|Other Accession||NM_001033053, NP_001028225|
|Reactivity||Human, Mouse, Rat, Rabbit, Pig, Horse, Bovine, Guinea Pig, Dog|
|Predicted||Human, Mouse, Rat, Horse, Bovine, Dog|
|Alias Symbol||CARD7, CLR17.1, DEFCAP, DEFCAP-L/S, DKFZp586O1822, KIAA0926, NAC, NALP1, PP1044, SLEV1, VAMAS1|
|Other Names||NACHT, LRR and PYD domains-containing protein 1, Caspase recruitment domain-containing protein 7, Death effector filament-forming ced-4-like apoptosis protein, Nucleotide-binding domain and caspase recruitment domain, NLRP1, CARD7, DEFCAP, KIAA0926, NAC, NALP1|
|Format||Liquid. Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.|
|Reconstitution & Storage||Add 50 ul of distilled water. Final anti-NLRP1 antibody concentration is 1 mg/ml in PBS buffer with 2% sucrose. For longer periods of storage, store at 20°C. Avoid repeat freeze-thaw cycles.|
|Precautions||NLRP1 antibody - N-terminal region is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||As the sensor component of the NLRP1 inflammasome, plays a crucial role in innate immunity and inflammation. In response to pathogens and other damage-associated signals, initiates the formation of the inflammasome polymeric complex, made of NLRP1, CASP1, and possibly PYCARD. Recruitment of proCASP1 to the inflammasome promotes its activation and CASP1-catalyzed IL1B and IL18 maturation and secretion in the extracellular milieu. Activation of NLRP1 inflammasome is also required for HMGB1 secretion. The active cytokines and HMGB1 stimulate inflammatory responses. Inflammasomes can also induce pyroptosis, an inflammatory form of programmed cell death (PubMed:22665479, PubMed:17418785). May be activated by muramyl dipeptide (MDP), a fragment of bacterial peptidoglycan, in a NOD2-dependent manner (PubMed:18511561). Contrary to its mouse ortholog, not activated by Bacillus anthracis lethal toxin (PubMed:19651869). It is unclear whether isoform 2 is involved in inflammasome formation. It is not cleaved within the FIIND domain, does not assemble into specks, nor promote IL1B release (PubMed:22665479). However, in an vitro cell-free system, it has been shown to be activated by MDP (PubMed:17349957). Binds ATP (PubMed:11113115, PubMed:15212762).|
|Cellular Location||Cytoplasm, cytosol. Cytoplasm. Inflammasome Nucleus. Note=Nucleocytoplasmic distribution in lymphoid organs (probably in T-cells) and in neurons. In epithelial cells, predominantly cytoplasmic|
|Tissue Location||Widely expressed (PubMed:11113115, PubMed:17164409). Abundantly expressed in primary immune cells (isoform 1 and isoform 2), including in neutrophils, monocytes/macrophages, dendritic cells (mostly Langerhans cells), and B- and T-lymphocytes (at protein level) (PubMed:15285719, PubMed:17164409). Strongly expressed in epithelial cells lining the glandular epithelium, such as that of the gastrointestinal tract (stomach, small intestine, colon), the respiratory tract (trachea and bronchi), and the endometrial and endocervical glands, gallbladder, prostate, and breast (at protein level). In testis, expressed in spermatogonia and primary spermatocytes, but not in Sertoli cells (at protein level). In the brain, expressed in neurons, in particular in pyramidal ones and in oligodendrocytes, but not detected in microglia (at protein level) (PubMed:17164409). Expressed in adult and fetal ocular tissues, including in adult and 24-week old fetal choroid, sclera, cornea, and optic nerve, as well as in adult retina and fetal retina/retinal pigment epithelium (PubMed:23349227)|
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Provided below are standard protocols that you may find useful for product applications.
Bertin J.,et al.Cell Death Differ. 7:1273-1274(2000).
Martinon F.,et al.Curr. Biol. 11:R118-R120(2001).
Hlaing T.,et al.J. Biol. Chem. 276:9230-9238(2001).
Chu Z.-L.,et al.J. Biol. Chem. 276:9239-9245(2001).
Nagase T.,et al.DNA Res. 6:63-70(1999).
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