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Thyroglobulin (Tg)

 THYG_RAT                Reviewed;        2768 AA.
P06882; Q9JKY6; Q9JM94;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
11-JAN-2001, sequence version 4.
23-MAY-2018, entry version 156.
RecName: Full=Thyroglobulin;
Short=Tg;
Flags: Precursor;
Name=Tg;
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 [MRNA], AND VARIANT HYPOTHYROIDISM ARG-2320.
STRAIN=Wistar Imamichi;
PubMed=11089535; DOI=10.1210/endo.141.11.7794;
Hishinuma A., Furudate S., Oh-Ishi M., Nagakubo N., Namatame T.,
Ieiri T.;
"A novel missense mutation (G2320R) in thyroglobulin causes
hypothyroidism in rdw rats.";
Endocrinology 141:4050-4055(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Fischer 344;
Ding M., Jung C.-C., Cheng J.-M., Miyamoto T., Furudate S.I., Agui T.;
"A missense mutation in the thyroglobulin gene causes hypothyroidism
and dwarfism not associated with goiter in the WIC-rdw rat.";
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-213.
STRAIN=Fischer; TISSUE=Thymocyte;
PubMed=2325666; DOI=10.1210/mend-4-1-155;
Graves P.N., Davies T.F.;
"A second thyroglobulin messenger RNA species (rTg-2) in rat
thyrocytes.";
Mol. Endocrinol. 4:155-161(1990).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59.
PubMed=3455768; DOI=10.1073/pnas.83.2.323;
Musti A.M., Avvedimento V.E., Polistina C., Ursini V.M., Obici S.,
Nitsch L., Cocozza S., di Lauro R.;
"The complete structure of the rat thyroglobulin gene.";
Proc. Natl. Acad. Sci. U.S.A. 83:323-327(1986).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1802-2768.
PubMed=3838512; DOI=10.1111/j.1432-1033.1985.tb08799.x;
di Lauro R., Obici S., Condliffe D., Ursini V.M., Musti A.M.,
Moscatelli C., Avvedimento V.E.;
"The sequence of 967 amino acids at the carboxyl-end of rat
thyroglobulin. Location and surroundings of two thyroxine-forming
sites.";
Eur. J. Biochem. 148:7-11(1985).
-!- FUNCTION: Precursor of the iodinated thyroid hormones thyroxine
(T4) and triiodothyronine (T3).
-!- SUBUNIT: Homodimer.
-!- INTERACTION:
P06761:Hspa5; NbExp=6; IntAct=EBI-1549657, EBI-916036;
P38659:Pdia4; NbExp=3; IntAct=EBI-1549657, EBI-917435;
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Thyroid gland specific.
-!- PTM: Sulfated tyrosines are desulfated during iodination.
{ECO:0000250}.
-!- DISEASE: Note=Defects in Tg are a cause of a form of
hypothyroidism in rdw rat.
-!- MISCELLANEOUS: It is not certain whether this thyroglobulin plays
any role in the formation of triiodothyronine.
-!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
{ECO:0000305}.
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EMBL; AB035201; BAA96132.1; -; mRNA.
EMBL; AF221622; AAF34909.1; -; mRNA.
EMBL; M35965; AAA42089.1; ALT_TERM; mRNA.
EMBL; M12559; AAA50379.1; -; Genomic_DNA.
EMBL; M12558; AAA50379.1; JOINED; Genomic_DNA.
EMBL; X02318; CAA26183.1; -; mRNA.
PIR; A22016; UIRT.
UniGene; Rn.10429; -.
ProteinModelPortal; P06882; -.
CORUM; P06882; -.
IntAct; P06882; 3.
STRING; 10116.ENSRNOP00000009241; -.
ESTHER; ratno-thyro; Thyroglobulin.
MEROPS; I31.950; -.
PaxDb; P06882; -.
PRIDE; P06882; -.
UCSC; RGD:3848; rat.
RGD; 3848; Tg.
eggNOG; ENOG410IG6K; Eukaryota.
eggNOG; COG2272; LUCA.
