C9616
Anti-Cytochrome c antibody produced in sheep
~0.5 mg/mL, affinity isolated antibody, buffered aqueous solution
别名:
Anti-CYC
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关于此项目
UNSPSC Code:
12352203
MDL number:
Conjugate:
unconjugated
Clone:
polyclonal
Application:
IF, IHC (p), WB
Citations:
10
biological source
sheep
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen 15 kDa
species reactivity
rabbit, rat, human, canine
concentration
~0.5 mg/mL
technique(s)
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 20-40 μg/mL using human heart tissue, indirect immunofluorescence: 5-10 μg/mL using human MCF-7 cells, western blot: 0.1-0.2 μg/mL using whole extracts of MCF−7, Jurkat, Rat−1, MDCK cells and extract of rat kidney or rat heart
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... CYCS(54205)
rat ... Cycs(25309)
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General description
Anti-Cytochrome c produced in sheep using purified rabbit cytochrome c conjugated to keyhole limpet hemocyanin (KLH).
Cytochrome c is an electron transport protein released from mitochondria as an early committed event in apoptosis. Cytochrome c and dATP are cofactors for the mammalian apoptosome, which is composed of Apaf-1, Bcl-2, and procaspase 9. When caspase 9 is activated, activation of other caspases follow including the death protease caspase 3. The release of cytochrome c is inhibited by the presence of Bcl-2 on these organelles preventing the initiation of apoptosis. In cells induced by several apoptotic agents (such as UV irradiation, staurosporine, and overexpression of Bax), caspase inhibitors do not prevent cytochrome c release.
Immunogen
rabbit cytochrome c.
Application
Anti-Cytochrome c antibody produced in sheep has been used in:
- immunocytochemistry
- immunostaining
- immunoblotting
- immunohistochemistry
Biochem/physiol Actions
Cytochrome c controls cellular electron transport and energy metabolism. It is involved in the transfer of electrons between complex III and complex IV in the mitochondrial electron transport chain. It is involved in apoptosis and activates the death protease caspase-3 (CCP32). The presence of Bcl-2 on the organelles inhibits the release of cytochrome c from mitochondria during apoptosis. Along with Apaf-1, and procaspase-9, it forms an essential component of vertebrate ”apoptosome”. Activation of caspase-9 and other capsases directs apoptosis. Serum cytochrome c is a sensitive apoptotic marker in vivo, and increased serum cytochrome c level can serve as a negative prognostic marker.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% BSA and 15 mM 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.
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存储类别
12 - Non Combustible Liquids
wgk
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
常规特殊物品
此项目有
Differential control of growth, apoptotic activity and gene expression in human colon cancer cells by extracts derived from medicinal herbs, Rhazya stricta and Zingiber officinale and their combination
Elkady AI, et al.
World Journal of Gastroenterology, 20(41), 15275-15275 (2014)
Katarzyna Barczyk et al.
International journal of cancer, 116(2), 167-173 (2005-04-01)
Despite significant progress in cancer therapy, the outcome of the treatment is often unfavorable. Better treatment monitoring would not only allow an individual more effective, patient-adjusted therapy, but also it would eliminate some of the side effects. Using a cytochrome
R M Kluck et al.
Science (New York, N.Y.), 275(5303), 1132-1136 (1997-02-21)
In a cell-free apoptosis system, mitochondria spontaneously released cytochrome c, which activated DEVD-specific caspases, leading to fodrin cleavage and apoptotic nuclear morphology. Bcl-2 acted in situ on mitochondria to prevent the release of cytochrome c and thus caspase activation. During
Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism.
P MITCHELL
Nature, 191, 144-148 (1961-07-08)
P Li et al.
Cell, 91(4), 479-489 (1997-12-09)
We report here the purification of the third protein factor, Apaf-3, that participates in caspase-3 activation in vitro. Apaf-3 was identified as a member of the caspase family, caspase-9. Caspase-9 and Apaf-1 bind to each other via their respective NH2-terminal
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