Recombinant Human FLIP protein (denatured) (Tag Free)
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Recombinant Human FLIP protein (denatured) (Tag Free) is a Human Full Length protein, in the 1 to 480 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE.
대체 명칭 보기
CASH, CASP8AP1, CLARP, MRIT, CFLAR, CASP8 and FADD-like apoptosis regulator, Caspase homolog, Caspase-eight-related protein, Caspase-like apoptosis regulatory protein, Cellular FLICE-like inhibitory protein, FADD-like antiapoptotic molecule 1, Inhibitor of FLICE, MACH-related inducer of toxicity, Usurpin, Casper, c-FLIP, FLAME-1, I-FLICE
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human FLIP protein (denatured) (Tag Free) (AB111628)
15% SDS-PAGE showing ab111628 at approximately 55.3kDa (3μg).
보완 제품
Reagents, Controls & Accessories
AB116027
Prestained Protein Ladder - Mid-range molecular weight (10 - 180 kDa)
- 5
- 2
Reactivity 정보
서열 정보
특성 및 보관 정보
제형
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분주 정보
보관 정보
추가 정보
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
FLIP protein impacts cellular processes by blocking the activation of caspase-8 preventing the apoptosis cascade from proceeding. It is not typically part of a large complex but interacts directly with the death-inducing signaling complex (DISC). By inhibiting the apoptotic machinery it protects cells from unnecessary death signals facilitating controlled cellular turnover and immune responses.
Pathways
FLIP affects apoptosis and NF-kB signaling. These pathways are vital for cell survival inflammation and immune responses. FLIP interacts closely with Fas-associated protein with death domain (FADD) and caspase-8 to regulate apoptotic pathways. It acts as a checkpoint in intrinsic and extrinsic apoptosis pathways thereby influencing both normal and pathological processes such as immune cell survival and proliferation.
일반 정보
기능
Apoptosis regulator protein which may function as a crucial link between cell survival and cell death pathways in mammalian cells (PubMed : 31046799). Acts as an inhibitor of TNFRSF6 mediated apoptosis. A proteolytic fragment (p43) is likely retained in the death-inducing signaling complex (DISC) thereby blocking further recruitment and processing of caspase-8 at the complex. Full length and shorter isoforms have been shown either to induce apoptosis or to reduce TNFRSF-triggered apoptosis. Lacks enzymatic (caspase) activity.
서열 유사성
Belongs to the peptidase C14A family.
Post-translational modifications
Proteolytically processed by CASP8 generating subunit p43 and p12.. Deubiquitinated by USP40, leading to stabilization.
타겟 정보
Product promise
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