There are 9+ publications for this product available. The Mouse Monoclonal anti-FLIP antibody is suitable to detect FLIP in samples from Human. It has been validated for WB, IHC and ICC.
Optimal working dilution should be determined by the investigator.
Restrictions
For Research Use only
Format
Liquid
Concentration
Lot specific
Buffer
In PBS containing 10 % glycerol and 0.02 % 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
4 °C,-20 °C
Storage Comment
Short Term Storage: +4°C Long Term Storage: -20°C Stable for at least 1 year after receipt when stored at -20°C.
Expiry Date
12 months
Hartwig, Montinaro, von Karstedt, Sevko, Surinova, Chakravarthy, Taraborrelli, Draber, Lafont, Arce Vargas, El-Bahrawy, Quezada, Walczak: "The TRAIL-Induced Cancer Secretome Promotes a Tumor-Supportive Immune Microenvironment via CCR2." in: Molecular cell, Vol. 65, Issue 4, pp. 730-742.e5, (2017) (PubMed).
Golks, Brenner, Krammer, Lavrik: "The c-FLIP-NH2 terminus (p22-FLIP) induces NF-kappaB activation." in: The Journal of experimental medicine, Vol. 203, Issue 5, pp. 1295-305, (2006) (PubMed).
Eichhorst, Krueger, Müerköster, Fas, Golks, Gruetzner, Schubert, Opelz, Bilzer, Gerbes, Krammer: "Suramin inhibits death receptor-induced apoptosis in vitro and fulminant apoptotic liver damage in mice." in: Nature medicine, Vol. 10, Issue 6, pp. 602-9, (2004) (PubMed).
Jang, Krammer, Salgame: "Lack of proapoptotic activity of soluble CD95 ligand is due to its failure to induce CD95 oligomers." in: Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research, Vol. 23, Issue 8, pp. 441-7, (2003) (PubMed).
Leverkus, Sprick, Wachter, Mengling, Baumann, Serfling, Bröcker, Goebeler, Neumann, Walczak: "Proteasome inhibition results in TRAIL sensitization of primary keratinocytes by removing the resistance-mediating block of effector caspase maturation." in: Molecular and cellular biology, Vol. 23, Issue 3, pp. 777-90, (2003) (PubMed).
Kim, Suh, Sporn, Reed: "An inducible pathway for degradation of FLIP protein sensitizes tumor cells to TRAIL-induced apoptosis." in: The Journal of biological chemistry, Vol. 277, Issue 25, pp. 22320-9, (2002) (PubMed).
Frese, Brunner, Gugger, Uduehi, Schmid et al.: "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 ..." in: The Journal of thoracic and cardiovascular surgery, Vol. 123, Issue 1, pp. 168-74, (2002) (PubMed).
Sprick, Rieser, Stahl, Grosse-Wilde, Weigand, Walczak: "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." in: The EMBO journal, Vol. 21, Issue 17, pp. 4520-30, (2002) (PubMed).
Scaffidi, Schmitz, Krammer, Peter: "The role of c-FLIP in modulation of CD95-induced apoptosis." in: The Journal of biological chemistry, Vol. 274, Issue 3, pp. 1541-8, (1999) (PubMed).
Target
FLIP (CFLAR)
(CASP8 and FADD-Like Apoptosis Regulator (CFLAR))
Alternative Name
FLIP
Background
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.