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Amino acids 49-102 form the expressed segment for recombinant Human TMX2. The calculated molecular weight for this TMX2 protein is 33.3 kDa. The TMX2 protein was expressed in e.coli. The TMX2 coding gene included the N-terminal GST tag, which simplifies the detection and purification processes of the recombinant TMX2 protein in following stages of expression and purification.Thioredoxin-related transmembrane protein 2 (TMX2) is a member of the thioredoxin superfamily, playing a role in redox regulation within the endoplasmic reticulum (ER). TMX2 contains a thioredoxin-like domain and multiple transmembrane helices, suggesting its association with the ER membrane. As part of the ER redox system, TMX2 is involved in maintaining protein folding and quality control by participating in disulfide bond formation and reduction. It may interact with other ER-resident proteins and contribute to the regulation of cellular responses to oxidative stress. Research on TMX2 spans various areas, including investigations into its specific redox functions, potential interactions with client proteins, and implications in cellular processes related to ER homeostasis.
Amino acids 49-102 form the expressed segment for recombinant Human TMX2. The calculated molecular weight for this TMX2 protein is 33.3 kDa. The TMX2 protein was expressed in e.coli. The TMX2 coding gene included the N-terminal GST tag, which simplifies the detection and purification processes of the recombinant TMX2 protein in following stages of expression and purification.Thioredoxin-related transmembrane protein 2 (TMX2) is a member of the thioredoxin superfamily, playing a role in redox regulation within the endoplasmic reticulum (ER). TMX2 contains a thioredoxin-like domain and multiple transmembrane helices, suggesting its association with the ER membrane. As part of the ER redox system, TMX2 is involved in maintaining protein folding and quality control by participating in disulfide bond formation and reduction. It may interact with other ER-resident proteins and contribute to the regulation of cellular responses to oxidative stress. Research on TMX2 spans various areas, including investigations into its specific redox functions, potential interactions with client proteins, and implications in cellular processes related to ER homeostasis.
| Cat.No | ACP03750 | Target Name | TMX2 |
|---|---|---|---|
| Form | Liquid or Lyophilized powder | Expression System | E.coli |
| Expression Range | 49-102aa | Mol Weight | 33.3kDa |
| Protein Length | Extracellular Domain | Purity | Greater than 90% as determined by SDS-PAGE. |
| Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | Q9Y320 |
|---|
Uniprot Id
Q9Y320
Target Species
Human
Target Name
TMX2
Target Full Name
Thioredoxin-related transmembrane protein 2
Target Function
Endoplasmic reticulum and mitochondria-associated protein that probably functions as a regulator of cellular redox state and thereby regulates protein post-translational modification, protein folding and mitochondrial activity. Indirectly regulates neuronal proliferation, migration, and organization in the developing brain.
Target Subcellular Location
Endoplasmic reticulum membrane; Single-pass type I membrane protein. Mitochondrion membrane.
Target Tissue Specificity
Widely expressed.
Target Research Area
Cell Biology
Target Synonyms
Cell proliferation inducing gene 26 protein; Cell proliferation-inducing gene 26 protein; CGI 31; Growth inhibiting gene 11; PDIA12; PIG26; Protein disulfide isomerase family A; member 12; Thioredoxin domain containing protein 14; Thioredoxin domain-containing protein 14; Thioredoxin related transmembrane protein 2; Thioredoxin-related transmembrane protein 2; tmx2; TMX2_HUMAN; TXNDC14
Target Background
This gene encodes a member of the disulfide isomerase (PDI) family of endoplasmic reticulum (ER) proteins that catalyze protein folding and thiol-disulfide interchange reactions. The encoded protein has an N-terminal ER-signal sequence, a catalytically active thioredoxin domain, one transmembrane domain and a C-terminal ER-retention sequence. This protein is enriched on the mitochondria-associated-membrane of the ER via palmitoylation of two of its cytosolically exposed cysteines.
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