ARC Antibody

ARC Antibody

Catalog# : 2185

Apoptosis is regulated by death domain (DD) and/or caspase recruitment domain (CARD) containing molecules and a caspase family of proteases. CARD containing cell death regulators include RAIDD, RICK BCL10, Apaf-1, caspase-9, and caspase-2. A novel CARD domain containing protein was recently identified and designated ARC for apoptosis repressor with CARD (1). ARC interacts with caspase-2 and –8 and inhibits enzymatic activity of caspase-8. ARC suppresses apoptosis induced by cell death adapters FADD and TRADD and by cell death receptors Fas, TNFR-1, and DR3. The messenger RNA of ARC is primarily expressed in skeletal muscle and cardiac tissue (1).

Additional Names : ARC (NT), ARC

Description
Left: Western blot analysis of ARC in HeLa whole cell lysates with ARC antibody at 1:500 dilution.



Source : ARC antibody was raised against a peptide corresponding to amino acids 2 to 18 of human origin. These sequences are identical to those of human nuclear protein Nop30 (2) and differ from those of the rat homolog of ARC by one amino acid (3).

Purification : Affinity chromatography purified via peptide column

Clonality and Clone : This is a polyclonal antibody.

Host : ARC antibody was raised in rabbit.

Immunogen : Human ARC (N-Terminus) Peptide (Cat. No. 2185P)

Tested Application(s) : E, WB

Buffer : Antibody is supplied in PBS containing 0.02% sodium azide.

Blocking Peptide : Cat. No. 2185P - ARC Peptide

Long-Term Storage : ARC antibody can be stored at 4ºC, stable for one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.

Positive Control

• Cat. No. 1201 - HeLa Cell Lysate

Species Reactivity :H, M, R

GI Number : 4505419

Accession Number : NP_003937

Short Description : (NT) Apoptosis Repressor with CARD domain

References

1. Koseki T, Inohara N, Chen S, Nunez G. ARC, an inhibitor of apoptosis expressed in skeletal muscle and heart that interacts selectively with caspases. Proc Natl Acad Sci USA 1998;95:5156-60
2. Stoss O, Schwaiger FW, Cooper TA, Stamm S. Alternative splicing determines the intracellular localization of the novel nuclear protein Nop30 and its interaction with the splicing factor SRp30c. J Biol Chem 1999;274(16):10951-62
3. Geertman R, McMahon A, Sabban EL. Cloning and characterization of cDNAs for novel proteins with glutamic acid-proline dipeptide tandem repeats. Biochim Biophys Acta 1996;1306(2-3):147-52 (WD 0300)

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