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Browse our CFLAR Proteins (CFLAR)

Full name:
CASP8 and FADD-Like Apoptosis Regulator Proteins (CFLAR)
On are 13 CASP8 and FADD-Like Apoptosis Regulator (CFLAR) Proteins from 7 different suppliers available. Additionally we are shipping CFLAR Antibodies (266) and CFLAR Kits (8) and many more products for this protein. A total of 308 CFLAR products are currently listed.
2310024N18Rik, A430105C05Rik, c-Flip, c-FLIPL, c-FLIPR, c-FLIPS, Cash, CASP8AP1, Casper, CFLAR, CLARP, Clarp1, ENSMUSG00000072980, FLAME, FLAME-1, FLAME1, Flip, Gm9845, I-FLICE, MRIT
list all proteins Gene Name GeneID UniProt
CFLAR 8837 O15519
CFLAR 12633 O35732
CFLAR 117279  

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CFLAR Proteins (CFLAR) by Origin

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Top referenced CFLAR Proteins

  1. Human CFLAR Protein expressed in Escherichia coli (E. coli) - ABIN667543 : Thome, Schneider, Hofmann, Fickenscher, Meinl, Neipel, Mattmann, Burns, Bodmer, Schröter, Scaffidi, Krammer, Peter, Tschopp: Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors. in Nature 1997 (PubMed)
    Show all 2 references for ABIN667543

More Proteins for CFLAR Interaction Partners

Human CASP8 and FADD-Like Apoptosis Regulator (CFLAR) interaction partners

  1. association of c-FLIPL and TIP49 provided an additional mechanism involved in c-FLIPL-mediated functions, including Wnt (show WNT2 Proteins) activation

  2. CFLAR role in the necroptosis in fibroblasts

  3. TRAIL can enhance RIP1 (show UQCRFS1 Proteins) and c-FLIPL expression in HepG2 cells.

  4. Combined triple actions of the TRAIL, the IAPs inhibitor, AT406, and the c-FLIP expression inhibitor, rocaglamide (ART), markedly improve TRAIL-induced apoptotic effects in most solid cancer cell lines through the activation of an extrinsic apoptosis pathway

  5. Our results postulate that thymoquinone induces apoptosis through downregulating c-FLIP and Bcl-2 which can be utilized as a chemotherapeutic agent to treat renal carcinoma.

  6. knockdown of cFLIPL and induced expression of FADD (show FADD Proteins) rapidly accumulate intracellular ROS (show ROS1 Proteins) accompanied by JNK1 (show MAPK8 Proteins) activation to substantiate apoptosis.

  7. Data show that heterogeneous nuclear ribonucleoprotein K (hnRNPK) stabilized of cellular FLICE-inhibitory protein (c-FLIP) protein through inhibition of glycogen synthase kinase 3 beta (GSK3beta) Ser9 phosphorylation during the TNF-related aoptosis-inducing ligand (TRAIL)-induced apoptosis.

  8. Data indicate that FADD (show FADD Proteins) mediated apoptotic cell death was directed by ubiquitination of cFLIPL and inhibition of NF-kappaB (show NFKB1 Proteins) activation.

  9. cFLIP long form shRNA serves a specific inhibitory role in cellular proliferation through inducing the activation of the JNK (show MAPK8 Proteins) pathway in A875 cells.

  10. Study demonstrated the function of FLIPL in facilitating hepatocellular carcinoma cells (HCC (show FAM126A Proteins)) aerobic glycolysis by modulating SGLT1 (show SLC5A1 Proteins)-mediated glucose uptake and FLIPL expression level was positively correlated with SGLT1 (show SLC5A1 Proteins) expression level in patients with HCC (show FAM126A Proteins).

Mouse (Murine) CASP8 and FADD-Like Apoptosis Regulator (CFLAR) interaction partners

  1. knockdown of cFLIPL and induced expression of FADD (show FADD Proteins) rapidly accumulate intracellular ROS (show ROS1 Proteins) accompanied by JNK1 (show MAPK8 Proteins) activation to substantiate apoptosis.

  2. CASP8 (show CASP8 Proteins) is present exclusively as its cleaved p43 (show AIMP1 Proteins) product, bound to cFLIPL.

  3. The generation of mouse line with Flip deficiency in cells that express cre under the CD11c (show ITGAX Proteins) promoter is reported.

  4. c-FLIPL deficiency induces the caspase (show CASP3 Proteins)-mediated processing of RTN4 (show RTN4 Proteins), thus affecting endoplasmic reticulum (ER) shape and coupling to mitochondria. Thus, it was concluded that c-FLIPL is a novel regulator of ER morphology and ER-mitochondria crosstalk.

