|Application ||WB, IHC-P, IF, E|
|Other Accession||AAA86890, 886050|
|Calculated MW||43262 Da|
|Application Notes||Casp-4 antibody can be used for the detection of Caspase-4 by Western blot at 1 and 2 µg/mL. Antibody can also be used for immunohistochemistry starting at 2 µg/mL. For immunofluorescence start at 10 µg/mL.|
|Other Names||Caspase-4 Antibody: TX, ICH-2, Mih1/TX, ICEREL-II, ICE(rel)II, ICH2, Caspase-4, Protease ICH-2, CASP-4, caspase 4, apoptosis-related cysteine peptidase|
|Target/Specificity||CASP4; Depending on cell lines or tissues used, other cleavage products may be observed.|
|Reconstitution & Storage||Caspase-4 antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.|
|Precautions||Caspase-4 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Inflammatory caspase (PubMed:7797510, PubMed:23516580, PubMed:25119034). Essential effector of NLRP3 inflammasome- dependent CASP1 activation and IL1B and IL18 secretion in response to non-canonical activators, such as UVB radiation, cholera enterotoxin subunit B and cytosolic LPS (PubMed:22246630, PubMed:26174085, PubMed:26173988, PubMed:26508369, PubMed:25964352). Independently of NLRP3 inflammasome and CASP1, promotes pyroptosis, through GSDMD cleavage and activation, and IL1A, IL18 and HMGB1 release in response to non-canonical inflammasome activators (PubMed:24879791, PubMed:25964352). Plays a crucial role in the restriction of Salmonella typhimurium replication in colonic epithelial cells during infection (PubMed:25121752). In later stages of the infection, LPS from cytosolic Salmonella triggers CASP4 activation, which ultimately results in pyroptosis of infected cells and their extrusion into the gut lumen, as well as in IL18 secretion. Pyroptosis limits bacterial replication, while cytokine secretion promotes the recruitment and activation of immune cells and triggers mucosal inflammation. Involved in LPS-induced IL6 secretion; this activity may not require caspase enzymatic activity (PubMed:26508369). Involved in cell death induced by endoplasmic reticulum stress and by treatment with cytotoxic APP peptides found Alzheimer's patient brains (PubMed:15123740, PubMed:22246630, PubMed:23661706). Activated by direct binding to LPS without the need of an upstream sensor (PubMed:25119034). Does not directly process IL1B (PubMed:7743998, PubMed:7797592, PubMed:7797510).|
|Cellular Location||Cytoplasm, cytosol. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Mitochondrion Inflammasome. Secreted. Note=Predominantly localizes to the endoplasmic reticulum (ER). Association with the ER membrane requires TMEM214 (PubMed:15123740). Released in the extracellular milieu by keratinocytes following UVB irradiation (PubMed:22246630).|
|Tissue Location||Widely expressed, including in keratinocytes and colonic and small intestinal epithelial cells (at protein level). Not detected in brain.|
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Provided below are standard protocols that you may find useful for product applications.
Caspase-4 Antibody: Caspases are a family of cysteine proteases that can be divided into the apoptotic and inflammatory caspase subfamilies. Unlike the apoptotic caspases, members of the inflammatory subfamily are generally not involved in cell death but are associated with the immune response to microbial pathogens. Members of this subfamily include caspase-1, -4, -5, and -12. Activation of these caspases results in the cleavage and activation of proinflammatory cytokines such as IL-1β and IL-18. Caspase-4 was initially identified as a homologous protein to Caspase-1 and the C. elegans Ced-3 which could induce apoptosis in transfected cells. More recent studies have shown that it can be activated by ER stress and has been suggested to be involved in multiple neuronal pathologies such as Alzheimer's disease.
Martinon F and Tschopp J. Inflammatory caspases: linking an intracellular innate immune system to autoinflammatory diseases. Cell 2004; 117:561-74.
Kuida K, Lippke JA, Ku G, et al. Altered cytokine export and apoptosis in mice deficient in interleukin-1 β converting enzyme. Science 1995; 267:2000-3.
Gracie JA, Robertson SE, and McInnes IB. Interleukin-18. J. Leukoc. Biol. 2003; 73:213-224.
Kamens J, Paskind M, Hugunin M, et al. Identification and characterization of ICH-2, a novel member of the interleukin-1 β-converting enzyme family of cysteine proteases. J. Biol. Chem. 1995; 270:15250-6.
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