HOGENOM; HOG000128427; -.
HOVERGEN; HBG017929; -.
InParanoid; P06882; -.
PhylomeDB; P06882; -.
PRO; PR:P06882; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0043168; F:anion binding; IDA:RGD.
GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0005102; F:signaling receptor binding; IDA:RGD.
GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0009268; P:response to pH; IDA:RGD.
GO; GO:0006590; P:thyroid hormone generation; IDA:RGD.
GO; GO:0045056; P:transcytosis; IDA:RGD.
CDD; cd00191; TY; 8.
Gene3D; 3.40.50.1820; -; 1.
Gene3D; 4.10.800.10; -; 7.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR002018; CarbesteraseB.
InterPro; IPR019819; Carboxylesterase_B_CS.
InterPro; IPR016324; Thyroglobulin.
InterPro; IPR000716; Thyroglobulin_1.
InterPro; IPR036857; Thyroglobulin_1_sf.
InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
Pfam; PF00135; COesterase; 1.
Pfam; PF07699; Ephrin_rec_like; 1.
Pfam; PF00086; Thyroglobulin_1; 11.
PIRSF; PIRSF001831; Thyroglobulin; 1.
SMART; SM01411; Ephrin_rec_like; 1.
SMART; SM00211; TY; 10.
SUPFAM; SSF53474; SSF53474; 1.
SUPFAM; SSF57610; SSF57610; 13.
PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PROSITE; PS00484; THYROGLOBULIN_1_1; 9.
PROSITE; PS51162; THYROGLOBULIN_1_2; 11.
1: Evidence at protein level;
Complete proteome; Disease mutation; Disulfide bond; Glycoprotein;
Hormone; Iodination; Reference proteome; Repeat; Secreted; Signal;
Sulfation; Thyroid hormone; Thyroid hormones biosynthesis.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 2768 Thyroglobulin.
/FTId=PRO_0000008638.
DOMAIN 32 93 Thyroglobulin type-1 1.
{ECO:0000255|PROSITE-ProRule:PRU00500}.
DOMAIN 94 161 Thyroglobulin type-1 2.
{ECO:0000255|PROSITE-ProRule:PRU00500}.
DOMAIN 162 298 Thyroglobulin type-1 3.
{ECO:0000255|PROSITE-ProRule:PRU00500}.
DOMAIN 299 359 Thyroglobulin type-1 4.
{ECO:0000255|PROSITE-ProRule:PRU00500}.
DOMAIN 605 658 Thyroglobulin type-1 5.
{ECO:0000255|PROSITE-ProRule:PRU00500}.
DOMAIN 659 726 Thyroglobulin type-1 6.
{ECO:0000255|PROSITE-ProRule:PRU00500}.
DOMAIN 727 922 Thyroglobulin type-1 7.
{ECO:0000255|PROSITE-ProRule:PRU00500}.
DOMAIN 923 1074 Thyroglobulin type-1 8.
{ECO:0000255|PROSITE-ProRule:PRU00500}.
DOMAIN 1075 1146 Thyroglobulin type-1 9.
{ECO:0000255|PROSITE-ProRule:PRU00500}.
DOMAIN 1147 1211 Thyroglobulin type-1 10.
{ECO:0000255|PROSITE-ProRule:PRU00500}.
REPEAT 1455 1468 Type II.
REPEAT 1469 1485 Type II.
REPEAT 1486 1502 Type II.
DOMAIN 1510 1564 Thyroglobulin type-1 11.
{ECO:0000255|PROSITE-ProRule:PRU00500}.
REPEAT 1602 1722 Type IIIA.
REPEAT 1723 1891 Type IIIB.
REPEAT 1892 1994 Type IIIA.
REPEAT 1995 2127 Type IIIB.
REPEAT 2128 2185 Type IIIA.
MOD_RES 25 25 Iodotyrosine; alternate.
{ECO:0000250|UniProtKB:P01266}.
MOD_RES 25 25 Sulfotyrosine; alternate. {ECO:0000250}.
