Technical Data
NALP2 (NACHT, LRR and PYD Domains-containing Protein 2, Nucleotide-binding site Protein 1, PYRIN Domain and NACHT Domain-containing Protein 1, PYRIN-containing APAF1-like Protein 2, NLRP2, NBS1, PAN1, PYPAF2)
NALP2 (also known as PAN1/PYPAF2) is a member of the NLR (NACHT-LRR) family which includes both NODs and NALPs (Bruey et al, 2004). Alternative names for the NLR family include CATERPILLER, NOD and NOD-LRR. NLR family members are thought to be intracellular pathogen-recognition receptors (PRRs) (reviewed in Martionon and Tschopp, 2005 and 2007; Creagh and O'Neill, 2006; Petrilli et al, 2005). PRRs are key components of immune systems and are involved in innate effector mechanisms and activation of adaptive immunity. Toll-like receptors (TLRs) are the most well studied PPRs and overlaps have been identified between the signaling pathways used by some NLRs and TLRs suggesting redundancy and cooperation between NLR and TLR pathways. At least fourteen NALPs have been identified in the human genome, and a common feature among NALPs 1-3, 6, and 12 is their ability to to recruit the adaptor protein ASC through a homotypic PYD-PYD interaction, which in turn recruits caspase-1 through a CARD-CARD interaction. The oligomerization of NALPs is thought to bring the inflammatory caspases into close proximity leading to their activation within the inflammasome. The inflammasome is a multiprotein complex of more than 700kD that is responsible for the activation of caspases 1 and 5, which leads to the processing and secretion of the pro-inflammatory cytokines IL-1b and IL-18. The NALP2/3 inflammasomes contain, in addition to NALP2 or NALP3, the caspase recruitment domain (CARD)-containing protein Cardinal, ASC and caspase 1. Processing of the pro-inflammatory cytokines IL-1b and IL-18 by caspases leads to to the secretion of active cytokines and elicits a potent inflammatory response. Similar to TLRs, activation of the inflammasome by NLRs occurs through the recognition of pathogen-associated molecular patterns (PAMPs) through their LRR (leucine rich) domains): TLR family members recognize bacteria, viruses, fungi and protoza, whereas NLRs with known functions recognize bacteria. The expression of NALP2 is upregulated in THP-1 macrophage cells by LPS and certain cytokines including interferon g and b, supporting a role for NALP2 in host-defense and inflammation (Bruey et al, 2004). Additionally, NALP2 is expressed in several human tumor cell lines. However, the endogenous expression of NALP2 varies widely among tumor cells lines, with the highest levels found in MCF-7 and MDA-MB-435 breast cancer, Caco2 colon cancer and UACC62 melanoma cells (Bruey et al, 2004). Recognizes NALP2; human NALP2 is a 1062aa protein. Is specific for NALP2 does not cross-react with related family members PAN2 or NAC.

Suitable for use in Western Blot, Immunohistochemistry and Immunoprecipitation. Other applications not tested.

Recommended Dilution:
Western Blot: 1:1000-1:2000
Immunohistochemistry (formalin fixed paraffin embedded): 1:1000-1:5000
Immunoprecipitation: 1:50-1:200
Immunohistochemistry: Frozen
Optimal dilutions to be determined by the researcher.

Positive Control:
Spleen, lymphoid, MCF-7 and THP-1 cell lines

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
50ul-20CBlue IceHumanRabbit
Not determined.
Synthetic peptide corresponding to aa97-115 (LKSFNKRKPLSLGITRKER) of human NALP2; GenBank no. gi|8923473|ref|NP_060322.1
Supplied as a liquid, 0.05% sodium azide.
Recognizes human NALP2.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Petrilli V, S Papin, and Jschopp. 2005. The inflammasome. Curr Biol 15:R581. 2. Martinon F and J Tschopp. 2005. NLRs join TLRs as innate sensors of pathogen. TRENDS in Immunology 26:447-454. 3. Martinon F and J Tschopp. 2007. Inflammatory caspase and inflammasomes: master switches of inflammation. Cell Death and Differentiation 14:10-22. 4. Cregh E and LAJ O'Neill. 2006. TLRs, NLRs and RLRs: a trinity of pathogen sensors that co-operate in innate immunity. TRENDS in Immunology 27:352-357.