protein

Recombinant Human Thyroglobulin(TG)

MBS954199

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human Thyroglobulin(TG)

Thyroglobulin

thyroglobulin; Thyroglobulin; thyroglobulin; thyroglobulin

TG

TG; TG; TGN; AITD3; Tg

THYG_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

21-300

2768

IFEYQVDAQPLRPCELQRETAFLKQADYVPQCAEDGSFQ
TVQCQNDGRSCWCVGANGSEVLGSRQPGRPVACLSFCQL
QKQQILLSGYINSTDTSYLPQCQDSGDYAPVQCDVQQVQ
CWCVDAEGMEVYGTRQLGRPKRCPRSCEIRNRRLLHGVG
DKSPPQCSAEGEFMPVQCKFVNTTDMMIFDLVHSYNRFP
DAFVTFSSFQRRFPEVSGYCHCADSQGRELAETGLELLL
DEIYDTIFAGLDLPSTFTETT

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Metabolism

Precursor of the iodinated thyroid hormones thyroxine (T4) and triiodothyronine (T3).

Primary structure of human thyroglobulin deduced from the sequence of its 8448-base complementary DNA.Malthiery Y., Lissitzky S.Eur. J. Biochem. 165:491-498(1987) The revised 8307 base pair coding sequence of human thyroglobulin transiently expressed in eukaryotic cells.van de Graaf S.A.R., Pauws E., de Vijlder J.J.M., Ris-Stalpers C.Eur. J. Endocrinol. 136:508-515(1997) DNA sequence and analysis of human chromosome 8.Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.Nature 439:331-335(2006) Sequence of the 5'-end quarter of the human-thyroglobulin messenger ribonucleic acid and of its deduced amino-acid sequence.Malthiery Y., Lissitzky S.Eur. J. Biochem. 147:53-58(1985) Structural organization of the 5' region of the thyroglobulin gene. Evidence for intron loss and 'exonization' during evolution.Parma J., Christophe D., Pohl V., Vassart G.J. Mol. Biol. 196:769-779(1987) An unusually long poly(purine) -poly(pyrimidine) sequence is located upstream from the human thyroglobulin gene.Christophe D., Cabrer B., Bacolla A., Targovnik H.M., Pohl V., Vassart G.Nucleic Acids Res. 13:5127-5144(1985) Genomic organization of the 5' region of the human thyroglobulin gene.Moya C.M., Mendive F.M., Rivolta C.M., Vassart G., Targovnik H.M.Eur. J. Endocrinol. 143:789-798(2000) Genomic organization of the 3' region of the human thyroglobulin gene.Mendive F.M., Rivolta C.M., Vassart G., Targovnik H.M.Thyroid 9:903-912(1999) Identification of a minor Tg mRNA transcript in RNA from normal and goitrous thyroids.Targovnik H.M., Cochaux P., Corach D., Vassart G.Mol. Cell. Endocrinol. 84:R23-R26(1992) Hormone synthesis in human thyroglobulin possible cleavage of the polypeptide chain at the tyrosine donor site.Marriq C., Lejeune P.J., Venot N., Vinet L.FEBS Lett. 242:414-418(1989) Preferential sites of proteolytic cleavage of bovine, human and rat thyroglobulin. The use of limited proteolysis to detect solvent-exposed regions of the primary structure.Gentile F., Salvatore G.Eur. J. Biochem. 218:603-621(1993) Characterization of hormonogenic sites in an N-terminal, cyanogen bromide fragment of human thyroglobulin.Xiao S., Pollock H.G., Taurog A., Rawitch A.B.Arch. Biochem. Biophys. 320:96-105(1995) Glycosylation in human thyroglobulin location of the N-linked oligosaccharide units and comparison with bovine thyroglobulin.Yang S.X., Pollock H.G., Rawitch A.B.Arch. Biochem. Biophys. 327:61-70(1996) Characterization of the type-1 repeat from thyroglobulin, a cysteine-rich module found in proteins from different families.Molina F., Bouanani M., Pau B., Granier C.Eur. J. Biochem. 240:125-133(1996) Consensus sequences for early iodination and hormonogenesis in human thyroglobulin.Lamas L., Anderson P.C., Fox J.W., Dunn J.T.J. Biol. Chem. 264:13541-13545(1989) Sulfated tyrosines of thyroglobulin are involved in thyroid hormone synthesis.Nlend M.-C., Cauvi D., Venot N., Chabaud O.Biochem. Biophys. Res. Commun. 262:193-197(1999) The hormonogenic tyrosine 5 of porcine thyroglobulin is sulfated.Venot N., Nlend M.-C., Cauvi D., Chabaud O.Biochem. Biophys. Res. Commun. 298:193-197(2002) A single chondroitin 6-sulfate oligosaccharide unit at Ser-2730 of human thyroglobulin enhances hormone formation and limits proteolytic accessibility at the carboxyl terminus. Potential insights into thyroid homeostasis and autoimmunity.Conte M., Arcaro A., D'Angelo D., Gnata A., Mamone G., Ferranti P., Formisano S., Gentile F.J. Biol. Chem. 281:22200-22211(2006) Thyroglobulin gene point mutation associated with non-endemic simple goitre.Corral J., Martin C., Perez R., Sanchez I., Mories M.T., San Millan J.L., Miralles J.M., Gonzalez-Sarmiento R.Lancet 341:462-464(1993) Two novel cysteine substitutions (C1263R and C1995S) of thyroglobulin cause a defect in intracellular transport of thyroglobulin in patients with congenital goiter and the variant type of adenomatous goiter.Hishinuma A., Takamatsu J., Ohyama Y., Yokozawa T., Kanno Y., Kuma K., Yoshida S., Matsuura N., Ieiri T.J. Clin. Endocrinol. Metab. 84:1438-1444(1999) Amino acid substitutions in the thyroglobulin gene are associated with susceptibility to human and murine autoimmune thyroid disease.Ban Y., Greenberg D.A., Concepcion E., Skrabanek L., Villanueva R., Tomer Y.Proc. Natl. Acad. Sci. U.S.A. 100:15119-15124(2003) A novel compound heterozygous mutation in the thyroglobulin gene resulting in congenital goitrous hypothyroidism with high serum triiodothyronine levels.Kitanaka S., Takeda A., Sato U., Miki Y., Hishinuma A., Ieiri T., Igarashi T.J. Hum. Genet. 51:379-382(2006) Congenital hypothyroidism with goitre caused by new mutations in the thyroglobulin gene.Caputo M., Rivolta C.M., Esperante S.A., Gruneiro-Papendieck L., Chiesa A., Pellizas C.G., Gonzalez-Sarmiento R., Targovnik H.M.Clin. Endocrinol. (Oxf.) 67:351-357(2007) Thyroglobulin gene mutations producing defective intracellular transport of thyroglobulin are associated with increased thyroidal type 2 iodothyronine deiodinase activity.Kanou Y., Hishinuma A., Tsunekawa K., Seki K., Mizuno Y., Fujisawa H., Imai T., Miura Y., Nagasaka T., Yamada C., Ieiri T., Murakami M., Murata Y.J. Clin. Endocrinol. Metab. 92:1451-1457(2007) The p.A2215D thyroglobulin gene mutation leads to deficient synthesis and secretion of the mutated protein and congenital hypothyroidism with wide phenotype variation.Pardo V., Vono-Toniolo J., Rubio I.G., Knobel M., Possato R.F., Targovnik H.M., Kopp P., Medeiros-Neto G.J. Clin. Endocrinol. Metab. 94:2938-2944(2009)

