anti-FLIP (human) mAb (NF6) (Biotin)
| Code | Size | Price |
|---|
| AG-20B-0056B-C050 | 50 ug | £270.00 |
Quantity:
Prices exclude any Taxes / VAT
Overview
Antibody Clonality: Monoclonal
Regulatory Status: RUO
Target Species: Human
Applications:
- Immunocytochemistry (ICC)
- Immunohistochemistry (IHC)
- Western Blot (WB)
Shipping:
-20°C
Storage:
-20°C
Documents
Further Information
Alternate Names/Synonyms:
I-FLICE; CLARP; CASPER; Usurpin, CASH; FLAME-1
Concentration:
1 mg/ml
EClass:
32160000
Form (Short):
liquid
Formulation:
Liquid. In PBS containing 10% glycerol and 0.02% sodium azide.
Handling Advice:
Avoid freeze/thaw cycles.
Immunogen:
Recombinant human FLIP (aa 1-480).
Labels - Conjugates:
Biotin
Long Description:
Monoclonal Antibody. Recognizes short (FLIPS) and long (FLIPL) splice variants of human FLIP. This antibody recognizes an epitope in the N-terminal DED region (aa1-194). Isotype: Mouse IgG1. Clone: NF6. Applications: ICC, IHC, WB. Liquid. In PBS containing 10% glycerol and 0.02% sodium azide. 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.
NCBI, Uniprot Number:
O15519
Package Type:
Plastic Vial
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.
Specificity:
Recognizes short (FLIPS) and long (FLIPL) splice variants of human FLIP. This antibody recognizes an epitope in the N-terminal DED region (aa1-194).
Transportation:
Non-hazardous
UNSPSC Category:
Primary Antibody Conjugates
UNSPSC Number:
12352203
Use & Stability:
Stable for at least 1 year after receipt when stored at -20°C.
References
The role of c-FLIP in modulation of CD95-induced apoptosis: S. Scaffidi, et al.; J. Biol. Chem. 274, 1541 (1999) | 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) | 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) | 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) | 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) | 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) | 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) | The c-FLIP-NH2 terminus (p22-FLIP) induces NF-kappaB activation: A. Golks, et al.; J. Exp. Med. 203, 1295 (2006) | 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) | 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) | 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) | 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) | 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) | 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)