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PathScan® RP c-IAP1 Sandwich ELISA Kit #50735

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    Product Specifications

    REACTIVITY H
    Application Key:
    • ELISA+-ELISA and/or ELISA-like Assays 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Description

    The rapid protocol (RP) PathScan® RP c-IAP1 Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of c-IAP1 protein in a reduced assay time of 1.5 hours. Incubation of cell lysates and detection antibody on the coated microwell plate forms a sandwich with c-IAP1 in a single step. The plate is then extensively washed and TMB reagent is added for signal development. The magnitude of absorbance for the developed color is proportional to the quantity of c-IAP1 protein. Learn more about your ELISA kit options here.

    *Antibodies in this kit are custom formulations specific to kit.

    Protocol

    Specificity / Sensitivity

    The PathScan® RP c-IAP1 Sandwich ELISA Kit detects endogenous levels of c-IAP1 protein. The kit sensitivity is shown in Figure 1. This kit detects proteins from the indicated species, as determined through in-house testing, but may also detect homologous proteins from other species.

    Species Reactivity:

    Human

    Background

    The inhibitor of apoptosis protein (IAP) family consists of an evolutionarily conserved group of apoptosis inhibitors containing a conserved 70 amino acid BIR (baculovirus inhibitor repeat) domain (1,2). Human members of this family include c-IAP1, c-IAP2, XIAP, survivin, livin, and NAIP. Overexpression of IAP family members, particularly survivin and livin, in cancer cell lines and primary tumors suggests an important role for these proteins in cancer progression (3-5). In general, the IAP proteins function through direct interactions to inhibit the activity of several caspases, including caspase-3, caspase-7, and caspase-9 (5,6). In addition, binding of IAP family members to the mitochondrial protein Smac blocks their interaction with caspase-9, thereby allowing the processing and activation of the caspase (2).

    c-IAP1 (gene name: BIRC2), which is structurally and functionally closely related to c-IAP2 (gene name: BIRC3), also contains a RING domain that confers E3 ubiquitin ligase activity (7). c-IAP1 is recruited to the TNF receptor complex upon ligand binding and functions as a positive regulator of the canonical NF-κB signaling pathway, leading to autoubiquitination as well as ubiquitination of other signaling targets, including RIP1 and TRAF family members (8-11). c-IAP is frequently overexpressed in many cancers, contributing to tumorigenesis by inhibiting apoptosis (12,13). IAP inhibitors, like Smac mimetics, can result in c-IAP1 degradation and have been pursued as therapeutic opportunities (14).

    Alternate Names

    API1; apoptosis inhibitor 1; baculoviral IAP repeat containing 2; baculoviral IAP repeat-containing 2; Baculoviral IAP repeat-containing protein 2; BIRC2; C-IAP1; Cellular inhibitor of apoptosis 1; cIAP1; hIAP-2; hIAP2; IAP homolog B; IAP-2; IAP2; Inhibitor of apoptosis protein 2; MIHB; NFR2-TRAF signalling complex protein; RING finger protein 48; RING-type E3 ubiquitin transferase BIRC2; RNF48; TNFR2-TRAF-signaling complex protein 2

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