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Cystic fibrosis transmembrane conductance regulator (CFTR) (ATP-binding cassette sub-family C member 7) (Channel conductance-controlling ATPase) (EC 3.6.3.49) (cAMP-dependent chloride channel)

 CFTR_RAT                Reviewed;        1476 AA.
P34158; Q2IBD3;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
12-JUN-2007, sequence version 3.
30-AUG-2017, entry version 162.
RecName: Full=Cystic fibrosis transmembrane conductance regulator;
Short=CFTR;
AltName: Full=ATP-binding cassette sub-family C member 7;
AltName: Full=Channel conductance-controlling ATPase;
EC=3.6.3.49 {ECO:0000250|UniProtKB:P13569};
AltName: Full=cAMP-dependent chloride channel;
Name=Cftr; Synonyms=Abcc7;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12917688; DOI=10.1038/nature01858;
Thomas J.W., Touchman J.W., Blakesley R.W., Bouffard G.G.,
Beckstrom-Sternberg S.M., Margulies E.H., Blanchette M., Siepel A.C.,
Thomas P.J., McDowell J.C., Maskeri B., Hansen N.F., Schwartz M.S.,
Weber R.J., Kent W.J., Karolchik D., Bruen T.C., Bevan R.,
Cutler D.J., Schwartz S., Elnitski L., Idol J.R., Prasad A.B.,
Lee-Lin S.-Q., Maduro V.V.B., Summers T.J., Portnoy M.E.,
Dietrich N.L., Akhter N., Ayele K., Benjamin B., Cariaga K.,
Brinkley C.P., Brooks S.Y., Granite S., Guan X., Gupta J.,
Haghighi P., Ho S.-L., Huang M.C., Karlins E., Laric P.L., Legaspi R.,
Lim M.J., Maduro Q.L., Masiello C.A., Mastrian S.D., McCloskey J.C.,
Pearson R., Stantripop S., Tiongson E.E., Tran J.T., Tsurgeon C.,
Vogt J.L., Walker M.A., Wetherby K.D., Wiggins L.S., Young A.C.,
Zhang L.-H., Osoegawa K., Zhu B., Zhao B., Shu C.L., De Jong P.J.,
Lawrence C.E., Smit A.F., Chakravarti A., Haussler D., Green P.,
Miller W., Green E.D.;
"Comparative analyses of multi-species sequences from targeted genomic
regions.";
Nature 424:788-793(2003).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
PubMed=7526924; DOI=10.1093/hmg/3.7.1089;
Denamur E., Chehab F.F.;
"Analysis of the mouse and rat CFTR promoter regions.";
Hum. Mol. Genet. 3:1089-1094(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 482-988.
PubMed=1282491; DOI=10.1016/S0888-7543(05)80107-7;
Trezise A.E., Szpirer C., Buchwald M.;
"Localization of the gene encoding the cystic fibrosis transmembrane
conductance regulator (CFTR) in the rat to chromosome 4 and
implications for the evolution of mammalian chromosomes.";
Genomics 14:869-874(1992).
[4]
INTERACTION WITH GOPC.
PubMed=11707463; DOI=10.1074/jbc.M110177200;
Cheng J., Moyer B.D., Milewski M., Loffing J., Ikeda M., Mickle J.E.,
Cutting G.R., Li M., Stanton B.A., Guggino W.B.;
"A Golgi-associated PDZ domain protein modulates cystic fibrosis
transmembrane regulator plasma membrane expression.";
J. Biol. Chem. 277:3520-3529(2002).
[5]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=12519745; DOI=10.1152/ajpcell.00227.2002;
Hallows K.R., Kobinger G.P., Wilson J.M., Witters L.A., Foskett J.K.;
"Physiological modulation of CFTR activity by AMP-activated protein
kinase in polarized T84 cells.";
Am. J. Physiol. 284:C1297-C1308(2003).
[6]
INTERACTION WITH SHANK2.
