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TXNDC12 Antibody (C-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| IHC-P, WB, E |
|---|---|
| Primary Accession | O95881 |
| Reactivity | Human, 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~~1:50~100 |
| 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.. |
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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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