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Merck
CN

D3438

Sigma-Aldrich

Anti-DFF45, N-Terminal antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

别名:

Anti-ICAD

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关于此项目

MDL编号:
UNSPSC代码:
12352203
NACRES:
NA.41
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生物来源

rabbit

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 45 kDa (non-apoptotic cells)

种属反应性

human

技术

western blot: 0.5 μg/mL using human HeLa cell extract

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

human ... DFFA(1676)

一般描述

DFF exists as an inactive cytoplasmic protein until activated by apoptotic signals. DFF40, the nuclease responsible for DNA fragmentation during apoptosis, exists as a heterodimeric complex with DFF45.

免疫原

synthetic peptide corresponding to amino acids 2-21 of the N-terminal region of human DFF45/ICAD (DNA Fragmentation Factor 45/Inhibitor of Caspase-3 Activated DNase I).

应用

Anti-DFF45 antibody produced in rabbit is suitable for immunoblotting at a working concentration of 0.5μg/mL using a total HeLa cell lysate.

生化/生理作用

DFF45 functions as both a chaperone, mediating the correct folding of DFF40, and an inhibitor of DFF40. DFF45 is cleaved by caspase-3 at two sites in response to apoptotic signals. This releases DFF40, the active nuclease. DFF40 seems to oligomerize, forming a large, functional complex which breaks down DNA by introducing double strand breaks. Also, DFF40 appears to interact directly with histone H1 that may stimulate its activity.

外形

Solution in phosphate buffered saline containing 0.02% sodium azide.

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B B Wolf et al.
The Journal of biological chemistry, 274(43), 30651-30656 (1999-10-16)
Caspase-3 initiates apoptotic DNA fragmentation by proteolytically inactivating DFF45 (DNA fragmentation factor-45)/ICAD (inhibitor of caspase-activated DNase), which releases active DFF40/CAD (caspase-activated DNase), the inhibitor's associated endonuclease. Here, we examined whether other apoptotic proteinases initiated DNA fragmentation via DFF45/ICAD inactivation. In
D Tang et al.
The Journal of biological chemistry, 273(44), 28549-28552 (1998-10-24)
Apoptosis involves the proteolysis of specific cellular proteins by a group of cysteine proteases known as caspases. Many of these cellular targets are either functionally inactivated (e.g. poly(ADP-ribose) polymerase) or activated (e.g. other caspases, gelsolin) by such processing, thereby facilitating
W Wöhrl et al.
Biochemical and biophysical research communications, 254(3), 552-558 (1999-01-28)
During apoptosis, changes to the nucleus of the dying cell include DNA degradation and structural collapse. These changes are accomplished by caspase-mediated cleavage of DNA-fragmenting factor DFF45, an inhibitor of the effector molecule DFF40. DFF45 and, more efficiently, a mutant
X Liu et al.
The Journal of biological chemistry, 274(20), 13836-13840 (1999-05-13)
DNA fragmentation factor (DFF) is a heterodimeric protein composed of 45-kDa (DFF45) and 40-kDa (DFF40) subunits, a protein that mediates regulated DNA fragmentation and chromatin condensation in response to apoptotic signals. DFF45 is a specific molecular chaperone and an inhibitor
H Sakahira et al.
Nature, 391(6662), 96-99 (1998-01-09)
Various molecules such as cytokines and anticancer drugs, as well as factor deprivation, rapidly induce apoptosis (programmed cell death), which is morphologically characterized by cell shrinkage and the blebbing of plasma membranes and by nuclear condensation. Caspases, particularly caspase 3

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