Disulfide-isomerase TMX3 Recombinant Protein | TMX3 recombinant protein

Recombinant Human Protein disulfide-isomerase TMX3

Cat. Num. AAA1390095

• Gene Names: TMX3; PDIA13; TXNDC10
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Disulfide-isomerase TMX3; Recombinant Human Protein disulfide-isomerase TMX3; Thioredoxin domain-containing protein 10; Thioredoxin-related transmembrane protein 3; TMX3 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 25-195aa; Full Length of Isoform 2
• Sequence: KGFVEDLDESFKENRNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSPVKVGKMDATSYSSIASEFGVRGYPTIKLLKGDLAYNYRGPRTKDDIIEFAHRVSGALIRPLPSQQMFEHMQKRHRVFFVYVGGESPLKEKYIDAASELIVYTYFFSASEEVVPEVIFKI
• Sequence Length: 195

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for TMX3 recombinant protein

Probable disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May act as a dithiol oxidase.

Product Categories/Family for TMX3 recombinant protein

Metabolism

References

Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro.Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.DNA Res. 8:85-95(2001) Complete sequencing and characterization of 21,243 full-length human cDNAs.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.Nat. Genet. 36:40-45(2004) The full-ORF clone resource of the German cDNA consortium.Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.BMC Genomics 8:399-399(2007) Identification and characterization of a novel thioredoxin-related transmembrane protein of the endoplasmic reticulum.Haugstetter J., Blicher T., Ellgaard L.J. Biol. Chem. 280:8371-8380(2005) Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.J. Proteome Res. 8:651-661(2009) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011)

NCBI and Uniprot Product Information

• NCBI GI #: 38505222
• NCBI GeneID: 54495
• NCBI Accession #: NP_061895.3
• NCBI GenBank Nucleotide #: NM_019022.3
• UniProt Accession #: Q96JJ7; Q52LT7; Q8N5J0; Q9NWJ9; B3KV75
• Molecular Weight: 35.6 kDa
• NCBI Official Synonym Full Names: thioredoxin related transmembrane protein 3
• NCBI Official Symbol: TMX3
• NCBI Official Synonym Symbols: PDIA13; TXNDC10
• NCBI Protein Information: protein disulfide-isomerase TMX3
• UniProt Protein Name: Protein disulfide-isomerase TMX3
• Protein Family: Protein disulfide-isomerase
• UniProt Gene Name: TMX3
• UniProt Synonym Gene Names: KIAA1830; TXNDC10
• UniProt Entry Name: TMX3_HUMAN

Uniprot Description

TXNDC10: Probable disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May act as a dithiol oxidase. Belongs to the protein disulfide isomerase family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Membrane protein, integral; EC 5.3.4.1; Isomerase

Chromosomal Location of Human Ortholog: 18q22

Cellular Component: cell surface; endoplasmic reticulum membrane; integral to membrane

Molecular Function: protein binding; protein disulfide isomerase activity; thiol oxidase activity

Biological Process: cell redox homeostasis; peptidyl-cysteine oxidation; protein folding