|Calculated MW||43262 Da|
|Application & Usage||Western blotting (0.5-4 µg/ml). However, the optimal conditions should be determined individually. 293 cell lysate can be used as a positive control. Detects the 43 kDa human caspase-4|
|Other Names||CASP-4, ICH-2 protease, TX protease, ICH2|
|Formulation||100 µg (0.5 mg/ml) immunoaffinity purified mouse IgG in PBS containing 0.5% BSA, 1.5 mM sodium azide and 30% glycerol.|
|Handling||The antibody solution should be gently mixed before use.|
|Reconstitution & Storage||-20 °C|
|Precautions||Caspase-4 Antibody (Clone D44) 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.
The caspase family of cysteine proteases play a key role in apoptosis. Like other caspases in the family, caspase-4 is also synthesized as inactive pro-enzyme that is processed in cells by self-proteolysis and/or cleavage by another upstream protease. The processed form of caspase-4 consists of large and small subunits which associate to form an active enzyme. Caspase-4 has been implicated involving in Fas-mediated apoptosis.
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