PubMed=14679199; DOI=10.1074/jbc.M312871200;
Kim J.Y., Han W., Namkung W., Lee J.H., Kim K.H., Shin H., Kim E.,
Lee M.G.;
"Inhibitory regulation of cystic fibrosis transmembrane conductance
regulator anion-transporting activities by Shank2.";
J. Biol. Chem. 279:10389-10396(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-808, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Epithelial ion channel that plays an important role in
the regulation of epithelial ion and water transport and fluid
homeostasis. Mediates the transport of chloride ions across the
cell membrane (By similarity). Channel activity is coupled to ATP
hydrolysis. The ion channel is also permeable to HCO(3-);
selectivity depends on the extracellular chloride concentration.
Exerts its function also by modulating the activity of other ion
channels and transporters. Contributes to the regulation of the pH
and the ion content of the epithelial fluid layer. Modulates the
activity of the epithelial sodium channel (ENaC) complex, in part
by regulating the cell surface expression of the ENaC complex. May
regulate bicarbonate secretion and salvage in epithelial cells by
regulating the transporter SLC4A7. Can inhibit the chloride
channel activity of ANO1 (By similarity). Plays a role in the
chloride and bicarbonate homeostasis during sperm epididymal
maturation and capacitation (By similarity).
{ECO:0000250|UniProtKB:P13569, ECO:0000250|UniProtKB:P26361}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000250|UniProtKB:P13569}.
-!- SUBUNIT: Monomer; does not require oligomerization for channel
activity. May form oligomers in the membrane (By similarity).
Interacts with SLC4A7 through SLC9A3R1 (By similarity). Interacts
with SHANK2 (PubMed:14679199). Interacts with SLC9A3R1 and MYO6.
Interacts (via C-terminus) with GOPC (via PDZ domain); this
promotes CFTR internalization and thereby decreases channel
activity (PubMed:11707463). Interacts with SLC4A7 through
SLC9A3R1. Found in a complex with MYO5B and RAB11A. Interacts with
ANO1. Interacts with SLC26A8 (By similarity). Interacts with
AHCYL1; the interaction increases CFTR activity (By similarity).
Interacts with CSE1L (By similarity).
{ECO:0000250|UniProtKB:P13569, ECO:0000250|UniProtKB:P26361,
ECO:0000269|PubMed:11707463, ECO:0000269|PubMed:14679199}.
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000250|UniProtKB:P26361}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P13569}. Early endosome membrane
{ECO:0000250|UniProtKB:P13569}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P13569}. Cell membrane
{ECO:0000250|UniProtKB:P26361}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P13569}. Recycling endosome membrane
{ECO:0000250|UniProtKB:P13569}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P13569}. Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:P13569}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P13569}. Note=The channel is internalized
from the cell surface into an endosomal recycling compartment,
from where it is recycled to the cell membrane. In the oviduct and
bronchus, detected on the apical side of epithelial cells, but not
associated with cilia. {ECO:0000250|UniProtKB:P13569}.
-!- TISSUE SPECIFICITY: Detected in epithelial cells in nasopharynx,
submandibular gland, pancreas and ileum (at protein level).
{ECO:0000269|PubMed:12519745}.
-!- DOMAIN: Binds and hydrolyzes ATP via the two cytoplasmic ABC
transporter nucleotide-binding domains. The two ATP-binding
domains interact with each other, forming a head-to-tail dimer.
Normal ATPase activity requires interaction between the two
domains. The first ABC transporter nucleotide-binding domain has
no ATPase activity by itself. {ECO:0000250|UniProtKB:P13569,
ECO:0000250|UniProtKB:P26361}.
-!- DOMAIN: The PDZ-binding motif mediates interactions with GOPC and
with the SLC4A7, SLC9A3R1/EBP50 complex.
{ECO:0000250|UniProtKB:P13569}.
-!- DOMAIN: The R region is intrinsically disordered. It mediates
channel activation when it is phosphorylated, but not in the
absence of phosphorylation. {ECO:0000250|UniProtKB:P13569}.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P13569}.
