CASP8 Monoclonal Antibody (E-AB-22107)
For research use only.
| Verified Samples |
Verified Samples in WB: Hela, Mouse brain, Rat brain Verified Samples in IHC: Mouse spleen Verified Samples in IF: Mouse liver |
| Dilution | WB 1:500-1:2000, IHC 1:100-1:300, IF 1:100-1:300 |
| Isotype | IgG |
| Host | Mouse |
| Reactivity | Human, Mouse, Rat |
| Applications | WB, IHC-p, IF |
| Clonality | Monoclonal |
| Immunogen | Recombinant Protein |
| Abbre | Caspase-8 |
| Synonyms | ALPS2B, Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 12 protein, Apoptotic cysteine protease, Apoptotic protease Mch-5, Apoptotic protease Mch5, CAP4, CASP-8, CASP8, Caspase 8, Caspase 8 apoptosis related cysteine peptidase, Caspase-8 sub |
| Swissprot | |
| Observed MW |
43 ,57kDa
The actual band is not consistent with the expectation.
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 | Cytoplasm. |
| Tissue Specificity | Isoform 1, isoform 5 and isoform 7 are expressed in a wide variety of tissues. Highest expression in peripheral blood leukocytes, spleen, thymus and liver. Barely detectable in brain, testis and skeletal muscle. |
| Concentration | 1 mg/mL |
| Buffer | Phosphate buffered solution, pH 7.4, containing 0.05% stabilizer, 0.5% protein protectant and 50% glycerol. |
| Purification Method | Protein A purification |
| Research Areas | Cancer, Cell Biology, Metabolism |
| Clone No. | 2E3 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | The product is shipped with ice pack,upon receipt,store it immediately at the temperature recommended. |
| background | Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-AMC. Likely target for the cowpox virus CRMA death inhibitory protein. Isoform 5, isoform 6, isoform 7 and isoform 8 lack the catalytic site and may interfere with the pro-apoptotic activity of the complex. |
Other Clones
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Other Formats
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Unconjugated
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