# | Product Name | Applications | Reactivity | |
---|---|---|---|---|
38916 | ARC (D7Q3G) Rabbit mAb |
|
H |
REACTIVITY | H |
SENSITIVITY | Endogenous |
MW (kDa) | 27 |
SOURCE | Rabbit |
Product Information
Application | Dilution |
---|---|
Western Blotting | 1:1000 |
For western blots, incubate membrane with diluted primary antibody in 5% w/v BSA, 1X TBS, 0.1% Tween® 20 at 4°C with gentle shaking, overnight.
NOTE: Please refer to primary antibody product webpage for recommended antibody dilution.
From sample preparation to detection, the reagents you need for your Western Blot are now in one convenient kit: #12957 Western Blotting Application Solutions Kit
NOTE: Prepare solutions with reverse osmosis deionized (RODI) or equivalent grade water.
Load 20 µl onto SDS-PAGE gel (10 cm x 10 cm).
NOTE: Loading of prestained molecular weight markers (#59329, 10 µl/lane) to verify electrotransfer and biotinylated protein ladder (#7727, 10 µl/lane) to determine molecular weights are recommended.
NOTE: Volumes are for 10 cm x 10 cm (100 cm2) of membrane; for different sized membranes, adjust volumes accordingly.
* Avoid repeated exposure to skin.
posted June 2005
revised June 2020
Protocol Id: 10
Human
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro125 of human ARC protein, specific to a region encoded by isoform 2 of the NOL3 gene. Antibodies are purified by protein A and peptide affinity chromatography.
Apoptosis repressor with caspase recruitment domain (ARC), also independently identified as muscle-enriched cytoplasmic protein (MYP), is a CARD domain protein that regulates apoptosis (1). The ARC protein CARD domain is highly homologous to those in other cell death regulators, including caspase-2, caspase-9, RAIDD, and Apaf-1 (2). The NOL3 gene encodes both the cytoplasmic ARC protein and a 30 kDa nucleolar protein (Nop30) that is involved in RNA splicing. ARC is encoded from isoform 2 of NOL3, while isoform 1 produced by alternative splicing encodes Nop30. Both ARC and Nop30 proteins share common amino-terminal sequences (3). Research studies show that ARC can bind to caspase-8 and caspase-2 and inhibit apoptosis through extrinsic pathways that involve the receptor proteins Fas, TNFR1, and DR3 (1). Additional research indicates that the ARC anti-apoptotic mechanism may include both intrinsic (mitochondrial) and extrinsic (death receptor) pathways (4). In addition to binding caspases, ARC can disrupt the interaction with the death domains of Fas and FADD, which inhibits death-inducing signaling complex (DISC) assembly. The CARD domain of ARC can inhibit intrinsic apoptosis through binding to the pro-apoptotic Bax protein (5). Phosphorylation of ARC at Thr149 by CK2 is required for targeting of ARC to the mitochondria (6). ARC is able to suppress necroptosis, a programmed pathway of necrosis triggered by blocking the recruitment of RIP1 to TNFR1 (7). Expression of ARC protein is predominantly seen in terminally differentiated cells under normal conditions and is markedly induced in a variety of cancers including pancreatic, colorectal, breast, lung, glioblastoma, liver, kidney, melanoma, and acute myeloid leukemia (1, 8-12).
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