Recombinant Human Thioredoxin Domain-Containing Protein 5 (TXNDC5) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-02448P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) TXNDC5.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) TXNDC5.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) TXNDC5.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) TXNDC5.
Greater than 90% as determined by SDS-PAGE.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) TXNDC5.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) TXNDC5.

Recombinant Human Thioredoxin Domain-Containing Protein 5 (TXNDC5) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-02448P
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Product Overview

Description Recombinant Human Thioredoxin Domain-Containing Protein 5 (TXNDC5) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb Q8NBS9
Target Symbol TXNDC5
Synonyms EndoPDI; Endoplasmic reticulum protein ERp46; Endoplasmic reticulum resident protein 46; Endothelial protein disulphide isomerase; ER protein 46; ERp46; Hcc 2; MGC3178; PDIA15; Protein disulfide isomerase family A member 15; STRF8; Thioredoxin domain containing 5 (endoplasmic reticulum); Thioredoxin domain containing 5; Thioredoxin domain containing protein 5; Thioredoxin domain-containing protein 5; Thioredoxin like protein p46; Thioredoxin related protein; Thioredoxin-like protein p46; TLP46; TXND5_HUMAN; TXNDC 5; Txndc5
Species Homo sapiens (Human)
Expression System E.coli
Tag N-GST
Target Protein Sequence MEDAKVYVAKVDCTAHSDVCSAQGVRGYPTLKLFKPGQEAVKYQGPRDFQTLENWMLQTLNEEPVTPEPEVEPPSAPELKQGLYELSASNFELHVAQGDHFIKFFAPWCGHCKALAPTWEQLALGLEHSETVKIGKVDCTQHYELCSGNQVRGYPTLLWFRDGKKVDQYKGKRDLESLREYVESQLQRTETGATETVTPSEAPVLAAEPEADKGTVLALTENNFDDTIAEGITFIKFYAPWCGHCKTLAPTWEELSKKEFPGLAGVKIAEVDCTAERNICSKYSVRGYPTLLLFRGGKKVSEHSGGRDLDSLHRFVLSQAKDEL
Expression Range 1-324aa
Protein Length Full Length of Isoform 2
Mol. Weight 63.2kDa
Research Area Cell Biology
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Possesses thioredoxin activity. Has been shown to reduce insulin disulfide bonds. Also complements protein disulfide-isomerase deficiency in yeast.
Subcellular Location Endoplasmic reticulum lumen.
Protein Families Protein disulfide isomerase family
Database References

HGNC: 21073

OMIM: 616412

KEGG: hsa:81567

STRING: 9606.ENSP00000369081

UniGene: PMID: 29749460

  • TXNDC5 is also closely associated with rheumatoid arthritis, diabetes, hepatic steatosis and vitiligo. [review] PMID: 28604976
  • High TXNDC5 expression is associated with renal cell carcinoma. PMID: 26810069
  • we defined an important role of TXNDC5 in CRPC and further investigations are needed to screen TXNDC5 antagonists as a novel therapeutic approaches to treat PCa patients with Castration-resistant prostate cancer. PMID: 25500540
  • Role of ERp46 in oxidative protein folding.Independent actions of ERp46 thioredoxin domains on folding substrates.Structure of thioredoxin ERp46 domains. PMID: 24462249
  • suggest that the tumorigenic properties of ERp46 in RCC cells are not related to an inhibitory modulation of AdipoR1 PMID: 24594673
  • Endo-PDI is a novel, important mediator of AP-1-driven gene expression and endothelial angiogenic function. PMID: 24103565
  • TXNDC5 has increased expression in many tumors that is involved in the proliferation and migration of tumor cells, acting as a tumor-enhancing gene. PMID: 24100949
  • results suggest that TXNDC5 polymorphisms could be related to the development of HCC in the Korean male population PMID: 24023338
  • Hyperoxidized peroxiredoxin 2 interacts with the protein disulfide- isomerase ERp46. PMID: 23713588
  • Hypoxia induced TXCNDC5 expression, which contributed to adiponectin expression, cytokine production and the cellular proliferation and migration of fibroblasts in rheumatoid arthritis. PMID: 23326410
  • Authors show that ERp46 is able to bind to a large pool of peptides containing aromatic and basic residues via all three of its catalytic domains (a(0), a and a'), though the a(0) domain may contain the primary binding site. PMID: 23376096
  • crystal structure of the third catalytic domain of protein disulfide isomerase ERp46 (also known as protein disulfide isomerase A5 and TXNDC5) was determined to 2.0 A resolution PMID: 22505402
  • TXNDC5 has a genetic effect on the risk of rheumatoid arthritis and ankylosing spondylitis PMID: 21801346
  • Overexpression of the TXNDC5 protein is associated with non-small cell lung carcinoma. PMID: 21617212
  • results suggest that TXNDC5 gene polymorphisms are associated with the development of nonsegmental vitiligo in the Korean population. PMID: 19906073
  • TXNDC5 can promote the growth and proliferation of gastric cells. Silencing of TXNDC5 can restrain the growth and proliferation of gastric cancer cells. PMID: 20157732
  • these results establish ERp46 as the first AdipoR1-specific interacting protein and suggest a role for ERp46 in adiponectin receptor biology and adiponectin signalling. PMID: 20074551
  • ERp46 has specificity towards peroxiredoxin-4, a thioredoxin peroxidase. PMID: 19887585
  • upregulation of TXNDC5 are involved in the early development of colorectal cancer PMID: 17895523
  • Member of the protein disulphide isomerase family and highly expressed in endothelial cells. Protects endothelial cells from apoptosis under hypoxia. PMID: 12963716

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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

    Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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