MOD_RES 25 25 Thyroxine; alternate.
{ECO:0000250|UniProtKB:P01266}.
MOD_RES 25 25 Triiodothyronine; alternate.
{ECO:0000250|UniProtKB:P01266}.
MOD_RES 150 150 Diiodotyrosine; alternate.
{ECO:0000250|UniProtKB:P01266}.
MOD_RES 150 150 Iodotyrosine; alternate.
{ECO:0000250|UniProtKB:P01266}.
MOD_RES 259 259 Iodotyrosine.
{ECO:0000250|UniProtKB:P01266}.
MOD_RES 704 704 Diiodotyrosine; alternate.
{ECO:0000250|UniProtKB:P01266}.
MOD_RES 704 704 Iodotyrosine; alternate.
{ECO:0000250|UniProtKB:P01266}.
MOD_RES 704 704 Thyroxine; alternate.
{ECO:0000250|UniProtKB:P01266}.
MOD_RES 704 704 Triiodothyronine; alternate.
{ECO:0000250|UniProtKB:P01266}.
MOD_RES 785 785 Iodotyrosine.
{ECO:0000250|UniProtKB:P01266}.
MOD_RES 867 867 Diiodotyrosine; alternate.
{ECO:0000250|UniProtKB:P01266}.
MOD_RES 867 867 Iodotyrosine; alternate.
{ECO:0000250|UniProtKB:P01266}.
MOD_RES 884 884 Diiodotyrosine.
{ECO:0000250|UniProtKB:P01266}.
MOD_RES 993 993 Diiodotyrosine; alternate.
{ECO:0000250|UniProtKB:P01266}.
MOD_RES 993 993 Iodotyrosine; alternate.
{ECO:0000250|UniProtKB:P01266}.
MOD_RES 1310 1310 Iodotyrosine.
{ECO:0000250|UniProtKB:P01266}.
MOD_RES 2184 2184 Iodotyrosine.
{ECO:0000250|UniProtKB:P01266}.
MOD_RES 2574 2574 Diiodotyrosine; alternate.
{ECO:0000250|UniProtKB:P01266}.
MOD_RES 2574 2574 Iodotyrosine; alternate.
{ECO:0000250|UniProtKB:P01266}.
MOD_RES 2574 2574 Thyroxine; alternate.
{ECO:0000250|UniProtKB:P01266}.
MOD_RES 2574 2574 Triiodothyronine; alternate.
{ECO:0000250|UniProtKB:P01266}.
MOD_RES 2588 2588 Iodotyrosine.
{ECO:0000250|UniProtKB:P01266}.
MOD_RES 2618 2618 Iodotyrosine.
{ECO:0000250|UniProtKB:P01266}.
MOD_RES 2698 2698 Diiodotyrosine.
{ECO:0000250|UniProtKB:P01266}.
MOD_RES 2766 2766 Diiodotyrosine; alternate.
{ECO:0000250|UniProtKB:P01266}.
MOD_RES 2766 2766 Iodotyrosine; alternate.
{ECO:0000250|UniProtKB:P01266}.
MOD_RES 2766 2766 Thyroxine; alternate.
{ECO:0000250|UniProtKB:P01266}.
MOD_RES 2766 2766 Triiodothyronine; alternate.
{ECO:0000250|UniProtKB:P01266}.
CARBOHYD 111 111 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 199 199 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 484 484 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 496 496 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 545 545 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 748 748 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 817 817 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 948 948 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1017 1017 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1141 1141 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1349 1349 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1365 1365 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1715 1715 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1773 1773 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1866 1866 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1937 1937 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2012 2012 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2122 2122 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2251 2251 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2296 2296 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2445 2445 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2583 2583 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 35 53 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 64 71 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 73 93 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 97 121 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 132 139 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 141 161 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 165 184 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 195 236 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 302 320 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 331 337 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 339 365 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 608 620 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 631 636 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 638 658 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 662 687 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 698 703 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 705 726 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 730 763 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 774 899 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 901 922 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 1043 1050 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 1052 1074 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 1078 1109 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 1127 1146 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 1150 1170 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 1182 1189 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 1191 1211 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 1513 1522 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 1542 1564 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 2265 2282 {ECO:0000255|PROSITE-ProRule:PRU00500}.
