Technical Data

F4550-01-APC
Clone Type
Polyclonal
Host
Rabbit
Source
Human
Conjugate
APC
Isotype
IgG
Grade
Affinity Purified
Applications
FLISA WB
Crossreactivity
Hu Mo Rt
Gene ID
8837
Shipping Temp
Blue Ice
Storage Temp
4°C Do Not Freeze
Notes
Preservative Free
BSA Free
Rabbit Anti-FLIP, CT (FLICE Inhibitory Protein) (APC)

FLICE-inhibitory proteins (FLIP) are widely expressed apoptosis regulator proteins. FLIPs may function as a crucial link between cell survival and cell death pathways in mammalian cells. At least 14 isoforms of FLIP have been defined arising from alternative splicing. The long form FLIP-L contains a domain similar to those found in caspases.

FLIP was cloned independently in a number of laboratories and is also known as Casper, I-FLICE, FLAME-1, CASH and CLARP. FLIP has two death effector domains (DEDs) and a caspase-like domain. It interacts with FADD and caspase-8 and -10, potently inhibiting apoptosis by all known death receptors. FLIP exists in a short form (FLIPS) and a long form (FLIPL).
Applications
Suitable for use in FLISA and Western Blot. Other applications not tested.
Recommended Dilution
Optimal dilutions to be determined by the researcher.
Storage and Stability
Store product at 4°C in the dark. DO NOT FREEZE! Stable at 4°C for 12 months after receipt as an undiluted liquid. Dilute required amount only prior to immediate use. Further dilutions can be made in assay buffer. Caution: APC conjugates are sensitive to light. For maximum recovery of product, centrifuge the original vial prior to removing the cap.
Note: Applications are based on unconjugated antibody.
Immunogen
Peptide corresponding to the C-terminus of human FLIP-L. Epitope: last 50aa
Form
Supplied as a liquid in PBS, pH 7.2. Labeled with Allophycocyanin (APC).
Purity
Purified by immunoaffinity chromatography.
Specificity
Recognizes human FLIP. Recognizes FLIPa only. Species Crossreactivity: mouse and rat

Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.

References
1. Thome M, Schneider P, Hofmann K, Fickenscher H, Meinl E, Neipel F, Mattmann C, Burns K, Bodmer JL, Schroter M, Scaffidi C, Krammer PH, Peter ME, Tschopp J. Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors. Nature 1997;386:517-521|2. Irmler M, Thome M, Hahne M, Schneider P, Hofmann K, Steiner V, Bodmer JL, Schroter M, Burns K, Mattmann C, Rimoldi D, French LE, Tschopp J. Inhibition of death receptor signals by cellular FLIP. Nature 1997;388:190-195 |3. Shu HB, Halpin DR, Goeddel DV. Casper is a FADD- and caspase-related inducer of apoptosis. Immunity 1997;6:751-763 |4. Hu S, Vincenz C, Ni J, Gentz R, Dixit VM. I-FLICE, a novel inhibitor of tumor necrosis factor receptor-1- and CD-95-induced apoptosis. J Biol Chem 1997;272:17255-17257 |5. Srinivasula SM, Ahmad M, Ottilie S, Bullrich F, Banks S, Wang Y, Fernandes-Alnemri T, Croce CM, Litwack G, Tomaselli KJ, Armstrong RC, Alnemri ES. FLAME-1, a novel FADD-like anti-apoptotic molecule that regulates Fas/TNFR1-induced apoptosis. J Biol Chem 1997;272:18542-18545 |6. Goltsev YV, Kovalenko AV, Arnold E, Varfolomeev EE, Brodianskii VM, Wallach D. CASH, a novel caspase homologue with death effector domains. J Biol Chem 1997;272:19641-19644 |7. Inohara N, Koseki T, Hu Y, Chen S, Nunez G. CLARP, a death effector domain-containing protein interacts with caspase-8 and regulates apoptosis. Proc Natl Acad Sci USA 1997;94:10717-10722 |8. Wallach D. Apoptosis. Placing death under control. Nature 1997;388:123
USBio References
No references available
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