; -.
OMA; QDKADTC; -.
PhylomeDB; P04268; -.
TreeFam; TF351519; -.
EvolutionaryTrace; P04268; -.
PRO; PR:P04268; -.
Proteomes; UP000000539; Chromosome 10.
Bgee; ENSGALG00000003521; -.
ExpressionAtlas; P04268; baseline and differential.
GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
GO; GO:0005884; C:actin filament; IBA:GO_Central.
GO; GO:0005862; C:muscle thin filament tropomyosin; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:AgBase.
GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
GO; GO:0008092; F:cytoskeletal protein binding; IPI:AgBase.
GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0008307; F:structural constituent of muscle; IBA:GO_Central.
GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
GO; GO:0060048; P:cardiac muscle contraction; IBA:GO_Central.
InterPro; IPR000533; Tropomyosin.
Pfam; PF00261; Tropomyosin; 1.
PRINTS; PR00194; TROPOMYOSIN.
PROSITE; PS00326; TROPOMYOSIN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Actin-binding; Alternative splicing;
Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
Direct protein sequencing; Muscle protein; Polymorphism;
Reference proteome.
CHAIN 1 284 Tropomyosin alpha-1 chain.
/FTId=PRO_0000205625.
COILED 1 284 {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000269|PubMed:3997866}.
VAR_SEQ 1 80 MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEERSKQLED
ELVALQKKLKGTEDELDKYSESLKDAQEKLELADKKATD
-> MAALSSLEAVRKKIRSLQEQADAAEERAGKLQREVDQE
RALREE (in isoform 6). {ECO:0000305}.
/FTId=VSP_006587.
VAR_SEQ 42 80 ELVALQKKLKGTEDELDKYSESLKDAQEKLELADKKATD
-> DIVQLEKQLRVTEDSRDQVLEELHKSEDSLLFAEENAA
K (in isoform 2). {ECO:0000305}.
/FTId=VSP_006588.
VAR_SEQ 189 212 KCAELEEELKTVTNNLKSLEAQAE -> QVRQLEEQLRIMD
QTLKALMAAED (in isoform 4).
{ECO:0000303|PubMed:7820856}.
/FTId=VSP_006589.
VAR_SEQ 258 284 DELYAQKLKYKAISEELDHALNDMTSI -> EKVAHAKEEN
LNMHQMLDQTLLELNNM (in isoform 2, isoform
4 and isoform 5).
{ECO:0000303|PubMed:7820856}.
/FTId=VSP_006590.
VAR_SEQ 259 284 ELYAQKLKYKAISEELDHALNDMTSI -> QLYQQLEQNSR
LTNELKLALNED (in isoform 6 and isoform
7). {ECO:0000305}.
/FTId=VSP_006591.
VARIANT 171 171 I -> V.
VARIANT 175 175 D -> E.
CONFLICT 34 34 E -> D (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 45 45 A -> S (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 63 63 S -> A (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 75 75 D -> E (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 83 84 SE -> AD (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 132 132 N -> S (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 157 157 E -> D (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 165 165 V -> A (in Ref. 2; AAA48610).
{ECO:0000305}.
CONFLICT 172 172 I -> L (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 174 174 G -> S (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 188 188 S -> G (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 229 229 T -> S (in Ref. 1; AA sequence).
{ECO:0000305}.
HELIX 1 96 {ECO:0000244|PDB:3U1C}.
HELIX 267 283 {ECO:0000244|PDB:3MTU}.
SEQUENCE 284 AA; 32766 MW; DBBBD3DB7F36DACB CRC64;
MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEERSKQLE DELVALQKKL KGTEDELDKY
SESLKDAQEK LELADKKATD AESEVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA
DESERGMKVI ENRAQKDEEK MEIQEIQLKE AKHIAEEADR KYEEVARKLV IIEGDLERAE
ERAELSESKC AELEEELKTV TNNLKSLEAQ AEKYSQKEDK YEEEIKVLTD KLKEAETRAE
FAERSVTKLE KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI


Related products :

