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Caveolin-3 (M-caveolin)

 CAV3_HUMAN              Reviewed;         151 AA.
P56539; A8K777; Q3T1A4;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 1.
23-MAY-2018, entry version 176.
RecName: Full=Caveolin-3;
AltName: Full=M-caveolin;
Name=CAV3;
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 VARIANTS LGMD1C 64-THR--THR-66 DEL AND
LEU-105.
PubMed=9537420; DOI=10.1038/ng0498-365;
Minetti C., Sotgia F., Bruno C., Scartezzini P., Broda P., Bado M.,
Masetti E., Mazzocco M., Egeo A., Donati M.A., Volonte D.,
Galbiati F., Cordone G., Bricarelli F.D., Lisanti M.P., Zara F.;
"Mutations in the caveolin-3 gene cause autosomal dominant limb-girdle
muscular dystrophy.";
Nat. Genet. 18:365-368(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Skeletal muscle;
PubMed=9545514; DOI=10.1016/S0925-4439(97)00095-1;
Biederer C., Ries S., Drobnik W., Schmitz G.;
"Molecular cloning of human caveolin 3.";
Biochim. Biophys. Acta 1406:5-9(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANTS SER-56 AND
TRP-72.
PubMed=9536092; DOI=10.1093/hmg/7.5.871;
McNally E.M., de Sa Moreira E., Duggan D.J., Bonnemann C.G.,
Lisanti M.P., Lidov H.G.W., Vainzof M., Passos-Bueno M.R.,
Hoffman E.P., Zatz M., Kunkel L.M.;
"Caveolin-3 in muscular dystrophy.";
Hum. Mol. Genet. 7:871-877(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skeletal muscle;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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]
INTERACTION WITH DAG1.
PubMed=10988290; DOI=10.1074/jbc.M005321200;
Sotgia F., Lee J.K., Das K., Bedford M., Petrucci T.C., Macioce P.,
Sargiacomo M., Bricarelli F.D., Minetti C., Sudol M., Lisanti M.P.;
"Caveolin-3 directly interacts with the C-terminal tail of beta
-dystroglycan. Identification of a central WW-like domain within
caveolin family members.";
J. Biol. Chem. 275:38048-38058(2000).
[8]
INTERACTION WITH DYSF, AND VARIANT LGMD1C PRO-64.
PubMed=11532985; DOI=10.1093/hmg/10.17.1761;
Matsuda C., Hayashi Y.K., Ogawa M., Aoki M., Murayama K., Nishino I.,
Nonaka I., Arahata K., Brown R.H. Jr.;
"The sarcolemmal proteins dysferlin and caveolin-3 interact in
skeletal muscle.";
Hum. Mol. Genet. 10:1761-1766(2001).
[9]
FUNCTION.
PubMed=19262564; DOI=10.1038/emboj.2009.46;
McMahon K.A., Zajicek H., Li W.P., Peyton M.J., Minna J.D.,
Hernandez V.J., Luby-Phelps K., Anderson R.G.;
"SRBC/cavin-3 is a caveolin adapter protein that regulates caveolae
function.";
EMBO J. 28:1001-1015(2009).
[10]
SUMOYLATION AT LYS-38.
PubMed=21362625; DOI=10.1074/jbc.M110.214270;
Fuhs S.R., Insel P.A.;
"Caveolin-3 undergoes SUMOylation by the SUMO E3 ligase PIASy:
sumoylation affects G-protein-coupled receptor desensitization.";
J. Biol. Chem. 286:14830-14841(2011).
[11]
INTERACTION WITH CAVIN1; CAVIN2 AND CAVIN4.
PubMed=24567387; DOI=10.1073/pnas.1315359111;
Ogata T., Naito D., Nakanishi N., Hayashi Y.K., Taniguchi T.,
Miyagawa K., Hamaoka T., Maruyama N., Matoba S., Ikeda K., Yamada H.,
Oh H., Ueyama T.;
"MURC/Cavin-4 facilitates recruitment of ERK to caveolae and
concentric cardiac hypertrophy induced by alpha1-adrenergic
receptors.";
Proc. Natl. Acad. Sci. U.S.A. 111:3811-3816(2014).
[12]
INTERACTION WITH CAVIN4.
PubMed=26497963; DOI=10.1152/ajpheart.00446.2015;
Naito D., Ogata T., Hamaoka T., Nakanishi N., Miyagawa K.,
Maruyama N., Kasahara T., Taniguchi T., Nishi M., Matoba S.,
Ueyama T.;
"The coiled-coil domain of MURC/cavin-4 is involved in membrane
trafficking of caveolin-3 in cardiomyocytes.";
Am. J. Physiol. 309:H2127-H2136(2015).
[13]
VARIANT LGMD1C THR-46.
