F9675
Anti-FLIPL C-Terminal antibody produced in rabbit
~0.5 mg/mL, IgG fraction of antiserum, buffered aqueous solution
别名:
Anti-CASHα
生物来源
rabbit
质量水平
偶联物
unconjugated
抗体形式
IgG fraction of antiserum
抗体产品类型
primary antibodies
克隆
polyclonal
表单
buffered aqueous solution
分子量
antigen 53 kDa
种属反应性
mouse
浓度
~0.5 mg/mL
技术
ELISA: suitable
immunocytochemistry: suitable
western blot: suitable
UniProt登记号
运输
dry ice
储存温度
−20°C
靶向翻译后修饰
unmodified
基因信息
mouse  ...  Cflar(12633)   
一般描述
In human Viral FLICE-inhibitory proteins (v-FLIPs) is identified as c-FLIP. It is composed of two death effector domains which have structural resemblance with the N-terminal half of caspase-8 and a caspase-like domain. It exist as multiple splice variants: FLIP α, β, γ, δ. Along with splice variants, it has two endogenous forms of the protein c-FLIPlong and c-FLIPshort.
免疫原
synthetic peptide corresponding to amino acids 449-465 of the C-terminal region of mouse FLIPL.
应用
Anti-FLIPL C-Terminal antibody is suitable for western blot at 1-2 μg/mL. Antibody can also be used for immunocytochemistry starting at 5 μg/mL. 
生化/生理作用
C-FLIP plays an important role in apoptosis signaling pathways. It acts as proapoptotic molecule or as an anti-apoptotic molecule. It has been reported that c-FLIP can interact with both FADD and caspase-8. It prevents caspase-8 recruitment and processing through DED-DED (death effector domain) interaction followed by CD95-induced apoptosis.
The antibody does not react with short form, FLIPS.
外形
Solution in 0.01 M phosphate buffered saline containing 0.02% sodium azide.
免责声明
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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储存分类代码
10 - Combustible liquids
法规信息
新产品
此项目有
M Thome et al.
Nature, 386(6624), 517-521 (1997-04-03)
Viruses have evolved many distinct strategies to avoid the host's apoptotic response. Here we describe a new family of viral inhibitors (v-FLIPs) which interfere with apoptosis signalled through death receptors and which are present in several gamma-herpesviruses (including Kaposi's-sarcoma-associated human
D K Han et al.
Proceedings of the National Academy of Sciences of the United States of America, 94(21), 11333-11338 (1997-10-23)
Activation of the cascade of proteolytic caspases has been identified as the final common pathway of apoptosis in diverse biological systems. We have isolated a gene, termed MRIT, that possesses overall sequence homology to FLICE (MACH), a large prodomain caspase
H B Shu et al.
Immunity, 6(6), 751-763 (1997-06-01)
Caspases are cysteine proteases that play a central role in apoptosis. Caspase-8 may be the first enzyme of the proteolytic cascade activated by the Fas ligand and tumor necrosis factor (TNF). Caspase-8 is recruited to Fas and TNF receptor-1 (TNF-R1)
Y V Goltsev et al.
The Journal of biological chemistry, 272(32), 19641-19644 (1997-08-08)
CASP-8 and CASP-10, members of a cysteine protease family that participates in apoptosis, interact with MORT1/FADD, an adapter protein in the CD120a (p55 tumor necrosis factor receptor), and CD95 (Fas/Apo-1) death-inducing signaling pathways, through a shared N-terminal sequence motif, the
D M Rasper et al.
Cell death and differentiation, 5(4), 271-288 (1999-04-14)
Apoptotic cell suicide initiated by ligation of CD95 (Fas/APO-1) occurs through recruitment, oligomerization and autocatalytic activation of the cysteine protease, caspase-8 (MACH, FLICE, Mch5). An endogenous mammalian regulator of this process, named Usurpin, has been identified (aliases for Usurpin include
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