|Calculated MW||47355 Da|
|Other Names||Flotillin-1, FLOT1|
|Target/Specificity||A synthetic peptide corresponding to residues in human Flotillin-1 was used as immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Flotillin-1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles.|
|Cellular Location||Cell membrane; Peripheral membrane protein. Membrane, caveola; Peripheral membrane protein. Melanosome Endosome. Note=Membrane-associated protein of caveolae. Identified by mass spectrometry in melanosome fractions from stage I to stage IV|
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Provided below are standard protocols that you may find useful for product applications.
Flotillin-1, also known as Reggie-2, belongs to a larger family of proteins that share an evolutionarily conserved stomatin/prohibitin/flotillin/HflK/C (SPFH) domain (1). Flotillin-1 is a lipid raft-associated protein that has been implicated in various cellular processes. Flotillin was first found in cells that lack morphologically definable caveolae, as well as in non-caveolar membranes (2) and was subsequently identified in low density detergent-insoluble complexes of endothelial cells, where they were termed flotillins (3). As well as its postulated role in neuronal regeneration, flotilllin-1 has been implicated in insulin signaling to trigger glucose transporter redistribution in adipocytes (4) Flotillin also associates with phagosomes in macrophages (5).
1. Tavernarakis, N., Driscoll, M., and Kyrpides, N. C. (1999) Trends Biochem. Sci. 24, 425
2. Stuermer, C. A., Lang, D. M., Kirsch, F., Wiechers, M., Deininger, S. O., and Plattner, H. (2001) Mol. Biol. Cell 12, 3031-3045
3. Bickel, P. E., Scherer, P. E., Schnitzer, J. E., Oh, P., Lisanti, M. P., and Lodish, H. F. (1997) J. Biol. Chem. 272, 13793-13802
4. Baumann, C. A., Ribon, V., Kanzaki, M., Thurmond, D. C., Mora, S., Shigematsu, S., Bickel, P. E., Pessin, J. E., and Saltiel, A. R. (2000) Nature 407, 202-207
5. Dermine, J. F., Duclos, S., Garin, J., St-, Louis, F., Rea, S., Parton, R. G., and Desjardins, M. (2001) J. Biol. Chem. 276, 18507-18512
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