Recombinant TXD12 Monoclonal Antibody (AN301120L)
For research use only.
| Verified Samples |
Verified Samples in WB: HepG2 Verified Samples in IHC: Human kidney |
| Dilution | IHC 1:500-1:2000, WB 1:2000-1:10000 |
| Isotype | IgG,κ |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Applications | WB, IHC |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant Human TXD12 protein |
| Abbre | TXD12 |
| Synonyms | hAG, AGR, TLP, UNQ, PRO, PDIA, hTLP, Thioredoxin-Like Protein p, Thioredoxin Domain-Containing Protein, TXNDC, ERP, TXNDC12, AG1, AGR1, ERP16, ERP18, ERP19, PDIA16, TLP19, hAG-1, hTLP19, Endoplasmic Reticulum Resident Protein 18, Endoplasmic Reticulum Resident Protein 19, ER Protein 18, ER Protein 19, Thioredoxin Domain-Containing Protein 12, Thioredoxin-Like Protein p19, UNQ713, PRO1376, 18 kDa, member 16, anterior gradient homolog 1, endoplasmic reticulum protein ERp19, endoplasmic reticulum thioredoxin superfamily member, ERP 18, hAG 1, hAG1, protein disulfide isomerase family A, thioredoxin domain containing 12 (endoplasmic reticulum, thioredoxin like protein p19, TXD12 |
| Swissprot | |
| Calculated MW | 19 kDa |
| Observed MW |
19 kDa
Western blotting is a method for detecting a certain protein in a complex sample based on the specific binding of antigen and antibody. Different proteins can be divided into bands based on different mobility rates. The mobility is affected by many factors, which may cause the observed band size to be inconsistent with the expected size. The common factors include: 1. Post-translational modifications: For example, modifications such as glycosylation, phosphorylation, methylation, and acetylation will increase the molecular weight of the protein. 2. Splicing variants: Different expression patterns of various mRNA splicing bodies may produce proteins of different sizes. 3. Post-translational cleavage: Many proteins are first synthesized into precursor proteins and then cleaved to form active forms, such as COL1A1. 4. Relative charge: the composition of amino acids (the proportion of charged amino acids and uncharged amino acids). 5. Formation of multimers: For example, in protein dimer, strong interactions between proteins can cause the bands to be larger. However, the use of reducing conditions can usually avoid the formation of multimers. If a protein in a sample has different modified forms at the same time, multiple bands may be detected on the membrane. |
| Cellular Localization | Endoplasmic reticulum lumen. |
| Concentration | 0.2 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A |
| Research Areas | Signal Transduction |
| Clone No. | 12G3 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | This gene encodes a member of the thioredoxin superfamily. Members of this family are characterized by a conserved active motif called the thioredoxin fold that catalyzes disulfide bond formation and isomerization. This protein localizes to the endoplasmic reticulum and has a single atypical active motif. The encoded protein is mainly involved in catalyzing native disulfide bond formation and displays activity similar to protein-disulfide isomerases. This protein may play a role in defense against endoplasmic reticulum stress. Alternate splicing results in both coding and non-coding variants. |
Other Clones
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Unconjugated
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