CARD12 Antibody [Allophycocyanin]

Novus Biologicals, part of Bio-Techne | Catalog # NBP2-98090APC

Novus Biologicals, part of Bio-Techne

Key Product Details

Species Reactivity

Validated:

Human

Applications

Immunohistochemistry-Paraffin

Label

Allophycocyanin (Excitation = 620-650 nm, Emission = 660-670 nm)

Antibody Source

Polyclonal Rabbit IgG

Concentration

Please see the vial label for concentration. If unlisted please contact technical services.

View all CARD12 Antibodies »

Product Summary for CARD12 Antibody [Allophycocyanin]

Immunogen

Produced in rabbits immunized with E. coli-derived Human CARD12 fragment.

Clonality

Polyclonal

Host

Rabbit

Isotype

IgG

Applications for CARD12 Antibody [Allophycocyanin]

Application
Recommended Usage

Immunohistochemistry-Paraffin

Optimal dilutions of this antibody should be experimentally determined.
Application Notes
Optimal dilution of this antibody should be experimentally determined.
Please Note: Optimal dilutions of this antibody should be experimentally determined.

Formulation, Preparation, and Storage

Purification

Antigen and protein A Affinity-purified

Formulation

PBS

Preservative

0.05% Sodium Azide

Concentration

Please see the vial label for concentration. If unlisted please contact technical services.

Shipping

The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.

Stability & Storage

Store at 4C in the dark.

Background: CARD12

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.

Alternate Names

CARD12leucine rich repeat and CARD domaincontaining 4, caspase recruitment domain family, member 12, Caspase recruitment domain-containing protein 12, Clan protein, CLAN1ipaf, CLANCARD, LRR, and NACHT-containing protein, CLR2.1, Ice protease-activating factor, Ipaf, NLR family, CARD domain containing 4

Gene Symbol

NLRC4

Additional CARD12 Products

Product Documents for CARD12 Antibody [Allophycocyanin]

Product Datasheets

Certificate of Analysis

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Product Specific Notices for CARD12 Antibody [Allophycocyanin]

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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