Catalog number Product name Quantity
EIAAB43575 Gamma-tropomyosin,Homo sapiens,hTM5,Human,TPM3,Tropomyosin alpha-3 chain,Tropomyosin-3,Tropomyosin-5
EIAAB43571 Gamma-tropomyosin,Rat,Rattus norvegicus,Tpm3,Tpm5,Tpm-5,Tropomyosin alpha-3 chain,Tropomyosin-3,Tropomyosin-5
EIAAB43558 Alpha-tropomyosin,C15orf13,Homo sapiens,Human,TMSA,TPM1,Tropomyosin alpha-1 chain,Tropomyosin-1
EIAAB43564 Alpha-tropomyosin,Oryctolagus cuniculus,Rabbit,TPM1,TPMA,Tropomyosin alpha-1 chain,Tropomyosin-1
EIAAB43561 Alpha-tm,Alpha-tropomyosin,Rat,Rattus norvegicus,Tpm1,Tpma,Tropomyosin alpha-1 chain,Tropomyosin-1
EIAAB43563 Alpha-tropomyosin,Mouse,Mus musculus,Tpm1,Tpm-1,Tpma,Tropomyosin alpha-1 chain,Tropomyosin-1
EIAAB43574 Gamma-tropomyosin,Mouse,Mus musculus,Tpm3,Tpm5,Tpm-5,Tropomyosin alpha-3 chain,Tropomyosin-3
EIAAB43572 Bos taurus,Bovine,Gamma-tropomyosin,TPM3,Tropomyosin alpha-3 chain,Tropomyosin-3
EIAAB43573 Gamma-tropomyosin,Pig,Sus scrofa,TPM3,Tropomyosin alpha-3 chain,Tropomyosin-3
EIAAB43559 Alpha-tropomyosin,Bos taurus,Bovine,TPM1,Tropomyosin alpha-1 chain,Tropomyosin-1
EIAAB43560 Alpha-tropomyosin,Pig,Sus scrofa,TPM1,Tropomyosin alpha-1 chain,Tropomyosin-1
EIAAB43562 Alpha-tropomyosin,Chicken,Gallus gallus,TPM1,Tropomyosin alpha-1 chain,Tropomyosin-1
EIAAB43579 Mouse,Mus musculus,Tpm4,Tropomyosin alpha-4 chain,Tropomyosin-4
EIAAB43577 Rat,Rattus norvegicus,TM-4,Tpm4,Tropomyosin alpha-4 chain,Tropomyosin-4
EIAAB43576 Homo sapiens,Human,TM30p1,TPM4,Tropomyosin alpha-4 chain,Tropomyosin-4
EIAAB43578 Pig,Sus scrofa,TPM4,Tropomyosin alpha-4 chain,Tropomyosin-4
10-288-22239F Tropomyosin alpha-4 chain - Tropomyosin-4; TM30p1 0.1 mg
10-288-22239F Tropomyosin alpha-4 chain - Tropomyosin-4; TM30p1 0.05 mg
EIAAB43570 Beta-tropomyosin,Homo sapiens,Human,TMSB,TPM2,Tropomyosin beta chain,Tropomyosin-2
EIAAB43566 Beta-tropomyosin,Oryctolagus cuniculus,Rabbit,TPM2,Tropomyosin beta chain,Tropomyosin-2
EIAAB43569 Beta-tropomyosin,Bos taurus,Bovine,TPM2,Tropomyosin beta chain,Tropomyosin-2
EIAAB43568 Beta-tropomyosin,Mouse,Mus musculus,Tpm2,Tpm-2,Tropomyosin beta chain,Tropomyosin-2
EIAAB43567 Beta-tropomyosin,Rat,Rattus norvegicus,Tpm2,Tropomyosin beta chain,Tropomyosin-2
EIAAB43565 Beta-tropomyosin,Chicken,Gallus gallus,TPM2,Tropomyosin beta chain,Tropomyosin-2
30-382 TPM2 is beta-tropomyosin, an isoform of tropomyosin that is mainly expressed in slow, type 1 muscle fibers.The TPM2 gene encodes beta-tropomyosin, an isoform of tropomyosin that is mainly expressed in 0.1 mg


 

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