CASP1 Polyclonal Antibody (E-AB-93260)
For research use only.
| Verified Samples |
Verified Samples in WB: Mouse testis Verified Samples in IF: C6, NIH/3T3 |
| Dilution | WB 1:500-1:2000, IF 1:50-1:200 |
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Mouse, Rat |
| Applications | WB, IF |
| Clonality | Polyclonal |
| Immunogen | A synthetic peptide of mouse CASP1 |
| Abbre | CASP1 |
| Synonyms | Casp, ICE, Il1, Il1bc, IC |
| Swissprot | |
| Calculated MW | 45 kDa |
| Observed MW |
48 kDa
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 | AIM2 inflammasome complex, cytoplasm, cytosol, extracellular region, extracellular space, inflammasome complex, IPAF inflammasome complex, mitochondrion, neuron projection, NLRP1 inflammasome complex, NLRP3 inflammasome complex, nucleus, plasma membrane. |
| Concentration | 1 mg/mL |
| Buffer | Phosphate buffered solution, pH 7.4, containing 0.05% stabilizer and 50% glycerol. |
| Purification Method | Affinity purification |
| 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 | Thiol protease involved in a variety of inflammatory processes by proteolytically cleaving other proteins, such as the precursors of the inflammatory cytokines interleukin-1 beta (IL1B and interleukin 18 (IL18 as well as the pyroptosis inducer Gasdermin-D (GSDMD, into active mature peptides. Plays a key role in cell immunity as an inflammatory response initiator: once activated through formation of an inflammasome complex, it initiates a proinflammatory response through the cleavage of the two inflammatory cytokines IL1B and IL18, releasing the mature cytokines which are involved in a variety of inflammatory processes. Cleaves a tetrapeptide after an Asp residue at position P1. Also initiates pyroptosis, a programmed lytic cell death pathway, through cleavage of GSDMD. In contrast to cleavage of interleukins IL1B and IL1B, recognition and cleavage of GSDMD is not strictly dependent on the consensus cleavage site but depends on an exosite interface on CASP1 that recognizes and binds the Gasdermin-D, C-terminal (GSDMD-CT part. Upon inflammasome activation, during DNA virus infection but not RNA virus challenge, controls antiviral immunity through the cleavage of CGAS, rendering it inactive. In apoptotic cells, cleaves SPHK2 which is released from cells and remains enzymatically active extracellularly (By similarity. |
Other Clones
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Other Formats
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Unconjugated
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