C7852
Anti-CAD antibody produced in rabbit
affinity isolated antibody, buffered aqueous solution
Synonym(s):
Anti-Caspase Activated DNase I, Anti-DFF40, Anti-DNA Fragmented Factor 40
Sign Into View Organizational & Contract Pricing
All Photos(1)
About This Item
MDL number:
UNSPSC Code:
12352203
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen 40 kDa
species reactivity
mouse
technique(s)
western blot: 1 μg/mL using mouse lung tissue lysate
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
Gene Information
mouse ... Dffb(13368)
General description
Caspase Activated DNase is a heterodimeric protein composed of ICAD and CAD (in human known as DFF45 and DFF40, respectively) two subunits, which triggers DNA fragmentation during apoptosis.
Immunogen
synthetic peptide corresponding to amino acids 205-222 of mouse CAD (cell death-inducing DFF-like effector A).
Application
Anti-CAD antibody was used for western blotting in a study of simultaneous downregulation of uPAR (urokinase-type plasminogen activator receptor] and Cathepsin B induces the up-regulation of pro-apoptotic genes.
Biochem/physiol Actions
In inactive state DFF exists as a cytoplasmic protein. After activated by apoptotic signals DFF45 functions as a chaperone, mediating the correct folding of DFF40, as well as an inhibitor of DFF40. In response to apoptotic signals, DFF45 is cleaved by caspase-3 at two sites; which results releasing of active nuclease, DFF40. Furthermore, DFF40 oligomerize to form a large, functional complex which further breaks down DNA by introducing double-strand breaks. However, DFF40 interact directly with histone H1 which may stimulate its activity.
Physical form
Solution in phosphate buffered saline, containing 0.02% sodium azide.
Disclaimer
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.
Not finding the right product?
Try our Product Selector Tool.
Choose from one of the most recent versions:
Certificates of Analysis (COA)
Lot/Batch Number
Don't see the Right Version?
If you require a particular version, you can look up a specific certificate by the Lot or Batch number.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Ke Mao et al.
Oncology letters, 13(2), 893-897 (2017-03-31)
Glioma is an aggressive form of brain cancer that occurs following the abnormal proliferation of glial cells. Although glioma cannot spread to other organs, the morbidity and mortality rates of the disease are high, even following surgery, radiotherapy and chemotherapy.
Christopher S Gondi et al.
Molecular cancer therapeutics, 5(12), 3197-3208 (2006-12-19)
The invasive character of gliomas depends on proteolytic cleavage of the surrounding extracellular matrix. Cathepsin B and urokinase-type plasminogen activator receptor (uPAR) together are known to be overexpressed in gliomas and, as such, are attractive targets for gene therapy. In
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
Active Filters
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service
