CARD12 Antibody Summary
A synthetic peptide corresponding to amino acids 971-989 (DFSTKEFLPDPALVRKLSQ) of human Ipaf/Clan/CARD12 was used as immunogen; GenBank no. gi|40788015|ref|NP_067032.3|.
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- Western Blot 1:1000-1:2000
- Immunohistochemistry-Paraffin 1:1000-1:5000
- Immunoprecipitation 1:50-1:200
Packaging, Storage & Formulations
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
0.05% Sodium Azide
Alternate Names for CARD12 Antibody
- CARD12leucine rich repeat and CARD domaincontaining 4
- caspase recruitment domain family, member 12
- Caspase recruitment domain-containing protein 12
- Clan protein
- CLANCARD, LRR, and NACHT-containing protein
- Ice protease-activating factor
- NLR family, CARD domain containing 4
Ipaf (also known as Clan/CARD12) is a CARD domain containing protein. CARD (caspase-associated recruitment domain) proteins are key regulators of cell death, cell survival and cytokine production (reviewed in Damiano and Reed, 2004). In general CARD proteins are implicated in host defense against infection, environmental stress or cellular damage. CARD domains are found in the N-terminal pro-domains of certain caspases, a family of apoptotic and pro-inflammatory proteases, as well as in a diversity of other proteins including Ipaf/Clan/CARD12. CARD domains are homotypic protein interaction motifs that enable networks of proteins to communicate via CARD-CARD interactions. There are at least three major signaling pathways in which CARD proteins act: (1) Regulation of caspase activation in the context of apoptosis (2) Regulation of caspase activation in the context of inflammation (3) Regaultion of NF-kB activation in the context of innate or adaptive immune responses. As there is significant crosstalk between pathways that lead to caspase-mediated apoptosis or inflammation and pathways that result in NF-kB activation, it is logical that similar protein modules such as CARD domains are found repeatedly in proteins from all three pathways. Ipaf plays a role in regulating caspase-1 activity, which in turn mediates the maturation of inflammatory cytokines IL-1b and IL-18 (reviewed in Lu et al, 2005). In transfected cells, Ipaf has been shown to directly interact with procaspase-1 and induce proteolytic activation of procaspase-1 in transfected cells. On the flip side, macrophages from IPAF deficient mice failed to activate caspase-1 in response to Salmonella typhimurium infection underscoring the importance of IPAF in vivo. IPAF also interact with the pro-apoptotic adaptor protein ASC and co-expression of IPAF with ASC has been shown to induce NF-kB activation and apoptosis.
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed
for 1 year from date of receipt.
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FAQs for CARD12 Antibody (NB100-56143). (Showing 1 - 1 of 1 FAQ).
I have purchased one of your antibodies (NB100-56143, polyclonal antibody to NLRC4) and require additional information, I have performed a western blot and detected multiple bands, I am unsure if these bands are breakdown products or detection of splice variants of the protein. In short, does your antibody detect NLRC4 splice variants?
- This antibody was made against the following peptide immunogen sequence: DFSTKEFLPDPALVRKLSQ. The antibody would be expected to recognize any NLRC4 forms that contain the sequence used for immunogen. I did a quick blast search (ncbi.nih.gov) and 345, 359, 404 and 989 amino acid forms containing this the immunogen sequence were identified. Of course, all proteins can have post-translational modifications and cleavage forms which can contribute to variable banding patterns. The IMG-5730 antibody has been evaluated with over expressed NLRC4 as shown on the data data sheet, but not with endogenous lysate, so I am not sure what the of endogenous NLRC4 is expressed or what size endogenous NLRC4 bands would typically be recognized with this antibody in a given lysate.
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