Recombinant Phospho-FADD (S194) Monoclonal Antibody (AN302084L)
For research use only.
| Verified Samples | Verified Samples in WB: HeLa |
| Dilution | WB 1:500-1:2000 |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, |
| Applications | WB |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant human FADD (phospho S194) fragment |
| Abbre | Phospho-FADD (S194) |
| Synonyms | GIG, MORT, FADD, GIG3, MORT1, Fas associated via death domain, FADD protein, Fas (TNFRSF6) associated via death domain, Fas associating death domain containing protein, Fas associating protein, Fas associating protein with death domain, Fas TNFRSF6 associated via death domain, FAS-associated death domain protein, FAS-associating death domain-containing protein, GIG 3, Growth inhibiting gene 3 protein, Growth-inhibiting gene 3 protein, H sapiens mRNA for mediator of receptor induced toxicity, Mediator of receptor induced toxicity, MGC8528, MORT 1, Protein FADD |
| Swissprot | |
| Calculated MW | 23 kDa |
| Observed MW |
23 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 | Cytosol, Membrane |
| Concentration | 1 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A purified |
| Research Areas | Cell Biology, Cancer |
| Clone No. | A808 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | The protein is an adaptor molecule that interacts with various cell surface receptors and mediates cell apoptotic signals. Through its C-terminal death domain, this protein can be recruited by TNFRSF6/Fas-receptor, tumor necrosis factor receptor, TNFRSF25, and TNFSF10/TRAIL-receptor, and thus it participates in the death signaling initiated by these receptors. Interaction of this protein with the receptors unmasks the N-terminal effector domain of this protein, which allows it to recruit caspase-8, and thereby activate the cysteine protease cascade. |
Other Clones
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