VARIANT 2320 2320 G -> R (in hypothyroidism; suppress
secretion of Tg).
{ECO:0000269|PubMed:11089535}.
CONFLICT 44 44 L -> V (in Ref. 4; AAA50379).
{ECO:0000305}.
CONFLICT 678 678 A -> V (in Ref. 2; AAF34909).
{ECO:0000305}.
CONFLICT 1492 1492 C -> F (in Ref. 2; AAF34909).
{ECO:0000305}.
CONFLICT 1732 1733 CC -> KS (in Ref. 2; AAF34909).
{ECO:0000305}.
CONFLICT 1914 1914 L -> F (in Ref. 5; CAA26183).
{ECO:0000305}.
CONFLICT 2043 2043 R -> A (in Ref. 5; CAA26183).
{ECO:0000305}.
CONFLICT 2081 2081 Q -> K (in Ref. 5; CAA26183).
{ECO:0000305}.
CONFLICT 2126 2126 A -> V (in Ref. 5; CAA26183).
{ECO:0000305}.
CONFLICT 2153 2153 R -> K (in Ref. 5; CAA26183).
{ECO:0000305}.
CONFLICT 2169 2169 S -> N (in Ref. 5; CAA26183).
{ECO:0000305}.
CONFLICT 2611 2611 M -> I (in Ref. 5; CAA26183).
{ECO:0000305}.
CONFLICT 2658 2658 Q -> H (in Ref. 5; CAA26183).
{ECO:0000305}.
SEQUENCE 2768 AA; 304645 MW; 290DD6943FF23F3D CRC64;
MMTLVLWVST LLSSVCLVAA NIFEYQVDAQ PLRPCELQRE KAFLKQDEYV PQCSEDGSFQ
TVQCQNDGQS CWCVDSDGTE VPGSRQLGRP TACLSFCQLH KQRILLSSYI NSTDALYLPQ
CQDSGNYAPV QCDLQQVQCW CVDTEGMEVY GTRQQGRPTR CPRSCEIRSR RLLHGVGDKS
PPQCDADGEF MPVQCKFVNT TDMMIFDLIH NYNRFPDAFV TFSAFRNRFP EVSGYCYCAD
SQGRELAETG LELLLDEIYD TIFAGLDQAS TFTQSTMYRI LQRRFLAIQL VISGRFRCPT
KCEVEQFTAT SFGHPYIPSC HRDGHYQTVQ CQMERMCWCV DAQGIEIPGT RQQGQPLFCA
KDQSCASERQ QALSRLYFET PGYFSPQDLL SSEDRLVPVS GARLDISCPP RIKELFVDSG
LLRSIAVERY QQLSESRSLL REAIRAIFPS RELAGLALQF TTNPKRLQQN LFGGTFLVNA
AQLNLSGALG TRSTFNFSQF FQQFGLPGFL VRDRATDLAK LLPVSLDSSP TPVPLRVPEK
RVAMNKSVVG TFGFKVNLQE NQDALKFLVS LMELPEFLVF LQRAVSVPED RARDLGDVME
MVFSAQACKQ TSGRFFVPSC TAEGSYEDIQ CYAGECWCVN SQGKEVEGSR VSGGHPRCPT
KCEKQRAQMQ NLAGAQPAGS SFFVPTCTSE GYFLPVQCFN SECYCVDAEG QVIPGTQSTI
GEPKLCPSVC QLQAEQAFLG VVGVLLSNSS MVPPISSVYI PQCSTSGQWM PVQCDGPHEQ
VFEWYERWNT QNSDGQELTT ATLLMKLMSY REVASTNFSL FLQSLYDAGQ QSIFPVLAQY
PSLQDVPQVV LEGATIQPGE NIFLDPYIFW QILNGQLSQY PGPYSDFSMP LEHFNLRSCW
CVDEAGQELD GTRTRAGEIP ACPGPCEEVK FRVLKFIKET EEIVSASNAS SFPLGESFLV
AKGIQLTSEE LGLPPLYPSR EAFSEKFLRG SEYAIRLAAQ STLTFYQKLR ASLGESNGTA
SLLWSGPYMP QCNTIGGWEP VQCHPGTGQC WCVDGWGELI PGSLMARSSQ MPQCPTSCEL
SRANGLISAW KQAGHQRNPG PGDLFTPVCL QTGEYVRQQT SGTGAWCVDP SSGEGVPTNT