PubMed=11001938; DOI=10.1093/oxfordjournals.hmg.a018926;
Herrmann R., Straub V., Blank M., Kutzick C., Franke N., Jacob E.N.,
Lenard H.-G., Kroger S., Voit T.;
"Dissociation of the dystroglycan complex in caveolin-3-deficient limb
girdle muscular dystrophy.";
Hum. Mol. Genet. 9:2335-2340(2000).
[14]
VARIANT HYPCK GLN-27.
PubMed=10746614; DOI=10.1212/WNL.54.6.1373;
Carbone I., Bruno C., Sotgia F., Bado M., Broda P., Masetti E.,
Panella A., Zara F., Bricarelli F.D., Cordone G., Lisanti M.P.,
Minetti C.;
"Mutation in the CAV3 gene causes partial caveolin-3 deficiency and
hyperCKemia.";
Neurology 54:1373-1376(2000).
[15]
VARIANTS SER-56; TRP-72 AND HIS-126.
PubMed=11251997;
DOI=10.1002/1096-8628(2001)9999:9999<::AID-AJMG1168>3.0.CO;2-O;
de Paula F., Vainzof M., Bernardino A.L.F., McNally E., Kunkel L.M.,
Zatz M.;
"Mutations in the caveolin-3 gene: when are they pathogenic?";
Am. J. Med. Genet. 99:303-307(2001).
[16]
INVOLVEMENT IN RMD2, VARIANTS RMD2 GLN-27; THR-46; VAL-46 AND LEU-105,
AND CHARACTERIZATION OF VARIANT RMD2 THR-46.
PubMed=11431690; DOI=10.1038/90050;
Betz R.C., Schoser B.G.H., Kasper D., Ricker K., Ramirez A., Stein V.,
Torbergsen T., Lee Y.-A., Nothen M.M., Wienker T.F., Malin J.-P.,
Propping P., Reis A., Mortier W., Jentsch T.J., Vorgerd M.,
Kubisch C.;
"Mutations in CAV3 cause mechanical hyperirritability of skeletal
muscle in rippling muscle disease.";
Nat. Genet. 28:218-219(2001).
[17]
INVOLVEMENT IN RMD2, AND VARIANT RMD2 GLN-27.
PubMed=11756609; DOI=10.1212/WNL.57.12.2273;
Vorgerd M., Ricker K., Ziemssen F., Kress W., Goebel H.H., Nix W.A.,
Kubisch C., Schoser B.G.H., Mortier W.;
"A sporadic case of rippling muscle disease caused by a de novo
caveolin-3 mutation.";
Neurology 57:2273-2277(2001).
[18]
VARIANT HYPCK LEU-29.
PubMed=12082049; DOI=10.1136/jnnp.73.1.65;
Merlini L., Carbone I., Capanni C., Sabatelli P., Tortorelli S.,
Sotgia F., Lisanti M.P., Bruno C., Minetti C.;
"Familial isolated hyperCKaemia associated with a new mutation in the
caveolin-3 (CAV-3) gene.";
J. Neurol. Neurosurg. Psych. 73:65-67(2002).
[19]
ERRATUM.
Merlini L., Carbone I., Capanni C., Sabatelli P., Tortorelli S.,
Sotgia F., Lisanti M.P., Bruno C., Minetti C.;
J. Neurol. Neurosurg. Psych. 74:142-142(2003).
[20]
VARIANT MPDT GLN-27.
PubMed=11805270; DOI=10.1212/WNL.58.2.323;
Tateyama M., Aoki M., Nishino I., Hayashi Y.K., Sekiguchi S.,
Shiga Y., Takahashi T., Onodera Y., Haginoya K., Kobayashi K.,
Iinuma K., Nonaka I., Arahata K., Itoyama Y.;
"Mutation in the caveolin-3 gene causes a peculiar form of distal
myopathy.";
Neurology 58:323-325(2002).
[21]
ERRATUM.
Tateyama M., Aoki M., Nishino I., Hayashi Y.K., Sekiguchi S.,
Shiga Y., Takahashi T., Onodera Y., Haginoya K., Kobayashi K.,
Iinuma K., Nonaka I., Arahata K., Itoyama Y.;
Neurology 58:839-839(2002).
[22]
VARIANT RMD2 GLU-28, AND VARIANT LGMD1C GLU-28.
PubMed=12557291; DOI=10.1002/ana.10442;
Fischer D., Schroers A., Blumcke I., Urbach H., Zerres K., Mortier W.,
Vorgerd M., Schroder R.;
"Consequences of a novel caveolin-3 mutation in a large German
family.";
Ann. Neurol. 53:233-241(2003).
[23]
VARIANTS RMD2 PRO-87 AND THR-93.
