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Specifications
- Protein/peptide type:Recombinant
- Source:E. coli
- Species:Human
- Size:0.05 mg
- Tag sequence:N-6 His tag
- Storage conditions:Lyophilized protein should be stored at −20 °C, though stable at room temperature for 3 weeks. Reconstituted protein solution can be stored at 4-7 °C for 2-7 days. Aliquots of reconstituted samples are stable at −20 °C for 3 months.
- Endotoxin content:<0.1 ng/ug (1 IEU/ug) as determined by LAL test.
- Protein synonyms:Cell proliferation-inducing gene 26 protein|TXNDC14|Thioredoxin-related transmembrane protein 2|TMX2|Thioredoxin domain-containing protein 14
- Protein/peptide name:TMX2
- Purity:> 95% as determined by reducing SDS-PAGE
- Molecular weight:21.9 kD
- Sequence:Met125-Lys296
- Formulation:Lyophilized from a 0.2 um filtered solution of 20mM Tris,150mM NaCl,pH8.0. Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100 ug/ml. Dissolve the Lyophilized protein in ddH2O. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
- Tested applications:Bioassay
- Cat. no.:75791-088
- Supplier No.:92-247
Specifications
About this item
TMX2 is a single-pass type I membrane protein and contains 1 thioredoxin domain. Thioredoxin plays an important role in various cellular processes through redox regulation. The molecular cloning and characterization of one member of the thioredoxin superfamily, designated as TMX2.The TMX2 cDNA consists of 1644 nucleotides and contains an open reading frame encoding a protein of 372 amino acids with a predicted molecular mass of 42.5 kDa and an isoelectric point of 8.94. The TMX2 protein may possess an N-terminal signal peptide, a potential transmembrane domain, an Myb DNA-binding domain repeat signature, a thioredoxin consensus pattern, an endoplasmic reticulum (ER) membrane retention signal (KKXX-like motif), and a dileucine motif in the tail.
- Fusion-Tag: N-6 His tag
This recombinant protein can be used for biological assays. For research use only.