  5. Acute organ failure following the loss of anti-apoptotic cellular FLICE-inhibitory protein involves activation of innate immune receptors.

  6. The results reveal a novel inhibitory role of c-FLIP in myeloid cell activation and demonstrate the unexpected anti-inflammatory activity of c-FLIP.

  7. Upon starvation, c-Flip affects lipid accumulation, ER stress and autophagy, thereby pointing to an important role of c-Flip in the adaptive response and ER stress response programs under both normal and pathological conditions.

  8. Flip preserves cardiac functions and inhibits cardiac hypertrophy partially by blocking ASK1 (show MAP3K5 Proteins)/P38 (show CRK Proteins) signaling.

  9. These data suggest that c-FLIP is a negative regulator of intrinsic apoptosis pathway in T lymphocytes.

  10. c-FLIPR is an important modulator of apoptosis and enforced expression leads to autoimmunity.

Cow (Bovine) CASP8 and FADD-Like Apoptosis Regulator (CFLAR) interaction partners

  1. results indicate downregulation of cFLIP during structural luteal regression, suggesting that cFLIP plays a survival role in the bovine corpus luteum

  2. Conservation of FLIP's ability to inhibit apoptosis and to downregulate NF-kappaB (show NFKB1 Proteins) activation across species.

Pig (Porcine) CASP8 and FADD-Like Apoptosis Regulator (CFLAR) interaction partners

  1. cellular-Flice like inhibitory protein (cFLIP) long form, plays an anti-apoptotic role in the granulosa cells of healthy follicles of pig ovaries [cFLIP]

  2. Intracellular remodeling with overexpression of pig c (show PIGC Proteins)-FLIP in xenograft cells may decrease the innate cellular responses against xenografts, facilitating long-term xenograft survival.

  3. Intracellular remodeling with the overexpression of c-FLIP(S/L) in xenograft cells may avoid innate cellular attacks against xenografts and facilitate long-term xenograft survival.

  4. Overexpression of c-FLIP in xenograft cells may prevent innate cellular attacks against xenografts opening the window of opportunity for long-term xenograft survival.

CFLAR Protein Profile

Protein Summary

The protein encoded by this gene is a regulator of apoptosis and is structurally similar to caspase-8. However, the encoded protein lacks caspase activity and appears to be itself cleaved into two peptides by caspase-8. Several transcript variants encoding different isoforms have been found for this gene, and partial evidence for several more variants exists.

Alternative names and synonyms associated with CFLAR

  • CASP8 and FADD-like apoptosis regulator a (cflara)
  • CASP8 and FADD-like apoptosis regulator (CFLAR)
  • CASP8 and FADD-like apoptosis regulator (cflar)
  • CASP8 and FADD-like apoptosis regulator (Cflar)
  • cellular FLICE-like inhibitory protein (C-FLIP)
  • 2310024N18Rik protein
  • A430105C05Rik protein
  • c-Flip protein
  • c-FLIPL protein
  • c-FLIPR protein
  • c-FLIPS protein
  • Cash protein
  • CASP8AP1 protein
  • Casper protein
  • CFLAR protein
  • CLARP protein
  • Clarp1 protein
  • ENSMUSG00000072980 protein
  • FLAME protein
  • FLAME-1 protein
  • FLAME1 protein
  • Flip protein
  • Gm9845 protein
  • I-FLICE protein
  • MRIT protein

Protein level used designations for CFLAR

FLIP , CASP8 and FADD-like apoptosis regulator , flice/caspase-i inhibitory protein , cellular FLICE-like inhibitory protein , CASP8 and FADD-like apoptosis regulator-like , FADD-like anti-apoptotic molecule , FADD-like antiapoptotic molecule 1 , MACH-related inducer of toxicity , caspase homolog , caspase-eight-related protein , caspase-like apoptosis regulatory protein , caspase-related inducer of apoptosis , inhibitor of FLICE , usurpin beta , usurpin , FLICE-like inhibitory protein

373114 Danio rerio
424080 Gallus gallus
459872 Pan troglodytes
574234 Macaca mulatta
779578 Xenopus (Silurana) tropicalis
780745 Xenopus laevis
100142680 Felis catus
100393782 Callithrix jacchus
100474872 Ailuropoda melanoleuca
100589650 Nomascus leucogenys
8837 Homo sapiens
12633 Mus musculus
488471 Canis lupus familiaris
497199 Bos taurus
117279 Rattus norvegicus
100172025 Pongo abelii
414381 Sus scrofa
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