PubMed=12666119; DOI=10.1002/ana.10501;
Kubisch C., Schoser B.G.H., von Duering M., Betz R.C., Goebel H.-H.,
Zahn S., Ehrbrecht A., Aasly J., Schroers A., Popovic N.,
Lochmueller H., Schroeder J.M., Bruening T., Malin J.-P., Fricke B.,
Meinck H.-M., Torbergsen T., Engels H., Voss B., Vorgerd M.;
"Homozygous mutations in caveolin-3 cause a severe form of rippling
muscle disease.";
Ann. Neurol. 53:512-520(2003).
[24]
VARIANT LGMD1C GLN-27.
PubMed=12939441; DOI=10.1212/01.WNL.0000076486.57572.5C;
Figarella-Branger D., Pouget J., Bernard R., Krahn M., Fernandez C.,
Levy N., Pellissier J.F.;
"Limb-girdle muscular dystrophy in a 71-year-old woman with an R27Q
mutation in the CAV3 gene.";
Neurology 61:562-564(2003).
[25]
VARIANT HYPCK PHE-97 DEL.
PubMed=14663034; DOI=10.1212/01.WNL.0000097320.35982.03;
Cagliani R., Bresolin N., Prelle A., Gallanti A., Fortunato F.,
Sironi M., Ciscato P., Fagiolari G., Bonato S., Galbiati S., Corti S.,
Lamperti C., Moggio M., Comi G.P.;
"A CAV3 microdeletion differentially affects skeletal muscle and
myocardium.";
Neurology 61:1513-1519(2003).
[26]
VARIANT CMH SER-64.
PubMed=14672715; DOI=10.1016/j.bbrc.2003.11.101;
Hayashi T., Arimura T., Ueda K., Shibata H., Hohda S., Takahashi M.,
Hori H., Koga Y., Oka N., Imaizumi T., Yasunami M., Kimura A.;
"Identification and functional analysis of a caveolin-3 mutation
associated with familial hypertrophic cardiomyopathy.";
Biochem. Biophys. Res. Commun. 313:178-184(2004).
[27]
VARIANT HYPCK MET-57.
PubMed=15099591; DOI=10.1016/j.nmd.2004.01.006;
Alias L., Gallano P., Moreno D., Pujol R., Martinez-Matos J.A.,
Baiget M., Ferrer I., Olive M.;
"A novel mutation in the caveolin-3 gene causing familial isolated
hyperCKaemia.";
Neuromuscul. Disord. 14:321-324(2004).
[28]
VARIANTS LGMD1C LYS-33 AND GLU-44.
PubMed=15564037; DOI=10.1016/j.nmd.2004.08.008;
Sugie K., Murayama K., Noguchi S., Murakami N., Mochizuki M.,
Hayashi Y.K., Nonaka I., Nishino I.;
"Two novel CAV3 gene mutations in Japanese families.";
Neuromuscul. Disord. 14:810-814(2004).
[29]
VARIANT RMD2 THR-93.
PubMed=15668980; DOI=10.1002/ana.20350;
Kubisch C., Ketelsen U.-P., Goebel I., Omran H.;
"Autosomal recessive rippling muscle disease with homozygous CAV3
mutations.";
Ann. Neurol. 57:303-304(2005).
[30]
VARIANT HYPCK GLN-27, VARIANT LGMD1C THR-46, VARIANT MPDT LYS-33, AND
VARIANT MYOPATHY ARG-61.
PubMed=15580566; DOI=10.1002/humu.20119;
Fulizio L., Chiara-Nascimbeni A., Fanin M., Piluso G., Politano L.,
Nigro V., Angelini C.;
"Molecular and muscle pathology in a series of caveolinopathy
patients.";
Hum. Mutat. 25:82-89(2005).
[31]
VARIANT RMD2 GLY-53.
PubMed=16458928; DOI=10.1016/j.jns.2005.11.032;
Dotti M.T., Malandrini A., Gambelli S., Salvadori C., De Stefano N.,
Federico A.;
"A new missense mutation in caveolin-3 gene causes rippling muscle
disease.";
J. Neurol. Sci. 243:61-64(2006).
[32]
VARIANTS LQT9 MET-78; THR-85; CYS-97 AND ARG-141, VARIANTS SER-56 AND
TRP-72, AND CHARACTERIZATION OF VARIANTS LQT9 CYS-97 AND ARG-141.
PubMed=17060380; DOI=10.1161/CIRCULATIONAHA.106.635268;
Vatta M., Ackerman M.J., Ye B., Makielski J.C., Ughanze E.E.,
Taylor E.W., Tester D.J., Balijepalli R.C., Foell J.D., Li Z.,
Kamp T.J., Towbin J.A.;
"Mutant caveolin-3 induces persistent late sodium current and is
associated with long-QT syndrome.";
Circulation 114:2104-2112(2006).
