TXNDC12 Antibody (C-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
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Application
| WB, IHC-P, E |
|---|---|
| Primary Accession | O95881 |
| Reactivity | Human, Rat, Mouse |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 19206 Da |
| Antigen Region | 144-172 aa |
| Gene ID | 51060 |
|---|---|
| Other Names | Thioredoxin domain-containing protein 12, Endoplasmic reticulum resident protein 18, ER protein 18, ERp18, Endoplasmic reticulum resident protein 19, ER protein 19, ERp19, Thioredoxin-like protein p19, hTLP19, TXNDC12, TLP19 |
| Target/Specificity | This TXNDC12 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 144-172 amino acids from the C-terminal region of human TXNDC12. |
| Dilution | WB~~1:1000 IHC-P~~1:100~500 E~~Use at an assay dependent concentration. |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | TXNDC12 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | TXNDC12 (HGNC:24626) |
|---|---|
| Function | Protein-disulfide reductase of the endoplasmic reticulum that promotes disulfide bond formation in client proteins through its thiol- disulfide oxidase activity. |
| Cellular Location | Endoplasmic reticulum lumen {ECO:0000255|PROSITE- ProRule:PRU10138, ECO:0000269|PubMed:12761212} |
| Tissue Location | Widely expressed.. |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
TXNDC12 belongs to the thioredoxin superfamily (see TXN; MIM 187700). Members of this superfamily possess a thioredoxin fold with a consensus active-site sequence (CxxC) and have roles in redox regulation, defense against oxidative stress, refolding of disulfide-containing proteins, and regulation of transcription factors
REFERENCES
Jessop, C.E., et al. J. Cell. Sci. 122 (PT 23), 4287-4295 (2009)
Rowe, M.L., et al. Biochemistry 48(21):4596-4606(2009)
Jeong, W., et al. J. Biol. Chem. 283(37):25557-25566(2008)
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