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TXNDC12 recombinant protein :: Thioredoxin domain-containing protein 12 Recombinant Protein

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Catalog # MBS1064185
Unit / Price
Scan QR to view Datasheet
  0.01 mg (E-Coli)  /  $160 +1 FREE 8GB USB
  0.05 mg (E-Coli)  /  $200 +1 FREE 8GB USB
  0.1 mg (E-Coli)  /  $295 +1 FREE 8GB USB
  0.2 mg (E-Coli)  /  $480 +1 FREE 8GB USB
  0.5 mg (E-Coli)  /  $790 +1 FREE 8GB USB
  1 mg (E-Coli)  /  $1,215 +1 FREE 8GB USB
Product Name

Thioredoxin domain-containing protein 12 (TXNDC12), Recombinant Protein

Full Product Name

Recombinant Human Thioredoxin domain-containing protein 12

Product Synonym Names
Endoplasmic reticulum resident protein 18; ER protein 18; ERp18; Endoplasmic reticulum resident protein 19; ER protein 19; ERp19; Thioredoxin-like protein p19h; TLP19
Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
Sequence Positions
27-172aa; Full Length
3D Structure
ModBase 3D Structure for O95881
E Coli or Yeast or Baculovirus or Mammalian Cell
Greater than 90% as determined by SDS-PAGE. (lot specific)
Liquid containing glycerol
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterile filter available upon request.
Low endotoxin available upon request.
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
ISO Certification
Manufactured in an ISO 9001:2008 Certified Laboratory.
Other Notes
Small volumes of TXNDC12 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
Related Product Information for
TXNDC12 recombinant protein
Possesses significant protein thiol-disulfide oxidase activity.
Product Categories/Family for TXNDC12 recombinant protein

TXNDC12 recombinant protein SDS-PAGE image
(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)
NCBI/Uniprot data below describe general gene information for TXNDC12. It may not necessarily be applicable to this product.
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
NCBI Official Full Name
thioredoxin domain-containing protein 12
NCBI Official Synonym Full Names
thioredoxin domain containing 12 (endoplasmic reticulum)
NCBI Official Symbol
TXNDC12  [Similar Products]
NCBI Official Synonym Symbols
AG1; AGR1; ERP16; ERP18; ERP19; TLP19; hAG-1; PDIA16; hTLP19
  [Similar Products]
NCBI Protein Information
thioredoxin domain-containing protein 12
UniProt Protein Name
Thioredoxin domain-containing protein 12
UniProt Synonym Protein Names
Endoplasmic reticulum resident protein 18; ER protein 18; ERp18; Endoplasmic reticulum resident protein 19; ER protein 19; ERp19; Thioredoxin-like protein p19; hTLP19
UniProt Gene Name
TXNDC12  [Similar Products]
UniProt Synonym Gene Names
TLP19; ER protein 18; ERp18; ER protein 19; ERp19  [Similar Products]
UniProt Entry Name
NCBI Summary for TXNDC12
This gene encodes a member of the thioredoxin superfamily. Members of this family are characterized by a conserved active motif called the thioredoxin fold that catalyzes disulfide bond formation and isomerization. This protein localizes to the endoplasmic reticulum and has a single atypical active motif. The encoded protein is mainly involved in catalyzing native disulfide bond formation and displays activity similar to protein-disulfide isomerases. This protein may play a role in defense against endoplasmic reticulum stress. Alternate splicing results in both coding and non-coding variants. [provided by RefSeq, Mar 2012]
UniProt Comments for TXNDC12
TXNDC12: Possesses significant protein thiol-disulfide oxidase activity.

Protein type: Secreted, signal peptide; Other Amino Acids Metabolism - glutathione; Secreted; Oxidoreductase; EC

Chromosomal Location of Human Ortholog: 1p32.3

Cellular Component: endoplasmic reticulum lumen

Molecular Function: peptide disulfide oxidoreductase activity; protein binding; protein-disulfide reductase (glutathione) activity

Biological Process: cell redox homeostasis
Product References and Citations for TXNDC12 recombinant protein
Isolation and characterization of a novel human thioredoxin-like gene hTLP19 encoding a secretory protein.Liu F., Rong Y.P., Zeng L.C., Zhang X., Han Z.G.Gene 315:71-78(2003) Mei G., Yu W., Gibbs R.A. The secreted protein discovery initiative (SPDI) , a large-scale effort to identify novel human secreted and transmembrane proteins a bioinformatics assessment.Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.Genome Res. 13:2265-2270(2003) Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries.Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y., Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.DNA Res. 12:117-126(2005) The DNA sequence and biological annotation of human chromosome 1.Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.Nature 441:315-321(2006) Signal peptide prediction based on analysis of experimentally verified cleavage sites.Zhang Z., Henzel W.J.Protein Sci. 13:2819-2824(2004) Functional characterization of ERp18, a new endoplasmic reticulum-located thioredoxin superfamily member.Alanen H.I., Williamson R.A., Howard M.J., Lappi A.-K., Jaentti H.P., Rautio S.M., Kellokumpu S., Ruddock L.W.J. Biol. Chem. 278:28912-28920(2003) 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) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) Solution structure and dynamics of ERp18, a small endoplasmic reticulum resident oxidoreductase.Rowe M.L., Ruddock L.W., Kelly G., Schmidt J.M., Williamson R.A., Howard M.J.Biochemistry 48:4596-4606(2009)

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