[33]
VARIANTS LQT9/SIDS LEU-14; MET-78 AND ARG-79, AND INVOLVEMENT IN SIDS.
PubMed=17275750; DOI=10.1016/j.hrthm.2006.11.030;
Cronk L.B., Ye B., Kaku T., Tester D.J., Vatta M., Makielski J.C.,
Ackerman M.J.;
"Novel mechanism for sudden infant death syndrome: persistent late
sodium current secondary to mutations in caveolin-3.";
Heart Rhythm 4:161-166(2007).
-!- FUNCTION: May act as a scaffolding protein within caveolar
membranes. Interacts directly with G-protein alpha subunits and
can functionally regulate their activity. May also regulate
voltage-gated potassium channels. Plays a role in the sarcolemma
repair mechanism of both skeletal muscle and cardiomyocytes that
permits rapid resealing of membranes disrupted by mechanical
stress (By similarity). Mediates the recruitment of CAVIN2 and
CAVIN3 proteins to the caveolae (PubMed:19262564).
{ECO:0000250|UniProtKB:P51637, ECO:0000269|PubMed:19262564}.
-!- SUBUNIT: Homooligomer. Interacts with DLG1 and KCNA5; forms a
ternary complex. Interacts with TRIM72. Interacts with MUSK; may
regulate MUSK signaling. Interacts with DAG1 (via its C-terminal);
the interaction prevents binding of DAG1 with DMD
(PubMed:10988290). Interacts with DYSF (PubMed:11532985).
Interacts with BVES (By similarity). Interacts with CAVIN1 and
CAVIN2 (PubMed:24567387). Interacts with CAVIN4 (PubMed:24567387,
PubMed:11251997). {ECO:0000250|UniProtKB:P51637,
ECO:0000250|UniProtKB:P51638, ECO:0000269|PubMed:10988290,
ECO:0000269|PubMed:11251997, ECO:0000269|PubMed:11532985,
ECO:0000269|PubMed:24567387}.
-!- INTERACTION:
P0DOE7:M (xeno); NbExp=2; IntAct=EBI-3905936, EBI-10042882;
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
Peripheral membrane protein {ECO:0000250}. Cell membrane
{ECO:0000250|UniProtKB:P51638}; Peripheral membrane protein
{ECO:0000250}. Membrane, caveola {ECO:0000250|UniProtKB:P51637};
Peripheral membrane protein {ECO:0000250}. Cell membrane,
sarcolemma {ECO:0000250|UniProtKB:P51637}. Note=Potential hairpin-
like structure in the membrane. Membrane protein of caveolae (By
similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed predominantly in muscle.
{ECO:0000269|PubMed:9545514}.
-!- PTM: Sumoylation with SUMO3 by PIAS4 may reduce agonist-induced
internalization and desensitization of adrenergic receptor ABRD2.
{ECO:0000269|PubMed:21362625}.
-!- DISEASE: Limb-girdle muscular dystrophy 1C (LGMD1C) [MIM:607801]:
A degenerative myopathy characterized by calf hypertrophy and mild
to moderate proximal muscle weakness. Inheritance can be autosomal
dominant or recessive. {ECO:0000269|PubMed:11001938,
ECO:0000269|PubMed:11532985, ECO:0000269|PubMed:12557291,
ECO:0000269|PubMed:12939441, ECO:0000269|PubMed:15564037,
ECO:0000269|PubMed:15580566, ECO:0000269|PubMed:9537420}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: HyperCKmia (HYPCK) [MIM:123320]: Characterized by
persistent elevated levels of serum creatine kinase without muscle
weakness. {ECO:0000269|PubMed:10746614,
ECO:0000269|PubMed:12082049, ECO:0000269|PubMed:14663034,
ECO:0000269|PubMed:15099591, ECO:0000269|PubMed:15580566}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Rippling muscle disease 2 (RMD2) [MIM:606072]: A disorder
characterized by mechanically triggered contractions of skeletal
muscle. Mechanical stimulation leads to electrically silent muscle
contractions that spread to neighboring fibers and cause visible
ripples to move over the muscle. RMD2 inheritance is autosomal
dominant or autosomal recessive. {ECO:0000269|PubMed:11431690,
ECO:0000269|PubMed:11756609, ECO:0000269|PubMed:12557291,
ECO:0000269|PubMed:12666119, ECO:0000269|PubMed:15668980,
ECO:0000269|PubMed:16458928}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Cardiomyopathy, familial hypertrophic (CMH) [MIM:192600]:
A hereditary heart disorder characterized by ventricular
hypertrophy, which is usually asymmetric and often involves the
interventricular septum. The symptoms include dyspnea, syncope,
collapse, palpitations, and chest pain. They can be readily
provoked by exercise. The disorder has inter- and intrafamilial
variability ranging from benign to malignant forms with high risk
of cardiac failure and sudden cardiac death.