NSSAQCPGLC DALKSRVLSR KVGLGYTPVC EALDGGFSPV QCDLAQGSCW CVLASGEEVP
GTRVVGTQPA CESPQCPLPF SGSDVTDGVV FCETASSSGV TTVQQCQLFC RQGLRNVFSP
GPLICNLESQ RWVTLPLPRA CQRPQLWQTM QTQAHFQLLL PPGKMCSIDY SGLLQAFQVF
ILDELITRGF CQIQVKTFGT LVSRTVCDNS SIQVGCLTAE RLGVNATWKL QLEDISVGSL
PNLHSIERAL MGQDLLGRFA NLIQSGKFQL HLDSKTFSAD TILYFLNGDR FVTSPMTQLG
CLEGFYRVST TSQDPLGCVK CPEGSFSQDG KCTPCPAGTY QGQAGSSACI PCPRGRTTTI
TGAFSKTHCV TDCQRDEAGL QCDQNGQYQA NQKDMDSGEV FCVDSEGQRL QWLQTEAGLS
ESQCLMMRKF EKAPESKVIF DASSPVIVKS RVPSANSPLV QCLADCADDE ACSFVTVSSM
SSEVSCDLYS WTRDNFACVT SDQEEDAVDS LKETSFGSLR CQVKVRNSGK DSLAVYVKKG
HEFTASGQKS FEPTGFQNVL SGLYSSVVFS ALGTNLTDTH LFCLLACDQD SCCDGFIVTQ
VKEGPTICGL LSAPDILVCH INDWRDASDT QANGTCAGVT YDQGSRQMTM SLGGQEFLQG
LTLLEGTQDS FISFQQVYLW KDSDIGSRPE SMGCGRGMVP KSEAPEGADM ATELFSPVDI
TQVIVNTSHS LPSQQYWLST HLFSAEQANL WCLSRCAQEP VFCQLADIME SSSLYFTCSL
YPEAQVCDND VESNAKNCSQ ILPRQPTALF QRKVVLNDRV KNFYTRLPFQ KLSGISIRDR
IPMSEKLISN GFFECERLCD RDPCCTGFGF LNVSQMQGGE MTCLTLNSMG IQTCSEENGA
TWRILDCGSE DTEVHTYPFG WYQKPAVWSD APSFCPSAAL QSLTEEKVAL DSWQTLALSS
VIIDPSIKHF DVAHISISAT RNFSLAQDFC LQECSRHQDC LVTTLQIQQG VVRCVFYPDI
QSCEHSLRSK TCWLLLHEEA AYIYRKSGAP LHQSDGISTP SVHIDSFGQL QGGSQVVKVG
TAWKQVYQFL GVPYAAPPLA ENRFQAPEVL NWTGSWDATK LRSSCWQPGT RTPTPPQISE
DCLYLNVFVP ENLVSNASVL VFFHNTVEME GSGGQLNIDG SILAAVGNLI VVTANYRLGV
FGFLSSGSDE VAGNWGLLDQ VAALTWVQTH IGAFGGDPQR VTLAADRGGA DVASIHLLIT
RPTRLQLFRK ALLMGGSALS PAAIISPDRA QQQAAALAKE VGCPNSSVQE VVSCFRQKPA
NILNEAQTKL LAVSGPFHYW GPVVDGQYLR ELPSRRLKRP LPVKVDLLIG GSQDDGLINR
AKAVKQFEES QGRTNSKTAF YQALQNSLGG EDSDARILAA AIWYYSLEHS TDDYASFSRA
LENATRDYFI ICPIVNMASL WARRTRGNVF MYHVPESYGH GSLELLADVQ YAFGLPFYSA
YQGYFSTEEQ SLSLKVMQYF SNFIRSGNPN YPHEFSQKAA EFATPWPDFV PGAGGESYKE
LSAQLPNRQG LKKADCSFWS KYIQTLKDAD GAKDAQLTKS GEEDLEVGPG SEEDFSGSLE
PVPKSYSK


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1B-607-C100 Mouse Monoclonal to Thyroglobulin Antigen Thyroglobulin Species Reactivity Human Negative Species Clone IP26 Isotype IgG1 Application FC Immunogen Format biotin 0.1 mg
1B-607-C025 Mouse Monoclonal to Thyroglobulin Antigen Thyroglobulin Species Reactivity Human Negative Species Clone IP26 Isotype IgG1 Application FC Immunogen Format biotin 0.025 mg
