CASP8 and FADD-like apoptosis regulator Adenovirus
FLIP (FLICE inhibitory protein), also designated CLARP, Casper, I-FLICE, FLAME-1 and MRIT, is expressed as both long (FLIPL) and short (FLIPS) isoforms and is involved in the regulation of apoptosis. The short form of FLIP contains two death effector domains homologous to the death effector domain of the FAS-associating protein FADD. The long form of FLIP contains an additional caspase-like domain, but lacks a catalytic active site and the residues that form the substrate binding pocket in most caspases.
1525
Ad-FLIP
Ready-to-use CASP8 and FADD-like apoptosis regulator Adenovirus. Ad-FLIP, CASP8 and FADD-like apoptosis regulator, CASH, FLIP, MRIT, CFLAR, CLARP, FLAME, CASPER, FLAME-1, I-FLICE, USURPIN, CASP8AP1 adenovirus 1525
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Gene Reference Data
Alternate Names
c-FLIP; c-FLIPL; c-FLIPR; c-FLIPS; CASH; CASP8AP1; Casper; CLARP; FLAME; FLAME-1; FLAME1; FLIP; I-FLICE; MRIT
Description (Vector)
CFLAR 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.
Gene ID
8837
Gene Name (Vector)
CASP8 and FADD like apoptosis regulator
Gene Symbol
CFLAR
HGNC ID
HGNC:1876
ORF Size (aa)
1443
ORF Size (bp)
1443 bp
RefSeq ID
NM_003879
RefSeq Synonyms
NM_003879, NM_001308043, NM_001308042, NM_001202519, NM_001202518, NM_001202517, NM_001202516, NM_001202515, NM_001127184, NM_001127183, BC001602,
Species
human
UniGene ID
Hs.390736
Related Citations
- Histone Deacetylase Inhibitors Interact with MDA-7/IL-24 to Kill Primary Human Glioblastoma Cells. Hossein A Hamed, etc, (2013), Molecular Pharmacology
- 17AAG and MEK1/2 inhibitors kill GI tumor cells via Ca2+-dependent suppression of GRP78/BiP and induction of ceramide and ROS. Teneille Walker, ETC, (2010), Mol Cancer Ther
- Smac Mimetic Compounds Potentiate Interleukin-1ß-mediated Cell Death. Cheung HH, etc, (2010), J Biol Chem
- Inhibition of Multiple Protective Signaling Pathways and Ad. 5/3 Delivery Enhances mda-7/IL-24 Therapy of Malignant Glioma. Hossein A Hamed, (2010), Molecular Therapy
- PERK-dependent regulation of ceramide synthase 6 and thioredoxin play a key role in mda-7/IL-24-induced killing of primary human glioblastoma multiforme cells. Adly Yacoub, (2009), Cancer Research
- Cisplatin Enhances Protein Kinase R-Like Endoplasmic Reticulum Kinase- and CD95-Dependent Melanoma Differentiation-Associated Gene-7/Interleukin-24¿Induced Killing in Ovarian Carcinoma Cells. Adly Yacoub, (2009), Molecular Pharmacology
- Mek1/2 Inhibitors And 17AAG Synergize To Kill Human Gi Tumor Cells In Vitro Via Suppression Of C-Flip-S Levels And Activation Of Cd95. Park MA, etc, (2009), Mol Cancer Ther
- Sorafenib And Vorinostat Kill Colon Cancer Cells By Cd95-Dependent And -Independent Mechanisms. Walker T, etc, (2009), Mol Pharmacol
- Bcl-2 Family Inhibitors Enhance Histone Deacetylase Inhibitor And Sorafenib Lethality Via Autophagy And Overcome Blockade Of The Extrinsic Pathway To Facilitate Killing. Martin, AP. etc, (2009), Mol Pharmacol
- Synergistic Interactions Between Interferon-{Gamma} And Trail Modulate C-Flip In Endothelial Cells, Mediating Their Lineage-Specific Sensitivity To Thrombotic Thrombocytopenic Purpura Plasma¿Associated Apoptosis. Stefanescu, R., etc., (2008), Blood
- Vorinostat And Sorafenib Synergistically Kill Tumor Cells Via Flip Suppression And Cd95 Activation. Zhang, G., etc., (2008), Clinical Cancer Research
- Caspase-, cathepsin-, and PERK-dependent regulation of MDA-7/IL-24-induced cell killing in primary human glioma cells. Yacoub, A. etc, (2008), Molecular Cancer Therapeutics
- Regulation Of Gst-Mda-7 Toxicity In Human Glioblastoma Cells By Erbb1, Erk1/2, Pi3k, And Jnk1-3 Pathway Signaling. Yacoub, A., etc., (2008), Molecular Cancer Therapeutics
- Vorinostat And Sorafenib Increase Er Stress, Autophagy And Apoptosis Via Ceramide-Dependent Cd95 And Perk Activation. Park MA, etc, (2008), Cancer Biol Ther
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About Storage Conditions
All our viral products should be kept at -80°C. At this temperature, the virus will remain stable for 6-12 months (and in some cases, up to 2 years). Once thawed, the product can be stored at 4°C for 2-3 weeks without significant loss of biological activity.
We recommend aliquoting your vectors into low protein binding tubes upon receipt. This helps avoid repeated freeze-thaw cycles, as well as prevent loss of virus. To maintain accurate titer, aliquot in at least 20ul per tube.