{ECO:0000269|PubMed:14672715}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Long QT syndrome 9 (LQT9) [MIM:611818]: A heart disorder
characterized by a prolonged QT interval on the ECG and
polymorphic ventricular arrhythmias. They cause syncope and sudden
death in response to exercise or emotional stress, and can present
with a sentinel event of sudden cardiac death in infancy.
{ECO:0000269|PubMed:17060380, ECO:0000269|PubMed:17275750}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Sudden infant death syndrome (SIDS) [MIM:272120]: SIDS is
the sudden death of an infant younger than 1 year that remains
unexplained after a thorough case investigation, including
performance of a complete autopsy, examination of the death scene,
and review of clinical history. Pathophysiologic mechanisms for
SIDS may include respiratory dysfunction, cardiac dysrhythmias,
cardiorespiratory instability, and inborn errors of metabolism,
but definitive pathogenic mechanisms precipitating an infant
sudden death remain elusive. {ECO:0000269|PubMed:17275750}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- DISEASE: Myopathy, distal, Tateyama type (MPDT) [MIM:614321]: A
disorder characterized by progressive muscular atrophy and muscle
weakness beginning in the hands, the legs, or the feet. Muscle
atrophy may be restricted to the small muscles of the hands and
feet. {ECO:0000269|PubMed:11805270, ECO:0000269|PubMed:15580566}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the caveolin family. {ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC14931.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAF84581.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=CAV3/LGMD1C; Note=Caveolin-3/LGMD-1C page;
URL="http://www.dmd.nl/cav3_home.html";
-!- WEB RESOURCE: Name=Wikipedia; Note=Caveolin entry;
URL="https://en.wikipedia.org/wiki/Caveolin";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF043101; AAC14931.1; ALT_INIT; mRNA.
EMBL; Y14747; CAA75042.1; -; mRNA.
EMBL; AF036367; AAC39758.1; -; Genomic_DNA.
EMBL; AF036366; AAC39758.1; JOINED; Genomic_DNA.
EMBL; AF036365; AAC39756.1; -; mRNA.
EMBL; AK291892; BAF84581.1; ALT_INIT; mRNA.
EMBL; AC068312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC069368; AAH69368.1; -; mRNA.
EMBL; BC102033; AAI02034.1; -; mRNA.
EMBL; BC102036; AAI02037.1; -; mRNA.
EMBL; BC102037; AAI02038.1; -; mRNA.
CCDS; CCDS2569.1; -.
RefSeq; NP_001225.1; NM_001234.4.
RefSeq; NP_203123.1; NM_033337.2.
UniGene; Hs.98303; -.
ProteinModelPortal; P56539; -.
BioGrid; 107307; 50.
CORUM; P56539; -.
IntAct; P56539; 7.
MINT; P56539; -.
STRING; 9606.ENSP00000341940; -.
TCDB; 1.F.1.2.1; the synaptosomal vesicle fusion pore (svf-pore) family.
PhosphoSitePlus; P56539; -.
SwissPalm; P56539; -.
BioMuta; CAV3; -.
DMDM; 3182930; -.
EPD; P56539; -.
MaxQB; P56539; -.
PaxDb; P56539; -.
PeptideAtlas; P56539; -.
PRIDE; P56539; -.
Ensembl; ENST00000343849; ENSP00000341940; ENSG00000182533.
Ensembl; ENST00000397368; ENSP00000380525; ENSG00000182533.
GeneID; 859; -.
KEGG; hsa:859; -.
UCSC; uc003bra.4; human.
CTD; 859; -.
DisGeNET; 859; -.
EuPathDB; HostDB:ENSG00000182533.6; -.
GeneCards; CAV3; -.
GeneReviews; CAV3; -.
HGNC; HGNC:1529; CAV3.
HPA; CAB017518; -.
HPA; CAB018557; -.
HPA; HPA054488; -.
MalaCards; CAV3; -.
MIM; 123320; phenotype.
MIM; 192600; phenotype.
MIM; 272120; phenotype.
MIM; 601253; gene.
MIM; 606072; phenotype.
MIM; 607801; phenotype.
MIM; 611818; phenotype.
MIM; 614321; phenotype.
neXtProt; NX_P56539; -.
OpenTargets; ENSG00000182533; -.
Orphanet; 265; Autosomal dominant limb-girdle muscular dystrophy type 1C.
Orphanet; 155; Familial isolated hypertrophic cardiomyopathy.
Orphanet; 97238; Rippling muscle disease.
Orphanet; 101016; Romano-Ward syndrome.