1107NF-v1059 Monoclonal Antibodies: Thyroglobulin(Clone b34.1); reactive species: Human; Clone: B34.1; Isotype: IgG1; Specificity: Thyroglobulin(Clone b34.1) 0.5/ml
SCH-PHP236 NATIVE HUMAN THYROGLOBULIN , Product Type Purified Protein, Specificity THYROGLOBULIN, Target Species Human, Host N_A, Format Purified, Isotypes , Applications E, Clone 1 mg
PHP236 NATIVE HUMAN THYROGLOBULIN , Product Type Purified Protein, Specificity THYROGLOBULIN, Target Species Human, Host N_A, Format Purified, Isotypes , Applications E, Clone 1 mg
8900-1004 NATIVE HUMAN THYROGLOBULIN, Product Type Purified Protein, Specificity THYROGLOBULIN, Target Species Human, Host N_A, Format Purified, Isotypes , Applications E, Clone 1 mg
8900-1354 NATIVE BOVINE THYROGLOBULIN, Product Type Purified Protein, Specificity THYROGLOBULIN, Target Species Bovine, Host N_A, Format Purified, Isotypes , Applications E, Clone 100 mg
SCH-8900-1004 NATIVE HUMAN THYROGLOBULIN, Product Type Purified Protein, Specificity THYROGLOBULIN, Target Species Human, Host N_A, Format Purified, Isotypes , Applications E, Clone 1 mg
SCH-8900-1354 NATIVE BOVINE THYROGLOBULIN, Product Type Purified Protein, Specificity THYROGLOBULIN, Target Species Bovine, Host N_A, Format Purified, Isotypes , Applications E, Clone 100 mg
20-272-192303 Thyroglobulin - Mouse monoclonal [12G9] to Thyroglobulin; Monoclonal 1 mg
SCH-MCA2868 MOUSE ANTI HUMAN THYROGLOBULIN, Product Type Monoclonal Antibody, Specificity THYROGLOBULIN, Target Species Human, Host Mouse, Format Purified, Isotypes IgG1, Applications E, Clone 5G4 0.2 mg
MCA2868 MOUSE ANTI HUMAN THYROGLOBULIN, Product Type Monoclonal Antibody, Specificity THYROGLOBULIN, Target Species Human, Host Mouse, Format Purified, Isotypes IgG1, Applications E, Clone 5G4 0.2 mg
MCA2867 MOUSE ANTI HUMAN THYROGLOBULIN, Product Type Monoclonal Antibody, Specificity THYROGLOBULIN, Target Species Human, Host Mouse, Format Purified, Isotypes IgG2a, Applications E, Clone 11A16 0.2 mg
SCH-MCA2867 MOUSE ANTI HUMAN THYROGLOBULIN, Product Type Monoclonal Antibody, Specificity THYROGLOBULIN, Target Species Human, Host Mouse, Format Purified, Isotypes IgG2a, Applications E, Clone 11A16 0.2 mg


 

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