Rabbit anti-Human CFLAR Polyclonal Antibody | anti-CFLAR antibody

CFLAR Antibody

Cat. Num. AAA9410489

• Gene Names: CFLAR; CASH; FLIP; MRIT; CLARP; FLAME; Casper; FLAME1; c-FLIP; FLAME-1; I-FLICE; c-FLIPL; c-FLIPR; c-FLIPS; CASP8AP1
• Reactivity: Human
• Applications: Western Blot, Immunohistochemistry
• Purity: Antibodies were purified by affinity purification using immunogen.
• Synonyms: CFLAR; Polyclonal Antibody; CFLAR Antibody; CASH; CASP8AP1; CLARP; Casper; FLAME; anti-CFLAR antibody

• Host: Rabbit
• Reactivity: Human
• Clonality: Polyclonal
• Specificity: The antibody detects endogenous level of total CFLAR protein.
• Purity/Purification: Antibodies were purified by affinity purification using immunogen.
• Form/Format: Supplied at 1.0mg/mL in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
• Concentration: 1.0 mg/ml (varies by lot)
• Sequence Length: 480

• Applicable Applications for anti-CFLAR antibody: Western Blot (WB), Immunohistochemistry (IHC)
• Application Notes: Western blotting: 1:500 - 1:2000; Immunohistochemistry: 1:50 - 1:200
• Immunogen Type: Recombinant Protein
• Immunogen Description: Recombinant protein of human CFLAR.
• Target Name: CFLAR
• Preparation and Storage: Store at -20 degree C

Western Blot (WB)

(Western blot analysis of extracts of Jurkat cell lines, using CFLAR antibody.)

Immunohistochemistry (IHC)

(Immunohistochemical analysis of paraffin-embedded rat testis using CFLAR antibody at dilution of 1:200 (200x lens).)

Related Product Information for anti-CFLAR antibody

Cellular FLIP (FLICE inhibitory protein) is a regulator of apoptosis that has various names, such as c-FLIP (1), Casper (2), CLARP (3), FLAME (4), I-FLICE (5), MRIT (6), CASH (7), and Usurpin (8). FLIP is expressed as two alternative splice isoforms, FLIP short (FLIPS) and FLIP long (FLIPL). FLIPS contains two death effector domains (DEDs) like those found on the death receptor adaptor protein FADD and the pro-domain of caspase-8. FLIPL shares significant homology with caspase-8 (FLICE), and contains an additional death effector domain, but FLIPL lacks the catalytic active site of the caspases and does not have protease activity. Both FLIP isoforms have been reported to interact with FADD and pro-caspase-8. The role of FLIP in apoptosis is controversial as some research studies have reported it to be anti-apoptotic, while others claim that it is pro-apoptotic. Overexpression of FLIPL can lead to caspase-8 heterodimers that produce an active protease, resulting in apoptosis. However, at physiological levels, it is thought that the binding of FLIP to the DED of FADD results in inhibition of caspase-8 processing. Reduction of FLIP by siRNA or gene targeting sensitizes cells to death receptor-mediated apoptosis. FLIP has also been implicated in the resistance of cancer cells to apoptosis and is upregulated in some cancer types including Hodgkin's lymphoma and ovarian and colon carcinomas (9).

Product Categories/Family for anti-CFLAR antibody

Total protein Ab

NCBI and Uniprot Product Information

• NCBI GI #: 187608577
• NCBI GeneID: 8837
• NCBI Accession #: NP_001120655.1
• NCBI GenBank Nucleotide #: NM_001127183.2
• UniProt Accession #: O15519; O14673; O14674; O14675; O15137; O15138; O15356; O15510; O43618; O43619; B4DJE0; B7Z9F9
• Molecular Weight: 44,112 Da
• NCBI Official Full Name: CASP8 and FADD-like apoptosis regulator isoform 1
• NCBI Official Synonym Full Names: CASP8 and FADD-like apoptosis regulator
• NCBI Official Symbol: CFLAR
• NCBI Official Synonym Symbols: CASH; FLIP; MRIT; CLARP; FLAME; Casper; FLAME1; c-FLIP; FLAME-1; I-FLICE; c-FLIPL; c-FLIPR; c-FLIPS; CASP8AP1
• NCBI Protein Information: CASP8 and FADD-like apoptosis regulator
• UniProt Protein Name: CASP8 and FADD-like apoptosis regulator
• Protein Family: CASP8 and FADD-like apoptosis regulator
• UniProt Gene Name: CFLAR
• UniProt Synonym Gene Names: CASH; CASP8AP1; CLARP; MRIT; CASH; Casper; CLARP; c-FLIP; FLAME-1; I-FLICE; MRIT
• UniProt Entry Name: CFLAR_HUMAN

NCBI Description

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. [provided by RefSeq, Feb 2011]

Uniprot Description

CFLAR: Apoptosis regulator protein which may function as a crucial link between cell survival and cell death pathways in mammalian cells. 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. TNFRSF6 stimulation triggers recruitment to the death- inducing signaling complex (DISC) formed by TNFRSF6, FADD and caspase-8. A proteolytic fragment (p43) stays associated with the DISC. Also interacts with caspase-10, caspase-3, TRAF1, TRAF2 and Bcl-X(L) (in vitro). Interacts with HBV protein X. Repressed by IL2/interleukin-2 after TCR stimulation, during progression to the S phase of the cell cycle. Widely expressed. Higher expression in skeletal muscle, pancreas, heart, kidney, placenta, and peripheral blood leukocytes. Also detected in diverse cell lines. Isoform 8 is predominantly expressed in testis and skeletal muscle. Belongs to the peptidase C14A family. 14 isoforms of the human protein are produced by alternative splicing.

Protein type: Apoptosis

Chromosomal Location of Human Ortholog: 2q33-q34

Cellular Component: cytoplasm; CD95 death-inducing signaling complex; cytosol; lipid raft

Molecular Function: protein binding; protease binding; cysteine-type endopeptidase activity; death receptor binding; enzyme activator activity; protein complex binding

Biological Process: caspase activation; skeletal muscle development; skeletal myofibril assembly; skeletal muscle atrophy; positive regulation of I-kappaB kinase/NF-kappaB cascade; viral reproduction; apoptosis; skeletal muscle regeneration; regulation of satellite cell proliferation; proteolysis; negative regulation of apoptosis; activation of NF-kappaB transcription factor