PharmGKB; PA26109; -.
eggNOG; ENOG410IXSQ; Eukaryota.
eggNOG; ENOG41121CB; LUCA.
GeneTree; ENSGT00390000014924; -.
HOGENOM; HOG000036550; -.
HOVERGEN; HBG003422; -.
InParanoid; P56539; -.
KO; K12959; -.
OMA; VKDIHFK; -.
OrthoDB; EOG091G0M1R; -.
PhylomeDB; P56539; -.
TreeFam; TF315736; -.
Reactome; R-HSA-445355; Smooth Muscle Contraction.
SignaLink; P56539; -.
SIGNOR; P56539; -.
ChiTaRS; CAV3; human.
GeneWiki; Caveolin_3; -.
GenomeRNAi; 859; -.
PRO; PR:P56539; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000182533; -.
CleanEx; HS_CAV3; -.
ExpressionAtlas; P56539; baseline and differential.
Genevisible; P56539; HS.
GO; GO:0005901; C:caveola; ISS:UniProtKB.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0045121; C:membrane raft; ISS:BHF-UCL.
GO; GO:0031594; C:neuromuscular junction; ISS:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
GO; GO:0030315; C:T-tubule; ISS:BHF-UCL.
GO; GO:0031982; C:vesicle; IEA:Ensembl.
GO; GO:0030018; C:Z disc; IEA:Ensembl.
GO; GO:0043014; F:alpha-tubulin binding; IEA:Ensembl.
GO; GO:0005246; F:calcium channel regulator activity; IDA:BHF-UCL.
GO; GO:0071253; F:connexin binding; IDA:BHF-UCL.
GO; GO:0044325; F:ion channel binding; IPI:BHF-UCL.
GO; GO:0019870; F:potassium channel inhibitor activity; ISS:BHF-UCL.
GO; GO:0008022; F:protein C-terminus binding; IDA:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
GO; GO:0032947; F:protein-containing complex scaffold activity; IPI:BHF-UCL.
GO; GO:0017080; F:sodium channel regulator activity; IDA:BHF-UCL.
GO; GO:0007015; P:actin filament organization; IEA:Ensembl.
GO; GO:0055013; P:cardiac muscle cell development; IEA:Ensembl.
GO; GO:0070836; P:caveola assembly; IDA:MGI.
GO; GO:0030154; P:cell differentiation; ISS:BHF-UCL.
GO; GO:0071417; P:cellular response to organonitrogen compound; IEA:Ensembl.
GO; GO:0042632; P:cholesterol homeostasis; ISS:BHF-UCL.
GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:Ensembl.
GO; GO:0035995; P:detection of muscle stretch; IEA:Ensembl.
GO; GO:0006897; P:endocytosis; ISS:BHF-UCL.
GO; GO:0042593; P:glucose homeostasis; ISS:BHF-UCL.
GO; GO:0060347; P:heart trabecula formation; IEA:Ensembl.
GO; GO:0031579; P:membrane raft organization; ISS:BHF-UCL.
GO; GO:0046716; P:muscle cell cellular homeostasis; ISS:BHF-UCL.
GO; GO:0006936; P:muscle contraction; TAS:Reactome.
GO; GO:0007517; P:muscle organ development; TAS:UniProtKB.
GO; GO:0007520; P:myoblast fusion; IEA:Ensembl.
GO; GO:0051926; P:negative regulation of calcium ion transport; IDA:MGI.
GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; IMP:BHF-UCL.
GO; GO:0061052; P:negative regulation of cell growth involved in cardiac muscle cell development; IEA:Ensembl.
GO; GO:0045792; P:negative regulation of cell size; IMP:BHF-UCL.
GO; GO:0043407; P:negative regulation of MAP kinase activity; IMP:BHF-UCL.
GO; GO:0043409; P:negative regulation of MAPK cascade; ISS:BHF-UCL.
GO; GO:1900826; P:negative regulation of membrane depolarization during cardiac muscle cell action potential; IEA:Ensembl.
GO; GO:0051001; P:negative regulation of nitric-oxide synthase activity; ISS:BHF-UCL.
GO; GO:1901380; P:negative regulation of potassium ion transmembrane transport; ISS:BHF-UCL.
GO; GO:1901017; P:negative regulation of potassium ion transmembrane transporter activity; ISS:BHF-UCL.
GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:BHF-UCL.
GO; GO:2000009; P:negative regulation of protein localization to cell surface; NAS:BHF-UCL.
GO; GO:0060299; P:negative regulation of sarcomere organization; IMP:BHF-UCL.
GO; GO:0051647; P:nucleus localization; IEA:Ensembl.
GO; GO:0007009; P:plasma membrane organization; ISS:BHF-UCL.
