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Mouse Anti-CASP1 Recombinant Antibody (CBYY-C0960) (CBMAB-C2397-YY)

This product is mouse antibody that recognizes CASP1. The antibody CBYY-C0960 can be used for immunoassay techniques such as: WB, ICC
See all CASP1 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBYY-C0960
Antibody Isotype
IgG2a
Application
WB, ICC

Basic Information

Immunogen
E.coli-derived recombinant human Caspase-1, Asn120-Asp297, Accession # P29466
Specificity
Human
Antibody Isotype
IgG2a
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Protein A/G purified
Buffer
LYOPH
Preservative
PBS
Concentration
Lyophilized
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Caspase 1
Entrez Gene ID
UniProt ID
Alternative Names
Caspase 9; Caspase 9, Apoptosis-Related Cysteine Peptidase; Protein Phosphatase 1, Regulatory Subunit 56; ICE-Like Apoptotic Protease 6; ICE-LAP6; APAF-3; MCH6; Caspase 9, Apoptosis-Related Cysteine Protease; Apoptotic Protease Activating Factor 3;
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 (PubMed:15326478, PubMed:1574116, PubMed:7876192, PubMed:15498465, PubMed:26375003, PubMed:32051255).
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 (PubMed:1574116, PubMed:7876192, PubMed:15498465, PubMed:15326478, PubMed:32051255).
Cleaves a tetrapeptide after an Asp residue at position P1 (PubMed:1574116, PubMed:7876192, PubMed:15498465).
Also initiates pyroptosis, a programmed lytic cell death pathway, through cleavage of GSDMD (PubMed:26375003).
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 (PubMed:32051255, PubMed:32109412, PubMed:32553275).
Upon inflammasome activation, during DNA virus infection but not RNA virus challenge, controls antiviral immunity through the cleavage of CGAS, rendering it inactive (PubMed:28314590).
In apoptotic cells, cleaves SPHK2 which is released from cells and remains enzymatically active extracellularly (PubMed:20197547).
Isoform Delta: Apoptosis inactive.
Isoform Epsilon: Apoptosis inactive.
Biological Process
Apoptotic process Source: ProtInc
Cellular response to cytokine stimulus Source: Reactome
Cellular response to interferon-gamma Source: UniProtKB
Cellular response to lipopolysaccharide Source: UniProtKB
Cellular response to mechanical stimulus Source: UniProtKB
Cellular response to organic substance Source: MGI
Cytokine-mediated signaling pathway Source: Reactome
Cytokine precursor processing Source: ARUK-UCL
Execution phase of apoptosis Source: GOC
Membrane hyperpolarization Source: Ensembl
Mitochondrial depolarization Source: Ensembl
Positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
Positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
Positive regulation of interleukin-1 alpha production Source: Ensembl
Positive regulation of interleukin-1 beta production Source: UniProtKB
Positive regulation of tumor necrosis factor-mediated signaling pathway Source: UniProtKB
Programmed necrotic cell death Source: Ensembl
Protein autoprocessing Source: UniProtKB
Proteolysis Source: UniProtKB
Purinergic nucleotide receptor signaling pathway Source: Reactome
Pyroptosis Source: UniProtKB
Regulation of apoptotic process Source: Reactome
Regulation of autophagy Source: Ensembl
Regulation of inflammatory response Source: UniProtKB
Response to ATP Source: Ensembl
Response to hypoxia Source: Ensembl
Signaling receptor ligand precursor processing Source: ARUK-UCL
Signal transduction Source: ProtInc
Toxin transport Source: Ensembl
Cellular Location
Cell membrane; Cytoplasm
PTM
The two subunits are derived from the precursor sequence by an autocatalytic mechanism.
Ubiquitinated via 'Lys-11'-linked polyubiquitination. Deubiquitinated by USP8.
Cleavage in the interdomain linker region is required to induce pyroptosis.

Zeng, X., Luo, X., Mao, X., Wen, D., Zhang, H., & Wang, J. (2021). Inflammatory and immune-related factor Caspase 1 contributes to the development of oral lichen planus. Archives of Oral Biology, 131, 105244.

Flores, J., Noël, A., Fillion, M. L., & LeBlanc, A. C. (2021). Therapeutic potential of Nlrp1 inflammasome, Caspase-1, or Caspase-6 against Alzheimer disease cognitive impairment. Cell Death & Differentiation, 1-13.

Crowley, S. M., Han, X., Allaire, J. M., Stahl, M., Rauch, I., Knodler, L. A., & Vallance, B. A. (2020). Intestinal restriction of Salmonella Typhimurium requires caspase-1 and caspase-11 epithelial intrinsic inflammasomes. PLoS pathogens, 16(4), e1008498.

Reinke, S., Linge, M., Diebner, H. H., Luksch, H., Glage, S., Gocht, A., ... & Winkler, S. (2020). Non-canonical caspase-1 signaling drives RIP2-dependent and TNF-α-mediated inflammation in vivo. Cell reports, 30(8), 2501-2511.

Wooff, Y., Fernando, N., Wong, J. H., Dietrich, C., Aggio-Bruce, R., Chu-Tan, J. A., ... & Natoli, R. (2020). Caspase-1-dependent inflammasomes mediate photoreceptor cell death in photo-oxidative damage-induced retinal degeneration. Scientific reports, 10(1), 1-20.

Kapplusch, F., Schulze, F., Rabe-Matschewsky, S., Russ, S., Herbig, M., Heymann, M. C., ... & Hofmann, S. R. (2019). CASP1 variants influence subcellular caspase-1 localization, pyroptosome formation, pro-inflammatory cell death and macrophage deformability. Clinical Immunology, 208, 108232.

Gonçalves, A. V., Margolis, S. R., Quirino, G. F., Mascarenhas, D. P., Rauch, I., Nichols, R. D., ... & Zamboni, D. S. (2019). Gasdermin-D and Caspase-7 are the key Caspase-1/8 substrates downstream of the NAIP5/NLRC4 inflammasome required for restriction of Legionella pneumophila. PLoS pathogens, 15(6), e1007886.

Chang, I., Mitsui, Y., Kim, S. K., Sun, J. S., Jeon, H. S., Kang, J. Y., ... & Tanaka, Y. (2017). Cytochrome P450 1B1 inhibition suppresses tumorigenicity of prostate cancer via caspase-1 activation. Oncotarget, 8(24), 39087.

Man, S. M., Karki, R., Briard, B., Burton, A., Gingras, S., Pelletier, S., & Kanneganti, T. D. (2017). Differential roles of caspase-1 and caspase-11 in infection and inflammation. Scientific reports, 7(1), 1-11.

Mascarenhas, D. P., Cerqueira, D. M., Pereira, M. S., Castanheira, F. V., Fernandes, T. D., Manin, G. Z., ... & Zamboni, D. S. (2017). Inhibition of caspase-1 or gasdermin-D enable caspase-8 activation in the Naip5/NLRC4/ASC inflammasome. PLoS pathogens, 13(8), e1006502.

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For research use only. Not intended for any clinical use.

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