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anti-Human DFFB Antibodies:
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Human Polyclonal DFFB Primary Antibody for WB - ABIN967293
Enari, Sakahira, Yokoyama, Okawa, Iwamatsu, Nagata: A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. in Nature 1998
Show all 4 Pubmed References
Human Monoclonal DFFB Primary Antibody for WB - ABIN266063
Yoshida, Urasaki, Waltham, Bergman, Pourquier, Rothwell, Inuzuka, Weinstein, Ueda, Appella, Hickson, Pommier: Human apurinic/apyrimidinic endonuclease (Ape1) and its N-terminal truncated form (AN34) are involved in DNA fragmentation during apoptosis. in The Journal of biological chemistry 2003
Show all 3 Pubmed References
Human Polyclonal DFFB Primary Antibody for WB - ABIN4892030
Yoon, Park, Han, Kang, Kim, Lee, Park, Shin, Kim, Yun, Chwae: Caspase-dependent cell death-associated release of nucleosome and damage-associated molecular patterns. in Cell death & disease 2014
the low expression levels of DFF40/CAD and the absence of DNA laddering as common molecular traits in glioblastoma
Data suggest DFF40 expression in breast cancer cell line is involved in drug sensitivity/resistance to doxorubicin; apoptotic cell death due to doxorubicin (a topoisomerase II (show TOP2 Antibodies) inhibitor) is enhanced by DFF40 overexpression in breast cancer cell line.
Data show that the caspase-activated DNase (CAD) is activated when caspases cleave its endogenous inhibitor ICAD (show DFFA Antibodies), resulting in the characteristic DNA laddering of apoptosis.
Combinatorial use of some sulfonamides such as acetazolamide along with increased expression of DFF40 can potently kill tumor cells via apoptosis.
DFF40/CAD-independent mechanism driving conformational nuclear changes during caspase (show CASP3 Antibodies)-dependent cell death
the highest order of chromatin compaction observed in the later steps of caspase (show CASP3 Antibodies)-dependent apoptosis relies on DFF40/CAD-mediated DNA damage by generating 3'-OH ends in single-strand rather than double-strand DNA nicks/breaks
These results suggest a cooperative activity between CAD (show CAD Antibodies) and DNAS1L3 (show DNASE1L3 Antibodies) to accomplish internucleosomal DNA fragmentation .
Human papillomavirus type 16 E6 protein inhibits DNA fragmentation via interaction with DNA fragmentation factor (show DFFA Antibodies) 40
During apoptotic rearrangement of interchromatin granule clusters, the nuclear matrix (NuMa (show NUMA1 Antibodies) rearrangement) and chromatin are closely associated. This process occurs in defined stages and depends on the activity of protein phosphatases, caspases and CAD (show CAD Antibodies).
the cytosolic levels of DFF40/CAD are determinants in achieving a complete apoptotic phenotype, including oligonucleosomal DNA degradation.
results show that caspase 3 (show CASP3 Antibodies)/CAD (show CAD Antibodies) promotes cell differentiation by directly modifying the DNA/nuclear microenvironment, which enhances the expression of critical regulatory genes
Co-transfection of mouse DFF45 (show DFFA Antibodies)(-/-) fibroblasts with plasmids encoding human DFF40 and DFF45 (show DFFA Antibodies) reversed the apoptosis resistance normally observed in these cells
The thymus of DNase II(-/-)CAD (show CAD Antibodies)(-/-) embryos contained many foci carrying undigested DNA and the cellularity was severely reduced due to a block in T cell development.
Interactions identified here between mouse liver histone H1 (show H1F0 Antibodies) carboxyl-terminal domain and DFF40/CAD target and activate linker DNA cleavage during the terminal stages of apoptosis.
The results suggest that CAD protein (show CAD Antibodies) may be preferentially degraded by the ubiquitin-proteasome system in the absence of its inhibitor (ICAD (show DFFA Antibodies)) to maintain protein quality control.
A los of caspase-activated DNASE enhances tumorigenesis induced by a chemical carcinogen in a model of skin carcinogenesis in mice.
Apoptosis is a cell death process that removes toxic and/or useless cells during mammalian development. The apoptotic process is accompanied by shrinkage and fragmentation of the cells and nuclei and degradation of the chromosomal DNA into nucleosomal units. DNA fragmentation factor (DFF) is a heterodimeric protein of 40-kD (DFFB) and 45-kD (DFFA) subunits. DFFA is the substrate for caspase-3 and triggers DNA fragmentation during apoptosis. DFF becomes activated when DFFA is cleaved by caspase-3. The cleaved fragments of DFFA dissociate from DFFB, the active component of DFF. DFFB has been found to trigger both DNA fragmentation and chromatin condensation during apoptosis. Alternatively spliced transcript variants encoding distinct isoforms have been found for this gene but the biological validity of these variants has not been determined.
DNA fragmentation factor subunit beta
, DNA fragmentation factor, 40 kD, beta polypeptide
, DNA fragmentation factor, 40kDa, beta polypeptide (caspase-activated DNase)
, DNA fragmentation factor 40 kDa subunit
, caspase-activated DNase
, caspase-activated deoxyribonuclease
, caspase-activated nuclease
, DNA fragmentation factor 40 kD beta polypeptide (caspase-activated DNase)
, DNA fragmentation factor, 40 kD, beta polypeptide (caspase-activated DNase)
, DNA fragmentation factor, beta polypeptide (caspase-activated DNase)
, DNA fragmentation factor, beta subunit
, DNA fragmentation factor, 40 kD, beta subunit
, DNase inhibited by DNA fragmentation factor