GO; GO:0001778; P:plasma membrane repair; IEA:Ensembl.
GO; GO:2001288; P:positive regulation of caveolin-mediated endocytosis; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:BHF-UCL.
GO; GO:0031116; P:positive regulation of microtubule polymerization; ISS:BHF-UCL.
GO; GO:0010831; P:positive regulation of myotube differentiation; IEA:Ensembl.
GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; NAS:BHF-UCL.
GO; GO:0008104; P:protein localization; ISS:BHF-UCL.
GO; GO:0072659; P:protein localization to plasma membrane; ISS:BHF-UCL.
GO; GO:0060762; P:regulation of branching involved in mammary gland duct morphogenesis; IEA:Ensembl.
GO; GO:0090279; P:regulation of calcium ion import; IDA:BHF-UCL.
GO; GO:1901019; P:regulation of calcium ion transmembrane transporter activity; IDA:BHF-UCL.
GO; GO:0098909; P:regulation of cardiac muscle cell action potential involved in regulation of contraction; IMP:BHF-UCL.
GO; GO:0055117; P:regulation of cardiac muscle contraction; IMP:BHF-UCL.
GO; GO:0008016; P:regulation of heart contraction; ISS:BHF-UCL.
GO; GO:0002027; P:regulation of heart rate; IMP:BHF-UCL.
GO; GO:1900825; P:regulation of membrane depolarization during cardiac muscle cell action potential; IMP:BHF-UCL.
GO; GO:0042391; P:regulation of membrane potential; IDA:BHF-UCL.
GO; GO:0051394; P:regulation of nerve growth factor receptor activity; IMP:MGI.
GO; GO:1900744; P:regulation of p38MAPK cascade; IEA:Ensembl.
GO; GO:0051896; P:regulation of protein kinase B signaling; IEA:Ensembl.
GO; GO:0038009; P:regulation of signal transduction by receptor internalization; IMP:MGI.
GO; GO:0014819; P:regulation of skeletal muscle contraction; IMP:BHF-UCL.
GO; GO:2000649; P:regulation of sodium ion transmembrane transporter activity; IDA:BHF-UCL.
GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
GO; GO:0060373; P:regulation of ventricular cardiac muscle cell membrane depolarization; IDA:BHF-UCL.
GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IMP:BHF-UCL.
GO; GO:0033292; P:T-tubule organization; TAS:BHF-UCL.
GO; GO:0006641; P:triglyceride metabolic process; ISS:BHF-UCL.
GO; GO:0086005; P:ventricular cardiac muscle cell action potential; ISS:BHF-UCL.
InterPro; IPR031091; CAV-3.
InterPro; IPR001612; Caveolin.
InterPro; IPR018361; Caveolin_CS.
PANTHER; PTHR10844; PTHR10844; 1.
PANTHER; PTHR10844:SF16; PTHR10844:SF16; 1.
Pfam; PF01146; Caveolin; 1.
PROSITE; PS01210; CAVEOLIN; 1.
1: Evidence at protein level;
Cardiomyopathy; Cell membrane; Complete proteome; Disease mutation;
Golgi apparatus; Isopeptide bond; Limb-girdle muscular dystrophy;
Long QT syndrome; Membrane; Polymorphism; Reference proteome;
Ubl conjugation.
CHAIN 1 151 Caveolin-3.
/FTId=PRO_0000144140.
TOPO_DOM 1 83 Cytoplasmic. {ECO:0000255}.
INTRAMEM 84 104 Helical. {ECO:0000255}.
TOPO_DOM 105 151 Cytoplasmic. {ECO:0000255}.
REGION 64 114 Required for interaction with DAG1.
{ECO:0000269|PubMed:10988290}.
CROSSLNK 38 38 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO3).
{ECO:0000269|PubMed:21362625}.
VARIANT 14 14 V -> L (in SIDS; dbSNP:rs121909281).
{ECO:0000269|PubMed:17275750}.
/FTId=VAR_043694.
VARIANT 27 27 R -> Q (in HYPCK, RMD2, LGMD1C and MPDT;
dbSNP:rs116840778).
{ECO:0000269|PubMed:10746614,
ECO:0000269|PubMed:11431690,
ECO:0000269|PubMed:11756609,
ECO:0000269|PubMed:11805270,
ECO:0000269|PubMed:12939441,
ECO:0000269|PubMed:15580566}.
/FTId=VAR_011512.
VARIANT 28 28 D -> E (in RMD2 and LGMD1C;
dbSNP:rs116840782).
{ECO:0000269|PubMed:12557291}.
/FTId=VAR_015374.
VARIANT 29 29 P -> L (in HYPCK; dbSNP:rs116840786).
{ECO:0000269|PubMed:12082049}.
/FTId=VAR_029540.
