Recombinant Human cIAP1 protein
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Recombinant Human cIAP1 protein is a Human Full Length protein, in the 1 to 618 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.
View Alternative Names
API1, MIHB, RNF48, BIRC2, Baculoviral IAP repeat-containing protein 2, Cellular inhibitor of apoptosis 1, IAP homolog B, Inhibitor of apoptosis protein 2, RING finger protein 48, RING-type E3 ubiquitin transferase BIRC2, TNFR2-TRAF-signaling complex protein 2, C-IAP1, hIAP-2, hIAP2
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human cIAP1 protein (AB114410)
12.5% SDS-PAGE analysis of ab114410, stained with Coomassie Blue.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
CIAP1 plays an important role in regulating apoptosis by inhibiting the activity of certain caspases including caspase-3 and caspase-7. It is often part of larger protein complexes that include other members of the IAP family such as cIAP2. By binding directly to tumor necrosis factor receptor-associated factors (TRAFs) cIAP1 helps modulate signaling pathways that determine cell survival or death contributing to cellular homeostasis.
Pathways
CIAP1 is intricately involved in the NF-κB signaling pathway and the TNF receptor signaling pathway. Its interaction with TRAFs links it to these critical pathways helping to control inflammatory and immune responses. Other proteins related to cIAP1 through these pathways include RIP1 and TRAF2 both important for transmitting signals that affect cell fate decisions.
Specifications
Form
Liquid
General info
Function
Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, mitogenic kinase signaling, and cell proliferation, as well as cell invasion and metastasis. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and regulates both canonical and non-canonical NF-kappa-B signaling by acting in opposite directions : acts as a positive regulator of the canonical pathway and suppresses constitutive activation of non-canonical NF-kappa-B signaling. The target proteins for its E3 ubiquitin-protein ligase activity include : RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, TRAF2, DIABLO/SMAC, MAP3K14/NIK, MAP3K5/ASK1, IKBKG/NEMO, IKBKE and MXD1/MAD1. Can also function as an E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation. Acts as an important regulator of innate immune signaling via regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs) and RIG-I like receptors (RLRs), collectively referred to as pattern recognition receptors (PRRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. Can stimulate the transcriptional activity of E2F1. Plays a role in the modulation of the cell cycle.
Sequence similarities
Belongs to the IAP family.
Post-translational modifications
Auto-ubiquitinated and degraded by the proteasome in apoptotic cells.. Upon stimulation of death receptors, including TNFRSF10B, recruited to receptors and cleaved by caspases. Proteolytic fragments remain associated with the receptors. This cleavage presumably inactivates the protein.
Subcellular localisation
Nucleus
Target data
Product promise
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