Baculoviral IAP Repeat Containing 3 (BIRC3) antibody
Alternatives Western Blotting (WB), Immunoprecipitation (IP)
|7 references available|
|Quantity||50 µg (0.25 mg/ml) (Variants)|
|Price||Product not available in this region.|
1) 51-9000062: Purified Mouse Anti-Human c-IAP-2.
Quantity: 50 µg (1 ea).
Concentration: 0.25 mg/ml.
Immunogen: Human c-IAP-2.
Isotype: Mouse IgG1, kappa.
Storage Buffer: Aqueous buffered solution containing BSA, glycerol, and Less or equal than 0.09% sodium azide.
2) 51-16526N: Jurkat Cell Lysate.
Quantity: 50 µg (1 ea).
Concentration: 1.0 mg/ml.
Storage Buffer: SDS-PAGE buffer (62mM Tris pH 6.8, 2% SDS, 0.9% b-mercaptoethanol, 0.003% bromophenol blue, 5% glycerol).
|Description||Programmed cell death is a normal physiologic process required for maintenance as well as for development in multi-cellular organisms. It is important for apoptosis to be tightly controlled because dysregulation of cell death pathways can lead to pathogenesis. One group of proteins which aids in the regulation of the apoptotic process is called inhibitors of apoptosis (IAPs). This group of proteins acts by directly inhibiting a class of proteins known as the executioners of apoptosis, the caspases. Caspases are inactive cytosolic proteases that upon activation can cause the demise of the cell. IAPs directly inhibit apoptosis by physically interacting with and blocking caspase activity. The first human IAP to be identified, NAIP, was discovered based on its association with a neurodegenerative disorder. Subsequently, six additional human IAPs have been identified, including survivin, XIAP, c-IAP-1, c-IAP-2, BRUCE, and pIAP. These proteins share sequence motifs including a RING zinc finger domain as well two to three copies of an ~65 amino acid baculovirus IAP repeat (BIR) domain. BIR regions promote protein-protein interaction(s) with caspases and are required for inhibition of caspase activity and apoptosis. While the RING zinc finger regions are not required for this function, they have been found to enhance the caspase inhibitory action of IAPs. Each of these inhibitors displays some specificity with regard to their ability to bind and inhibit caspases. c-IAP-1, c-IAP-2 and XIAP have been shown to block the activity of caspases-3 and -7, while NAIP does not. Thus, IAPs provide a central role in regulation of apoptosis, while subtle differences between the IAPs may confer specificity in the regulation of the various caspases. c-IAP-1 has a molecular weight of ~72 kDa in SDS/PAGE. The antibody recognizes human c-IAP-2. Recombinant human c-IAP-2 expressed in E. coli was used as an immunogen.|
1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. This product is sold under license from Aegera Therapeutics, Inc.
4. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
5. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
Related Products: ABIN967389, ABIN968537
|Application Notes||Applications include western blot analysis (1.0-4.0 µg/ml). Jurkat control lysate [50 µg (1 µg/µl)] is provided as a western blot positive control (store lysate at -20°C). Additional control lysate (ABIN968537) is also sold seperately. Additional applications not routinely tested include immunoprecipitation (2 µg of antibody/200 µg of lysate).|
|Purification||Purified from tissue culture supernatant or ascites by affinity chromatography.|
|Buffer||Aqueous buffered solution containing BSA, glycerol.|
|Preservative||0.09% Sodium azide.|
|Storage||Store undiluted at -20°C.|
|Restrictions||For Research Use only|
|Western blot analysis of c-IAP-2. Jurkat cell lysate was probed with anti-c-IAP-2 (clone F30-2285, component 51-9000062) at concentrations of 4.0 (lane 1), 2.0 (lane 2), and 1.0 µg/ml (lane 3). c-IAP-2 is identified as a band of ~72 kDa.|
Roy, Mahadevan, McLean et al.: "The gene for neuronal apoptosis inhibitory protein is partially deleted in individuals with spinal muscular atrophy." in: Cell, Vol. 80, Issue 1, pp. 167-78, 1995 (PubMed).
Rothe, Pan, Henzel et al.: "The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins." in: Cell, Vol. 83, Issue 7, pp. 1243-52, 1996 (PubMed).
Roy, Deveraux, Takahashi et al.: "The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases." in: The EMBO journal, Vol. 16, Issue 23, pp. 6914-25, 1998 (PubMed).
Deveraux, Reed: "IAP family proteins--suppressors of apoptosis." in: Genes & development, Vol. 13, Issue 3, pp. 239-52, 1999 (PubMed).
Goyal: "Cell death inhibition: keeping caspases in check." in: Cell, Vol. 104, Issue 6, pp. 805-8, 2001 (PubMed).
Salvesen, Duckett: "IAP proteins: blocking the road to death's door." in: Nature reviews. Molecular cell biology, Vol. 3, Issue 6, pp. 401-10, 2002 (PubMed).
Krajewska, Krajewski, Banares et al.: "Elevated expression of inhibitor of apoptosis proteins in prostate cancer." in: Clinical cancer research : an official journal of the American Association for Cancer Research, Vol. 9, Issue 13, pp. 4914-25, 2003 (PubMed).