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Second Mitochondria-Derived Activator of Caspase (DIABLO) (AA 125-239) antibody

Details for Product No. ABIN968785, Supplier: Log in to see
Antigen
  • smac
  • smac3
  • diablo-s
  • 0610041G12Rik
  • 1700006L01Rik
  • AU040403
  • Smac
  • DFNA64
  • SMAC
  • DBO
  • XSmac
Alternatives
anti-Human Second Mitochondria-Derived Activator of Caspase antibody for Western Blotting
Epitope
AA 125-239
32
16
13
11
7
5
4
4
4
3
3
2
2
2
2
1
1
1
Reactivity
Dog (Canine), Human, Rat (Rattus)
134
55
34
4
3
3
2
1
1
Host
Mouse
115
28
8
1
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
1
1
1
Application
Immunofluorescence (IF), Western Blotting (WB)
139
57
56
32
21
9
8
6
4
3
2
2
2
2
1
1
1
1
Supplier
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Immunogen Human Smac/DIABLO aa. 125-239
Clone 56-Smac-DIABLO
Isotype IgG2b
Cross-Reactivity Rat (Rattus), Dog (Canine)
Characteristics 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
Purification The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.
Alternative Name Smac/DIABLO (DIABLO Antibody Abstract)
Background Apoptosis is a genetically programmed, selective process of cell death that occurs during normal cell differentiation and development of multicellular organisms. Inhibitors of apoptosis proteins (IAPs), hILP/XIAP, c-IAP1, c-IAP2, and survivin, suppress apoptosis by preventing procaspase activation and inhibiting mature caspase activity. Smac/DIABLO (second mitochondria-derived activator of caspases) eliminates the inhibitory effect of many IAPs, and has been shown to interact with hILP, c-IAP1, c-IAP2, and survivin. The interaction with hILP occurs through Smac/DIABLO binding to the second and third BIR domains of hILP. Smac/DIABLO protein contains an N-terminal mitochondria targeting sequence (MTS) and a procaspase-3 activation domain. The N-terminal MTS is cleaved after import into the mitochondria, and the activity of the mature Smac/DIABLO is dependent on homodimerization and release from the mitochondria. Overexpression of Smac/DIABLO in HeLa cells increases the sensitivity to UV-mediated apoptosis. Thus, Smac/DIABLO acts as an apoptotic activator through its binding to IAPs and activation of caspases.
Molecular Weight 22 kDa
Research Area Apoptosis/Necrosis
Pathways Apoptosis, Caspase Cascade in Apoptosis
Comment

Related Products: ABIN968535, ABIN967389

Restrictions For Research Use only
Format Liquid
Concentration 250 μg/mL
Buffer Aqueous buffered solution containing BSA, glycerol, and ≤0.09 % sodium azide.
Preservative Sodium azide
Precaution of Use This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Storage Comment Store undiluted at -20°C.
Supplier Images
Western Blotting (WB) image for anti-Second Mitochondria-Derived Activator of Caspase (DIABLO) (AA 125-239) antibody (ABIN968785) Western blot analysis of Smac/DIABLO on a HeLa cell lysate (Human cervical epitheloid...
Product cited in: Kim, Broxmeyer: "Therapeutic potential of 4-1BB (CD137) as a regulator for effector CD8(+) T cells." in: Journal of hematotherapy & stem cell research, Vol. 10, Issue 4, pp. 441-9, 2001 (PubMed).

Chai, Du, Wu et al.: "Structural and biochemical basis of apoptotic activation by Smac/DIABLO." in: Nature, Vol. 406, Issue 6798, pp. 855-62, 2000 (PubMed).

Du, Fang, Li et al.: "Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition." in: Cell, Vol. 102, Issue 1, pp. 33-42, 2000 (PubMed).

Ikuta, Weissman: "Evidence that hematopoietic stem cells express mouse c-kit but do not depend on steel factor for their generation." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 89, Issue 4, pp. 1502-6, 1992 (PubMed).