HPA019044
Anti-CFLAR antibody produced in rabbit
affinity isolated antibody, buffered aqueous glycerol solution
Sinônimo(s):
Anti-C-FLIP, Anti-CASH, Anti-CASP8 and FADD-like apoptosis regulator, Anti-CASP8AP1, Anti-CLARP, Anti-Casper, Anti-FLAME, Anti-FLIP, Anti-I-FLICE, Anti-MRIT
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About This Item
conjugado:
unconjugated
application:
IF
IHC
IHC
clone:
polyclonal
reatividade de espécies:
human
citations:
4
técnica(s):
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:200-1:500
immunohistochemistry: 1:200-1:500
Produtos recomendados
fonte biológica
rabbit
Nível de qualidade
conjugado
unconjugated
forma do anticorpo
affinity isolated antibody
tipo de produto de anticorpo
primary antibodies
clone
polyclonal
linha de produto
Prestige Antibodies® Powered by Atlas Antibodies
Formulário
buffered aqueous glycerol solution
reatividade de espécies
human
técnica(s)
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:200-1:500
sequência de imunogênio
IHQVEEALDTDEKEMLLFLCRDVAIDVVPPNVRDLLDILRERGKLSVGDLAELLYRVRRFDLLKRILKMDRKAVETHLLRNPHLVSDYRVLMAEIGEDLDKSDVSS
nº de adesão UniProt
Condições de expedição
wet ice
temperatura de armazenamento
−20°C
modificação pós-traducional do alvo
unmodified
Informações sobre genes
human ... CFLAR(8837)
Descrição geral
The gene CFLAR (CASP8 and FADD-like apoptosis regulator) is mapped to human chromosome 2q33-q34. The protein localizes in the cytoplasm. CFLAR is commonly referred as c-FLIP (Cellular FLICE-like inhibitory protein).
Imunogênio
CASP8 and FADD-like apoptosis regulator recombinant protein epitope signature tag (PrEST)
Aplicação
Anti-CFLAR antibody produced in rabbit, a Prestige Antibody, is developed and validated by the Human Protein Atlas (HPA) project . Each antibody is tested by immunohistochemistry against hundreds of normal and disease tissues. These images can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. The antibodies are also tested using immunofluorescence and western blotting. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.
Ações bioquímicas/fisiológicas
CFLAR (CASP8 and FADD-like apoptosis regulator) has been shown to suppress CD95-mediated apoptosis via inhibition of caspase-8 processing at the death-inducing signaling complex (DISC). Increase in levels of CFLAR inhibits Hepatitis B virus (HBV) X protein-mediated apoptosis. Presence of CFLAR protects cells from Fas, TNF (tumor necrosis factor) and TRAIL (TNF-related apoptosis-inducing ligand) receptors induced apoptosis. CFLAR is also associated with tumor growth and escape from immunity.
Características e benefícios
Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.
Every Prestige Antibody is tested in the following ways:
Every Prestige Antibody is tested in the following ways:
- IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
- Protein array of 364 human recombinant protein fragments.
Ligação
Corresponding Antigen APREST74820
forma física
Solution in phosphate buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide.
Informações legais
Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany
Exoneração de responsabilidade
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Código de classe de armazenamento
10 - Combustible liquids
Classe de risco de água (WGK)
WGK 1
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
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M Stacey Ricci et al.
Molecular and cellular biology, 24(19), 8541-8555 (2004-09-16)
Tumor necrosis factor alpha (TNF-alpha)-related apoptosis-inducing ligand (TRAIL) is a member of the TNF-alpha family of death receptor ligands and holds great therapeutic potential as a tumor cell-specific cytotoxic agent. Using a panel of established tumor cell lines and normal
Kyun-Hwan Kim et al.
The EMBO journal, 22(9), 2104-2116 (2003-05-03)
Despite its implication in the progression of hepatitis B virus (HBV)-associated liver disease, the pro-apoptotic function of HBx protein remains poorly understood. We show that the expression of HBx leads to hyperactivation of caspase-8 and caspase-3 upon treatment with tumor
C Scaffidi et al.
The Journal of biological chemistry, 274(3), 1541-1548 (1999-01-09)
Upon stimulation, CD95 (APO-1/Fas) recruits the adapter molecule Fas-associated death domain protein (FADD)/MORT1 and caspase-8 (FADD-like interleukin-1beta-converting enzyme (FLICE)/MACH/MCH5) into the death-inducing signaling complex (DISC). Recently, a molecule with sequence homology to caspase-8 was identified, termed cellular FLICE-inhibitory protein (c-FLIP).
David R Jones et al.
Journal of thoracic oncology : official publication of the International Association for the Study of Lung Cancer, 7(11), 1683-1690 (2012-10-13)
Despite complete surgical resection survival in early-stage non-small-cell lung cancer (NSCLC) remains poor. On the basis of prior preclinical evaluations, we hypothesized that combined induction proteasome and histone deacetylase inhibitor therapy, followed by tumor resection, is feasible. A phase I
Sireesha V Garimella et al.
Breast cancer research : BCR, 16(2), R41-R41 (2014-04-22)
Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) binds to its receptors, TRAIL-receptor 1 (TRAIL-R1) and TRAIL-receptor 2 (TRAIL-R2), leading to apoptosis by activation of caspase-8 and the downstream executioner caspases, caspase-3 and caspase-7 (caspase-3/7). Triple-negative breast cancer (TNBC) cell lines with
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