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anti-FLIP (human), mAb (NF6)

AG-20B-0056-C050 50 µg $260.00
AG-20B-0056-C100 100 µg $390.00
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Additional Information

Product Data
Synonyms I-FLICE; CLARP; CASPER; Usurpin, CASH; FLAME-1
Properties
Clone NF6
Isotype Mouse IgG1
Immunogen/Antigen Recombinant human FLIP (aa 1-480).
Application Immunocytochemistry
Immunohistochemistry (paraffin sections)
Western Blot
Crossreactivity Human
Specificity Recognizes short (FLIPS) and long (FLIPL) splice variants of human FLIP.
Concentration 1 mg/ml
Formulation Liquid. In PBS containing 10% glycerol and 0.02% sodium azide.
Product Type Monoclonal Antibody
Shipping and Handling
Shipping BLUE ICE
Short Term Storage +4°C
Long Term Storage -20°C
Handling Advice Avoid freeze/thaw cycles.
Use/Stability Stable for at least 1 year after receipt when stored at -20°C.
Documents
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Product Description

FLIP is an apoptosis regulator protein which functions as a crucial link between cell survival and cell death pathways in mammalian cells and acts as an inhibitor of TNFRSF6 mediated apoptosis. A proteolytic fragment (p43) is likely retained in the death-inducing signaling complex (DISC) thereby blocking further recruitment and processing of caspase-8 at the complex. Full length and shorter isoforms have been shown either to induce apoptosis or to reduce TNFRSF-triggered apoptosis. FLIP lacks enzymatic (caspase) activity. FLIP is highly expressed in skeletal muscle, pancreas, heart, kidney, placenta and peripheral blood leukocytes.

Product References

  1. The role of c-FLIP in modulation of CD95-induced apoptosis: S. Scaffidi, et al.; J. Biol. Chem. 274, 1541 (1999)
  2. An inducible pathway for degradation of FLIP protein sensitizes tumor cells to TRAIL-induced apoptosis: Y. Kim, et al.; J. Biol. Chem. 277, 22320 (2002)
  3. Caspase-10 is recruited to and activated at the native TRAIL and CD95 death-inducing signalling complexes in a FADD-dependent manner but can not functionally substitute caspase-8: M.R. Sprick, et al.; EMBO J. 21, 4520 (2002)
  4. Enhancement of Apo2L/TRAIL (tumor necrosis factor-related apoptosis-inducing ligand)-induced apoptosis in non-small cell lung cancer cell lines by chemotherapeutic agents without correlation to the expression level of cellular protease: S. Frese, et al.; J. Thorac. Cardiovasc. Surg. 123, 168 (2002)
  5. Lack of Proapoptotic Activity of Soluble CD95 Ligand Is Due to Its Failure to Induce CD95 Oligomers: S. Jang, et al.; J. Int. Cyt. Res. 23, 441 (2003)
  6. Proteasome inhibition results in TRAIL sensitization of primary keratinocytes by removing the resistance-mediating block of effector caspase maturation: M. Leverkus, et al.; Mol. Cell. Biol. 23, 777 (2003)
  7. Suramin inhibits death receptor-induced apoptosis in vitro and fulminant apoptotic liver damage in mice: S.T. Eichhorst, et al.; Nature Med. 10, 602 (2004)
  8. The c-FLIP-NH2 terminus (p22-FLIP) induces NF-kappaB activation: A. Golks, et al.; J. Exp. Med. 203, 1295 (2006)
  9. Caspase-2 is activated at the CD95 death-inducing signaling complex in the course of CD95-induced apoptosis: I.N. Lavrik, et al.; Blood 108, 559 (2006)
  10. The role of CAP3 in CD95 signaling: new insights into the mechanism of procaspase-8 activation: A. Golks, et al.; Cell Death Diff. 13, 489 (2006)
  11. Expression of c-FLIP is primarily detected in diffuse large B-cell lymphoma and Hodgkin's lymphoma and correlates with lack of caspase 8 activation: I.S. van Houdt, et al.; Histopathology 51, 778 (2007)
  12. CD95 Stimulation Results in the Formation of a Novel Death Effector Domain Protein-containing Complex: I.N. Lavrik, et al.; J. Biol. Chem. 283, 26401 (2008)
  13. A New C-terminal Cleavage Product of Procaspase-8, p30, Defines an Alternative Pathway of Procaspase-8 Activation: J.C. Hoffmann, et al.; Mol. Cell Biol. 29, 4431 (2009)
  14. Stoichiometry of the CD95 Death-Inducing Signaling Complex: Experimental and Modeling Evidence for a Death Effector Domain Chain Model: K. Schleich, et al.; Mol. Cell 47, 1 (2012)
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