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The antibody against CASP1 was raised in rabbit using the Recombinant Human Caspase-1 protein (120-269AA) as the immunogen. This antibody exists as a non-conjugated isotype IgG, purified by protein G with a purity greater than 95%. This antibody has been validated on ELISA, IHC.
The antibody against CASP1 was raised in rabbit using the Recombinant Human Caspase-1 protein (120-269AA) as the immunogen. This antibody exists as a non-conjugated isotype IgG, purified by protein G with a purity greater than 95%. This antibody has been validated on ELISA, IHC.
$299.00
| Cat.No | ADC-54344A | Clonality | Polyclonal |
|---|---|---|---|
| Host Species | Rabbit | Target Name | CASP1 |
| Form | Liquid | Species Reactivity | Human |
| Isotype | IgG | Storage Buffer | 0.01M PBS, 0.03% Proclin 300; Constituents: 50% Glycerol, PH 7.4 |
| Purification Method | >95%, Protein G purified | Conjugate | Non-conjugated |
| Application | ELISA, IHC | Storage | Upon receipt |
| Immunogen Description | Recombinant Human Caspase-1 protein (120-269AA) | Target Species | Human |
|---|---|---|---|
| Immunogen Sequence | Complete sequences for the immunogen, target protein, and peptides are available upon request. | Uniprot ID | P29466 |
Uniprot Id
P29466
Target Species
Human
Target Name
CASP1
Target Full Name
Caspase-1
Target Function
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.; Apoptosis inactive.; Apoptosis inactive.
Target Subcellular Location
Cytoplasm. Cell membrane.
Target Protein Families
Peptidase C14A family
Target Tissue Specificity
Expressed in larger amounts in spleen and lung. Detected in liver, heart, small intestine, colon, thymus, prostate, skeletal muscle, peripheral blood leukocytes, kidney and testis. No expression in the brain.
Target Research Area
Apoptosis
Target Synonyms
CASP-1; CASP1; CASP1_HUMAN; Caspase 1; Caspase-1 subunit p10; ICE; IL-1 beta-converting enzyme; IL-1BC; IL1 beta converting enzyme; IL1B convertase; Interleukin 1 beta convertase; Interleukin 1B converting enzyme; Interleukin-1 beta convertase; Interleukin-1 beta-converting enzyme; p45
Target Background
This gene encodes a protein which is 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 which undergo proteolytic processing at conserved aspartic residues to produce 2 subunits, large and small, that dimerize to form the active enzyme. This gene was identified by its ability to proteolytically cleave and activate the inactive precursor of interleukin-1, a cytokine involved in the processes such as inflammation, septic shock, and wound healing. This gene has been shown to induce cell apoptosis and may function in various developmental stages. Studies of a similar gene in mouse suggest a role in the pathogenesis of Huntington disease. Alternative splicing results in transcript variants encoding distinct isoforms.
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