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c-IAP1 monoclonal antibody (1E1-1-10)

 
ALX-803-335-C100 100 µg 291.00 USD
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Product Specification

Alternative Name:HIAP2, BIRC-2, Baculoviral IAP repeat-containing protein-2, Cellular inhibitor of apoptosis-1, Human inhibitor of apoptosis protein-2, Inhibitor of apoptosis protein-2
 
Clone:1E1-1-10
 
Host:Rat
 
Isotype:IgG2a
 
Immunogen:Synthetic peptide corresponding to aa 221-232 of mouse c-IAP1.
 
UniProt ID:Q62210
 
Species reactivity:Human, Mouse
 
Applications:WB
 
Recommended Dilutions/Conditions:Western Blot (1:1,000-1:4,000 using ECL; suggested blocking and dilution buffer is PBST containing 0.1% Tween 20 and either 5% skim milk or 5% BSA. Suggested incubation time is 1 hour at room temperature or overnight at 4°C.)
Suggested dilutions/conditions may not be available for all applications.
Optimal conditions must be determined individually for each application.
 
Application Notes:Detects a band of ~62kDa by Western blot.
Not recommended for Immunohistochemistry or Immunoprecipitation.
 
Positive Control:Included. (ALX-803-335-POS. Wild type MEF lysate in SDS loading buffer). Negative control also included (ALX-803-335-NEG. c-Iap1-/- MEF lysate in SDS loading buffer.)
 
Formulation:Liquid. 0.2μm-filtered solution in PBS containing 0.05% sodium azide.
 
Use/Stability:Stable for at least 12 months after receipt when stored at -80°C.
 
Handling:Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -80°C.
 
Shipping:Shipped on Dry Ice
 
Short Term Storage:+4°C
 
Long Term Storage:-80°C
 
Scientific Background:All members of the inhibitor of apoptosis proteins (IAP) family contain at least one, but usually three copies of baculovirus IAP repeat (BIR), a ~70-aa zinc binding domain, and upon overexpression suppress apoptosis. The BIR motif is capable of interacting with caspases and occluding their catalytic pockets. Certain IAPs also possess C-terminal RING domains. RING-containing proteins often act as E3 ubiquitin ligases and can catalyse the degradation of both, themselves and selected target proteins through ubiquitylation. So far, eight human IAPs have been identified: Apollon (Bruce), c-IAP1 (HIAP2; MIHB), c-IAP2 (HIAP1; MIHC), ILP-2 (Ts-IAP), Livin (ML-IAP; KIAP), NAIP, Survivin (TIAP) and XIAP (ILP-1; MIHA). c-IAP1 has been shown to inhibit specific caspases.
 
803-335
Figure 1: Western blot analysis of c-IAP1 in mouse bone marrow-derived macrophages of the indicated strains lysed in DISC buffer (150mM sodium chloride, 2mM EDTA, 1% Triton X-100, 10% glycerol, 20mM Tris pH 7.5) using MAb to c-IAP1 (1E1-1-10) (Prod. No. ALX-803-335) followed by HRP-anti rat antibody and developed by ECL.Molecular weight marker (kD) is shown at the left. Lanes have been digitally excised from a single blot to aid comparison.
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Figure 2: Western blot analysis of human c-IAP1 using MAb to c-IAP1 (1E1-1-10)A: MDA-MB-231 cell lysateB: MDA-MB-231 +LBW 1μM/1h cell lysate (LBW causes degradation of c-IAP1; A. Gaither, et al., 2007)(Image courtesy of Dr. Pascal Meier, The Institute of Cancer Research, London.)
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Figure 3: MAb to c-IAP1 (1E1-1-10) is specific for mouse and human c-IAP1. A) Wild type and c-IAP1-/- MEFs were treated +/- TWEAK for 6 hours and whole cell lysates prepared and separated on an SDS-PAGE gel, transferred to a PVDF membrane and probed with MAb to c-IAP1 (1E1-1-10). TWEAK causes a partial loss of c-IAP1. B) 4 human cell lines were treated overnight with an IAP antagonist that induces rapid degradation of c-IAP1. Cells were lysed with DISC lysis buffer and separated on an SDS-PAGE gel, transferred and probed with the MAb to c-IAP1 (1E1-1-10) as in A. XIAP and c-IAP2 blots demonstrate the specificity of the c-IAP1 antibody.
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Product Literature References

Coordinated ubiquitination and phosphorylation of RIP1 regulates necroptotic cell death: M.C. de Almagro, et al.; Cell Death Differ. 24, 26 (2017), Application(s): Western Blot, Abstract; Full Text
Cellular IAP proteins and LUBAC differentially regulate necrosome-associated RIP1 ubiquitination: M.C. de Almagro, et al.; Cell Death Dis. 6, e1800 (2015), Abstract; Full Text
Effects of physiological and synthetic IAP antagonism on c-IAP-dependent signaling: A.J. Kocab, et al.; Oncogene 34, 5472 (2015), Abstract;
An inactivating caspase 11 passenger mutation originating from the 129 murine strain in mice targeted for c-IAP1: N.S. Kenneth, et al.; Biochem. J. 443, 355 (2012), Application(s): WB using mouse embryonic fibroblast (MEF) cell lysate, Abstract; Full Text
Molecular determinants of Smac mimetic induced degradation of cIAP1 and cIAP2: M. Darding, et al.; Cell Death Differ. 18, 1376 (2011), Abstract; Full Text
TAK1 is required for survival of mouse fibroblasts treated with TRAIL, and does so by NF-kappaB dependent induction of cFLIPL: J.M. Lluis, et al.; PLoS One 5, e8620 (2010), Abstract; Full Text
TNF signaling, but not TWEAK triggered cellular Inhibitor of Apoptosis protein 1 (cIAP1) degradation, requires cIAP1 RING dimerization and E2 binding: R. Feltham, et al.; J. Biol. Chem. 285, 17525 (2010), Abstract; Full Text
Cellular IAPs inhibit a cryptic CD95-induced cell death by limiting RIP1 kinase recruitment: P. Geserick, et al.; J. Cell Biol. 187, 1037 (2009), Abstract; Full Text
TRAF2 must bind to cellular inhibitors of apoptosis for tumor necrosis factor (tnf) to efficiently activate nf-{kappa}b and to prevent tnf-induced apoptosis: J.E. Vince, et al.; J. Biol. Chem. 284, 35906 (2009), Abstract;
TWEAK-FN14 signaling induces lysosomal degradation of a cIAP1-TRAF2 complex to sensitize tumor cells to TNFalpha: J.E. Vince, et al.; J. Cell. Biol. 182, 171 (2008), Abstract; Full Text
A Smac mimetic rescue screen reveals roles for inhibitor of apoptosis proteins in tumor necrosis factor-alpha signaling: A. Gaither, et al.; Cancer Res. 67, 11493 (2007), Abstract; Full Text
IAP antagonists target cIAP1 to induce TNFalpha-dependent apoptosis: J.E. Vince, et al.; Cell 131, 682 (2007), Abstract;
Determination of cell survival by RING-mediated regulation of inhibitor of apoptosis (IAP) protein abundance: J. Silke, et al.; PNAS 102, 16182 (2005), Abstract; Full Text

General Literature References

Destabilizing influences in apoptosis: sowing the seeds of IAP destruction: S.J. Martin; Cell 109, 793 (2002), Review, Abstract;

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