CFLAR Proteins

CFLAR (CASP8 And FADD Like Apoptosis Regulator) is a Protein Coding gene. Diseases associated with CFLAR include Cerebral Arteriopathy, Autosomal Dominant, With Subcortical Infarcts And Leukoencephalopathy, Type 1 and Colon Adenocarcinoma. Among its related pathways are Apoptosis and survival Caspase cascade and CDK-mediated phosphorylation and removal of Cdc6. Gene Ontology (GO) annotations related to this gene include cysteine-type peptidase activity. An important paralog of this gene is CASP8.

The following recombinant CFLAR proteins are manufactured in house under a complete QC system by CUSABIO. They are expressed by Yeast, E.coli, Baculovirus, Mammalian cell, In Vivo Biotinylation in E.coli. Highlights of these recombinant CFLAR proteins as follow:
High purity, Low endotoxin, Multiple Tags, Animal-free, Wide applications (Cell assay, Protein-protein interaction, Drug-related studies, Enzymatic activity in vitro, Protein structure analysis, etc.)
In addition, various options on sizes, excellent technical support, and recombinant CFLAR proteins custom service will be also offered.

CFLAR Proteins Catalog

CFLAR Proteins for Mus musculus (Mouse)

CFLAR Proteins for Homo sapiens (Human)

CFLAR Proteins for Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)

CFLAR Background

CFLAR, short for CASP8 and FADD-like apoptosis regulator, is also known as cellular FLICE--like inhibitory protein (c-FLIP). c-FLIP is expressed constitutively in many cell types, but its lifespan is short because its expression can be regulated by a variety of stimuli [1]. Although many splice variants of c-FLIP have been reported at the mRNA level, only short FLIP (c-FLIPS) and long FLIP (c-FLIPL) could be detected on the protein level as so far [2]. As the mammalian homolog of v-FLIP (virus FLICE-like inhibitory protein), c-FLIP is structurally and sequentially homologous with caspase-8 and caspase-10 that are involved in the initiation of DR (death receptor)-induced apoptosis. c-FLIP consists of two sequential N-terminal DEDs (death effector domain), followed by a C-terminal extension containing a caspase-homologous domain analogous to caspase-8 and caspase-10. Nevertheless, c-FLIP is catalytically inactive because several amino acids conserved in caspases are substituted, such as the cysteine residue within the QACXG-motif and the histidine residue within the HG-motif [3][4]. c-FLIP acts as a dominant-negative inhibitor to hinder apoptosis caused by death-inducing ligands through the binding of the FAS-associated death domain (FADD) protein and/or caspases-8 and caspase-10 at the level of the death-inducing signaling complex (DISC) [5]. Consistently, Yeh WC et al. revealed a protective role for c-FLIP in DR-induced apoptosis of fibroblast cell lines derived from c-FLIP-knockout mice [6]. Since c-FLIP is a major regulator of DR-induced apoptosis, and since the aberrant c-FLIP expression is intertwined with a rising number of pathologies, detecting c-FLIP levels might be valuable to diagnosis, and drugs that only change c-FLIP-expression levels will certainly be a benefit in the treatment of relevant diseases [7].

[1] Micheau O, Lens S, et al. NF-kappaB signals induce the expression of c-FLIP [J]. Mol Cell Biol. 2001 Aug; 21(16):5299-305.
[2] Scaffidi C., Schmitz I., et al. The role of c-FLIP in modulation of CD95-induced apoptosis [J]. J. Biol. Chem. 1999, 274:1541-1548.
[3] Thome M, Tschopp J Regulation of lymphocyte proliferation and death by FLIP [J]. Nat Rev Immunol. 2001 Oct; 1(1):50-8.
[4] Nicholson DW, Thornberry NA Caspases: killer proteases [J]. Trends Biochem Sci. 1997 Aug; 22(8):299-306.
[5] Irmler M, Thome M, et al. Inhibition of death receptor signals by cellular FLIP [J]. Nature. 1997 Jul 10; 388(6638):190-5.
[6] Yeh WC, Itie A, et al. Requirement for Casper (c-FLIP) in regulation of death receptor-induced apoptosis and embryonic development. Immunity [J]. 2000 Jun; 12(6):633-42.
[7] Olivier Micheau. Cellular FLICE-inhibitory protein: an attractive therapeutic target?[J] Expert Opin Ther Targets. 2003 Aug; 7(4): 559-573.


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