-!- PTM: Phosphorylated; cAMP treatment promotes phosphorylation and
activates the channel. Dephosphorylation decreases the ATPase
activity (in vitro). Phosphorylation at PKA sites activates the
channel. Phosphorylation at PKC sites enhances the response to
phosphorylation by PKA. Phosphorylated by AMPK; this inhibits
channel activity. {ECO:0000250|UniProtKB:P13569}.
-!- PTM: Ubiquitinated, leading to its degradation in the lysosome.
Deubiquitination by USP10 in early endosomes enhances its
endocytic recycling to the cell membrane. Ubiquitinated by RNF185
during ER stress. {ECO:0000250|UniProtKB:P13569}.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC
family. CFTR transporter (TC 3.A.1.202) subfamily. {ECO:0000305}.
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EMBL; DP000027; AAR16315.1; -; Genomic_DNA.
EMBL; L26098; AAA73561.1; -; Genomic_DNA.
EMBL; M89906; AAA40918.1; -; mRNA.
PIR; I84733; I84733.
RefSeq; NP_113694.1; NM_031506.1.
UniGene; Rn.124539; -.
ProteinModelPortal; P34158; -.
BioGrid; 246440; 3.
STRING; 10116.ENSRNOP00000010981; -.
BindingDB; P34158; -.
ChEMBL; CHEMBL3992; -.
iPTMnet; P34158; -.
PhosphoSitePlus; P34158; -.
PaxDb; P34158; -.
PRIDE; P34158; -.
GeneID; 24255; -.
KEGG; rno:24255; -.
CTD; 1080; -.
RGD; 2332; Cftr.
eggNOG; KOG0054; Eukaryota.
eggNOG; COG1132; LUCA.
HOVERGEN; HBG004169; -.
InParanoid; P34158; -.
KO; K05031; -.
PhylomeDB; P34158; -.
TreeFam; TF105200; -.
PRO; PR:P34158; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:RGD.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0005769; C:early endosome; ISS:UniProtKB.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005902; C:microvillus; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; ISS:UniProtKB.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IBA:GO_Central.
GO; GO:0015106; F:bicarbonate transmembrane transporter activity; ISS:UniProtKB.
GO; GO:0005254; F:chloride channel activity; ISS:UniProtKB.
GO; GO:0019869; F:chloride channel inhibitor activity; ISS:UniProtKB.
GO; GO:0015108; F:chloride transmembrane transporter activity; ISS:UniProtKB.
GO; GO:0005260; F:intracellular ATPase-gated chloride channel activity; ISS:UniProtKB.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0015701; P:bicarbonate transport; IMP:RGD.
GO; GO:0071454; P:cellular response to anoxia; IEP:RGD.
GO; GO:0071320; P:cellular response to cAMP; ISS:UniProtKB.
GO; GO:1904322; P:cellular response to forskolin; ISS:UniProtKB.
GO; GO:0034605; P:cellular response to heat; IEP:RGD.
GO; GO:0032870; P:cellular response to hormone stimulus; IEP:RGD.
GO; GO:1902476; P:chloride transmembrane transport; ISS:UniProtKB.
GO; GO:0006821; P:chloride transport; IMP:RGD.
GO; GO:0051454; P:intracellular pH elevation; ISS:UniProtKB.
GO; GO:0015705; P:iodide transport; IMP:RGD.
GO; GO:0097421; P:liver regeneration; IEP:RGD.
GO; GO:0030324; P:lung development; IMP:RGD.
GO; GO:0060081; P:membrane hyperpolarization; ISS:UniProtKB.
GO; GO:0050891; P:multicellular organismal water homeostasis; ISS:UniProtKB.
GO; GO:2000077; P:negative regulation of type B pancreatic cell development; IMP:RGD.
GO; GO:1905460; P:negative regulation of vascular associated smooth muscle cell apoptotic process; IMP:RGD.
GO; GO:0097755; P:positive regulation of blood vessel diameter; IDA:RGD.
GO; GO:1904446; P:positive regulation of establishment of Sertoli cell barrier; IMP:RGD.
GO; GO:0033005; P:positive regulation of mast cell activation; IMP:RGD.