55770862

NP_003226.4

NM_003235.4

P01266

59kD

Autoimmune Thyroid Disease Pathway (83121); Autoimmune Thyroid Disease Pathway (533); Thyroid Hormone Synthesis Pathway (835410); Thyroid Hormone Synthesis Pathway (839541); Thyroxine (Thyroid Hormone) Production Pathway (920992)

Thyroglobulin (Tg) is a glycoprotein homodimer produced predominantly by the thryroid gland. It acts as a substrate for the synthesis of thyroxine and triiodothyronine as well as the storage of the inactive forms of thyroid hormone and iodine. Thyroglobulin is secreted from the endoplasmic reticulum to its site of iodination, and subsequent thyroxine biosynthesis, in the follicular lumen. Mutations in this gene cause thyroid dyshormonogenesis, manifested as goiter, and are associated with moderate to severe congenital hypothyroidism. Polymorphisms in this gene are associated with susceptibility to autoimmune thyroid diseases (AITD) such as Graves disease and Hashimoto thryoiditis. [provided by RefSeq, Nov 2009]

TG: Precursor of the iodinated thyroid hormones thyroxine (T4) and triiodothyronine (T3). Defects in TG are the cause of thyroid dyshormonogenesis 3 (TDH3). A disorder due to thyroid dyshormonogenesis, causing large goiters of elastic and soft consistency in the majority of patients. Although the degree of thyroid dysfunction varies considerably among patients with defective thyroglobulin synthesis, patients usually have a relatively high serum free triiodothyronine (T3) concentration with disproportionately low free tetraiodothyronine (T4) level. The maintenance of relatively high free T3 levels prevents profound tissue hypothyroidism except in brain and pituitary, which are dependent on T4 supply, resulting in neurologic and intellectual defects in some cases. Variations in TG are associated with susceptibility to autoimmune thyroid disease type 3 (AITD3). AITDs including Graves disease (GD) and Hashimoto thyroiditis (HT), are among the most common human autoimmune diseases. They are complex diseases, which are caused by an interaction between susceptibility genes and nongenetic factors, such as infection. Belongs to the type-B carboxylesterase/lipase family. 2 isoforms of the human protein are produced by alternative splicing. Protein type: Secreted, signal peptide; Secreted. Chromosomal Location of Human Ortholog: 8q24. Cellular Component: endoplasmic reticulum; extracellular region; extracellular space; Golgi apparatus; perinuclear region of cytoplasm; protein complex. Molecular Function: anion binding; chaperone binding; hormone activity; protein complex binding; protein homodimerization activity. Biological Process: hormone biosynthetic process; iodide transport; regulation of myelination; response to lipopolysaccharide; response to pH; signal transduction; thyroid gland development; thyroid hormone metabolic process; transcytosis. Disease: Autoimmune Thyroid Disease, Susceptibility To, 3; Thyroid Dyshormonogenesis 3

0.05 mg (E-Coli)

190 USD

0.05 mg (Yeast)

190

0.2 mg (E-Coli)

460

0.2 mg (Yeast)

460

0.5 mg (Yeast)

750