VARIANT 33 33 N -> K (in LGMD1C and MPDT;
dbSNP:rs1008642).
{ECO:0000269|PubMed:15564037,
ECO:0000269|PubMed:15580566}.
/FTId=VAR_021016.
VARIANT 44 44 V -> E (in LGMD1C; dbSNP:rs116840788).
{ECO:0000269|PubMed:15564037}.
/FTId=VAR_021017.
VARIANT 46 46 A -> T (in LGMD1C and RMD2; decreased
surface expression of the CAV3 protein;
dbSNP:rs116840789).
{ECO:0000269|PubMed:11001938,
ECO:0000269|PubMed:11431690,
ECO:0000269|PubMed:15580566}.
/FTId=VAR_011513.
VARIANT 46 46 A -> V (in RMD2; dbSNP:rs116840773).
{ECO:0000269|PubMed:11431690}.
/FTId=VAR_011514.
VARIANT 53 53 S -> G (in RMD2; dbSNP:rs116840794).
{ECO:0000269|PubMed:16458928}.
/FTId=VAR_029541.
VARIANT 56 56 G -> S (in dbSNP:rs72546667).
{ECO:0000269|PubMed:11251997,
ECO:0000269|PubMed:17060380,
ECO:0000269|PubMed:9536092}.
/FTId=VAR_029542.
VARIANT 57 57 V -> M (in HYPCK; dbSNP:rs116840795).
{ECO:0000269|PubMed:15099591}.
/FTId=VAR_010742.
VARIANT 61 61 S -> R (in a patient with mild proximal
myopathy; dbSNP:rs116840796).
{ECO:0000269|PubMed:15580566}.
/FTId=VAR_026696.
VARIANT 64 66 Missing (in LGMD1C).
{ECO:0000269|PubMed:9537420}.
/FTId=VAR_001402.
VARIANT 64 64 T -> P (in LGMD1C; dbSNP:rs199476332).
{ECO:0000269|PubMed:11532985}.
/FTId=VAR_021018.
VARIANT 64 64 T -> S (in CMH; dbSNP:rs121909280).
{ECO:0000269|PubMed:14672715}.
/FTId=VAR_029543.
VARIANT 72 72 C -> W (in dbSNP:rs116840776).
{ECO:0000269|PubMed:11251997,
ECO:0000269|PubMed:17060380,
ECO:0000269|PubMed:9536092}.
/FTId=VAR_010743.
VARIANT 78 78 T -> M (in LQT9 and SIDS;
dbSNP:rs72546668).
{ECO:0000269|PubMed:17060380,
ECO:0000269|PubMed:17275750}.
/FTId=VAR_043695.
VARIANT 79 79 L -> R (in LQT9 and SIDS;
dbSNP:rs121909282).
{ECO:0000269|PubMed:17275750}.
/FTId=VAR_043696.
VARIANT 85 85 A -> T (in LQT9; dbSNP:rs104893715).
{ECO:0000269|PubMed:17060380}.
/FTId=VAR_043697.
VARIANT 87 87 L -> P (in RMD2; dbSNP:rs28936685).
{ECO:0000269|PubMed:12666119}.
/FTId=VAR_016207.
VARIANT 93 93 A -> T (in RMD2; dbSNP:rs28936686).
{ECO:0000269|PubMed:12666119,
ECO:0000269|PubMed:15668980}.
/FTId=VAR_016208.
VARIANT 97 97 F -> C (in LQT9; increase in late sodium
current; dbSNP:rs104893714).
{ECO:0000269|PubMed:17060380}.
/FTId=VAR_043698.
VARIANT 97 97 Missing (in HYPCK).
{ECO:0000269|PubMed:14663034}.
/FTId=VAR_029544.
VARIANT 105 105 P -> L (in LGMD1C and RMD2;
dbSNP:rs116840805).
{ECO:0000269|PubMed:11431690,
ECO:0000269|PubMed:9537420}.
/FTId=VAR_001403.
VARIANT 126 126 R -> H (in dbSNP:rs116840777).
{ECO:0000269|PubMed:11251997}.
/FTId=VAR_029545.
VARIANT 141 141 S -> R (in LQT9; increase in late sodium
current; dbSNP:rs104893713).
{ECO:0000269|PubMed:17060380}.
/FTId=VAR_043699.
SEQUENCE 151 AA; 17259 MW; C695E14F5B8F4753 CRC64;
MMAEEHTDLE AQIVKDIHCK EIDLVNRDPK NINEDIVKVD FEDVIAEPVG TYSFDGVWKV
SYTTFTVSKY WCYRLLSTLL GVPLALLWGF LFACISFCHI WAVVPCIKSY LIEIQCISHI
YSLCIRTFCN PLFAALGQVC SSIKVVLRKE V


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