GO; GO:0034097; P:response to cytokine; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0043627; P:response to estrogen; IEP:RGD.
GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
GO; GO:0048240; P:sperm capacitation; ISS:UniProtKB.
GO; GO:0030321; P:transepithelial chloride transport; IMP:RGD.
GO; GO:0035377; P:transepithelial water transport; ISS:UniProtKB.
GO; GO:0042311; P:vasodilation; IMP:RGD.
GO; GO:0006833; P:water transport; IMP:RGD.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR011527; ABC1_TM_dom.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR009147; CFTR/ABCC7.
InterPro; IPR025837; CFTR_reg_dom.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR24223:SF273; PTHR24223:SF273; 1.
Pfam; PF00664; ABC_membrane; 2.
Pfam; PF00005; ABC_tran; 2.
Pfam; PF14396; CFTR_R; 1.
PRINTS; PR01851; CYSFIBREGLTR.
SMART; SM00382; AAA; 2.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF90123; SSF90123; 3.
TIGRFAMs; TIGR01271; CFTR_protein; 1.
PROSITE; PS50929; ABC_TM1F; 2.
PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
1: Evidence at protein level;
ATP-binding; Cell membrane; Chloride; Chloride channel;
Complete proteome; Endoplasmic reticulum; Endosome; Glycoprotein;
Hydrolase; Ion channel; Ion transport; Lipoprotein; Membrane;
Nucleotide-binding; Palmitate; Phosphoprotein; Reference proteome;
Repeat; Transmembrane; Transmembrane helix; Transport;
Ubl conjugation.
CHAIN 1 1476 Cystic fibrosis transmembrane conductance
regulator.
/FTId=PRO_0000093428.
TOPO_DOM 1 77 Cytoplasmic.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 78 98 Helical; Name=1.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 99 122 Extracellular.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 123 146 Helical; Name=2.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 147 195 Cytoplasmic.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 196 216 Helical; Name=3.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 217 222 Extracellular.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 223 243 Helical; Name=4.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 244 298 Cytoplasmic.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 299 319 Helical; Name=5.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 320 339 Extracellular.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 340 358 Helical; Name=6.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 359 853 Cytoplasmic.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 854 874 Helical; Name=7.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 875 913 Extracellular.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 914 934 Discontinuously helical; Name=8.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 935 985 Cytoplasmic.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 986 1006 Helical; Name=9.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 1007 1008 Extracellular.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 1009 1029 Helical; Name=10.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 1030 1090 Cytoplasmic.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 1091 1111 Helical; Name=11.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 1112 1125 Extracellular.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 1126 1146 Helical; Name=12.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 1147 1476 Cytoplasmic.
{ECO:0000250|UniProtKB:P13569}.
DOMAIN 81 365 ABC transmembrane type-1 1.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 412 646 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 854 1153 ABC transmembrane type-1 2.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 1208 1439 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 458 465 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 458 465 ATP 1. {ECO:0000250|UniProtKB:P26361,
ECO:0000255|PROSITE-ProRule:PRU00434}.
NP_BIND 1240 1247 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 1240 1247 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
REGION 654 826 Intrinsically disordered R region.
{ECO:0000250|UniProtKB:P13569}.
MOTIF 1474 1476 PDZ-binding.
{ECO:0000269|PubMed:11707463}.
BINDING 401 401 ATP 1. {ECO:0000250|UniProtKB:P13569}.
BINDING 493 493 ATP 1. {ECO:0000250|UniProtKB:P26361}.
BINDING 1215 1215 ATP 2. {ECO:0000250|UniProtKB:P13569}.
MOD_RES 549 549 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 660 660 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 670 670 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 684 684 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 698 698 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 710 710 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 715 715 Phosphothreonine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 732 732 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 763 763 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 785 785 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 790 790 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 808 808 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1440 1440 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 1452 1452 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
LIPID 524 524 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P13569}.
LIPID 1391 1391 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P13569}.
CARBOHYD 889 889 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 895 895 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 987 988 FD -> LT (in Ref. 3; AAA40918).
