Recombinant Caspase-8 Monoclonal Antibody (AN301327L)
For research use only.
| Verified Samples | Verified Samples in WB: Jurkat |
| Dilution | WB 1:2000-1:10000 |
| Isotype | IgG,κ |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Applications | WB |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant Human Caspase-8 protein |
| Abbre | Caspase-8 |
| Synonyms | MCH, CAP, ALPS2B, CAP4, Casp-8, FLICE, MACH, MCH5, Caspase 8, CASP8, Caspase-8, Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 12 protein, Apoptotic cysteine protease, Apoptotic protease Mch5, Apoptotic protease Mch-5, Caspase 8 apoptosis related cysteine peptidase, Caspase-8 subunit p10, CED 3, FADD Like ICE, FADD-homologous ICE/ced-3-like protease, FADD-like ICE, FLJ17672, ICE-like apoptotic protease 5, MACH alpha 1/2/3 protein, MACH beta 1/2/3/4 protein, MGC78473, MORT1 associated ced 3 homolog, MORT1-associated ced-3 homolog, OTTHUMP00000163717, OTTHUMP00000163720, OTTHUMP00000163724, OTTHUMP00000163725, OTTHUMP00000165062, OTTHUMP00000165063, OTTHUMP00000165064, OTTHUMP00000206552, OTTHUMP00000206582 |
| Swissprot | |
| Calculated MW | 55 kDa |
| Observed MW |
55 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 | Cytoplasm, Nucleus. |
| Concentration | 0.2 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A |
| Research Areas | Cell Biology, Cancer, Metabolism |
| Clone No. | 9C7 |
| 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 cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes composed of a prodomain, a large protease subunit, and a small protease subunit. Activation of caspases requires proteolytic processing at conserved internal aspartic residues to generate a heterodimeric enzyme consisting of the large and small subunits. This protein is involved in the programmed cell death induced by Fas and various apoptotic stimuli. The N-terminal FADD-like death effector domain of this protein suggests that it may interact with Fas-interacting protein FADD. This protein was detected in the insoluble fraction of the affected brain region from Huntington disease patients but not in those from normal controls, which implicated the role in neurodegenerative diseases. |
Other Clones
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Unconjugated
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