Purity/Purification
Greater than 90% as determined by SDS-PAGE.
Form/Format
Liquid containing glycerol
Sequence Positions
21-300
Sequence
IFEYQVDAQPLRPCELQRETAFLKQADYVPQCAEDGSFQTVQCQNDGRSCWCVGANGSEVLGSRQPGRPVACLSFCQLQKQQILLSGYINSTDTSYLPQCQDSGDYAPVQCDVQQVQCWCVDAEGMEVYGTRQLGRPKRCPRSCEIRNRRLLHGVGDKSPPQCSAEGEFMPVQCKFVNTTDMMIFDLVHSYNRFPDAFVTFSSFQRRFPEVSGYCHCADSQGRELAETGLELLLDEIYDTIFAGLDLPSTFTETT
Sequence Length
2768
Product Note
Applications are user defined. Product is developed and quality control tested in house, data or additional information may be provided upon request. The researcher needs to establish and confirm the suitability of the product for their application.
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
Related Product Information for TG recombinant protein
Precursor of the iodinated thyroid hormones thyroxine (T4) and triiodothyronine (T3).
Product Categories/Family for TG recombinant protein
References
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)
NCBI and Uniprot Product Information
NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
Molecular Weight
59kD
NCBI Official Full Name
thyroglobulin
NCBI Official Synonym Full Names
thyroglobulin
NCBI Official Symbol
TG
NCBI Official Synonym Symbols
TGN; AITD3
NCBI Protein Information
thyroglobulin
UniProt Protein Name
Thyroglobulin
UniProt Gene Name
TG
UniProt Synonym Gene Names
Tg
UniProt Entry Name
THYG_HUMAN
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Product Notes
The TG tg (Catalog #AAA113454) is a Recombinant Protein and is intended for research purposes only. The product is available for immediate purchase. The immunogen sequence is 21-300. The amino acid sequence is listed below: IFEYQVDAQP LRPCELQRET AFLKQADYVP QCAEDGSFQT VQCQNDGRSC WCVGANGSEV LGSRQPGRPV ACLSFCQLQK QQILLSGYIN STDTSYLPQC QDSGDYAPVQ CDVQQVQCWC VDAEGMEVYG TRQLGRPKRC PRSCEIRNRR LLHGVGDKSP PQCSAEGEFM PVQCKFVNTT DMMIFDLVHS YNRFPDAFVT FSSFQRRFPE VSGYCHCADS QGRELAETGL ELLLDEIYDT IFAGLDLPST FTETT. It is sometimes possible for the material contained within the vial of "Thyroglobulin, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.Precautions
All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.Disclaimer
Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.Item has been added to Shopping Cart
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