{ECO:0000305}.
SEQUENCE 1476 AA; 167830 MW; B2B2A25EB5107640 CRC64;
MQKSPLEKAS FISKLFFSWT TPILRKGYRH HLELSDIYQA PSSDSADHLS EKLEREWDRE
QASKKKPQLI HALRRCFVWR FVFYGVLLYL GEVTKAVQPV LLGRIIASYD PDNTEERSIA
IYLGIGLCLL FIVRTLLLHP AIFGLHHIGM QMRIAMFSLI YKKTLKLSSR VLDKISIGQL
ISLLSNNLNK FDEGLALAHF IWIAPLQVVL LMGLLWDLLQ FSAFCGLGLL IVLVIFQAIL
GKMMVKYRDK RAAKINERLV ITSEVIDNIY SVKAYCWESA MEKIIESLRE EELKMTRRSA
YMRFFTSSAF FFSGFFVVFL SVLPYTVING IVLRKIFTTI SFCIVLRMSV TRQFPTAVQI
WYDSLGMIRK IQDFLQTQEY KVLEYNLMFT GLVMENVTAF WEEGFQELLE KVQLNNDDRK
TSNGENHLSF SHLCLVGNPV LKNINLNIKK GEMLAITGST GAGKTSLLML ILGELEASEG
IIKHSGRVSF SSQISWIMPG TIKENIIFGV SYDEYRYKSV VKACQLQEDI TKFAEQDNTV
LGEGGVTLSG GQRARISLAR AVYKDADLYL LDSPFGYLDV LTEEQIFESC VCKLMASKTR
ILVTSKMEQL KKADKILILH EGSSYFYGTF SELQSLRPDF SSKLMGYDTF DQFTEERRSS
ILTETLRRFS VDDASTTWNK AKQSFRQTGE FGEKRKNSIL SSFSSVKKIS IVQKTPLSIE
GESDDLQERR LSLVPDSEHG EAALPRSNMI TAGPTFPGRR RQSVLDLMTF TPSSVSSSLQ
RTRASIRKIS LAPRISLKEE DIYSRRLSQD STLNITEEIN EEDLKECFFD DMVKIPTVTT
WNTYLRYFTL HRGLFAVLIW CVLVFLVEVA ASLFVLWLLK NNPVNGGNNG TKIANTSYVV
VITSSSFYYI FYIYVGVADT LLALSLFRGL PLVHTLITAS KILHRKMLHS ILHAPMSTFN
KLKAGGILNR FSKDIAILDD FLPLTIFDFI QLLFIVVGAI IVVSALQPYI FLATVPGLAV
FILLRAYFLH TSQQLKQLES EGRSPIFTHL VTSLKGLWTL RAFRRQTYFE TLFHKALNLH
TANWFMYLAT LRWFQMRIDM IFVLFFIVVT FISILTTGEG EGTTGIILTL AMNIMSTLQW
AVNSSIDTDS LMRSVSRVFK FIDIQTEESI CTKIMKELHS EDSPNALVIK NEHVKKCDTW
PSGGEMVVKD LTVKYVDDGN AILENISFSI SPGQRVGLLG RTGSGKSTLL SAFLRMLNIK
GEIQIDGVSW NSMTLQEWRK AFGVITQKVF IFSGTFRQNL DPNGKWRDEE IWKVADQVGL
KSVIEQFPGQ LNFTLVDGGY VLSHGHKQLM CLARSVLSKA KIILLDEPSA NLDPITYQVI
RRVLRQAFAG CTVVLCEHRI EAMLDCQRFL VIEQGNVWQY ESLQALLSEK SVFQRALSSS
EKMKLFHGRH SSKQKPRTQI TAVKEETEEE VQETRL


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EIAAB06993 ABCC7,ATP-binding cassette sub-family C member 7,cAMP-dependent chloride channel,CFTR,CFTR,Channel conductance-controlling ATPase,Cystic fibrosis transmembrane conductance regulator,Oryctolagus cunicu
EIAAB06991 ABCC7,ATP-binding cassette sub-family C member 7,Bos taurus,Bovine,cAMP-dependent chloride channel,CFTR,CFTR,Channel conductance-controlling ATPase,Cystic fibrosis transmembrane conductance regulator
EIAAB06992 Abcc7,ATP-binding cassette sub-family C member 7,cAMP-dependent chloride channel,CFTR,Cftr,Channel conductance-controlling ATPase,Cystic fibrosis transmembrane conductance regulator,Rat,Rattus norvegi
EIAAB06988 Abcc7,ATP-binding cassette sub-family C member 7,cAMP-dependent chloride channel,CFTR,Cftr,Channel conductance-controlling ATPase,Cystic fibrosis transmembrane conductance regulator,Mouse,Mus musculus
EIAAB06994 ABCC7,ATP-binding cassette sub-family C member 7,cAMP-dependent chloride channel,CFTR,CFTR,Channel conductance-controlling ATPase,Cystic fibrosis transmembrane conductance regulator,Homo sapiens,Human
EIAAB06990 ABCC7,ATP-binding cassette sub-family C member 7,cAMP-dependent chloride channel,Canis familiaris,Canis lupus familiaris,CFTR,CFTR,Channel conductance-controlling ATPase,Cystic fibrosis transmembrane
20-783-73186 MOUSE ANTI HUMAN CFTR - CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR PROTEIN; CFTR; cAMP-dependent chloride channel; ATP-binding cassette transporter sub-family C member 7 Monoclonal 0.2 mg
CGA CFTR Gene cystic fibrosis transmembrane conductance regulator (ATP-binding cassette sub-family C, member 7)
CSB-EL005292RA Rat cystic fibrosis transmembrane conductance regulator (ATP-binding cassette sub-family C, member 7) (CFTR) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL005292DO Dog cystic fibrosis transmembrane conductance regulator (ATP-binding cassette sub-family C, member 7) (CFTR) ELISA kit, Species Dog, Sample Type serum, plasma 96T
CSB-EL005292PI Pig cystic fibrosis transmembrane conductance regulator (ATP-binding cassette sub-family C, member 7) (CFTR) ELISA kit, Species Pig, Sample Type serum, plasma 96T
CSB-EL005292SH Sheep cystic fibrosis transmembrane conductance regulator (ATP-binding cassette sub-family C, member 7) (CFTR) ELISA kit, Species Sheep, Sample Type serum, plasma 96T
CSB-EL005292RH Monkey cystic fibrosis transmembrane conductance regulator (ATP-binding cassette sub-family C, member 7) (CFTR) ELISA kit, Species Monkey, Sample Type serum, plasma 96T
CSB-EL005292MO Mouse cystic fibrosis transmembrane conductance regulator (ATP-binding cassette sub-family C, member 7) (CFTR) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL005292HU Human cystic fibrosis transmembrane conductance regulator (ATP-binding cassette sub-family C, member 7) (CFTR) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL005292BO Bovine cystic fibrosis transmembrane conductance regulator (ATP-binding cassette sub-family C, member 7) (CFTR) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
CSB-EL005292GU Guinea pig cystic fibrosis transmembrane conductance regulator (ATP-binding cassette sub-family C, member 7) (CFTR) ELISA kit, Species Guinea pig, Sample Type serum, plasma 96T
CSB-EL005292HO Horse cystic fibrosis transmembrane conductance regulator (ATP-binding cassette sub-family C, member 7) (CFTR) ELISA kit, Species Horse, Sample Type serum, plasma 96T
CSB-EL005292RB Rabbit cystic fibrosis transmembrane conductance regulator (ATP-binding cassette sub-family C, member 7) (CFTR) ELISA kit, Species Rabbit, Sample Type serum, plasma 96T
DL-CFTR-Hu Human Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) ELISA Kit 96T
Y102989 Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) 200ug
Y108236 Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) 100ug
Y102988 Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) 200ug
GWB-E45859 Cystic Fibrosis Transmembrane Conductance Regulator (CFTR), Antibody


 

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