Technical Data
F4568
Flotillin 1 (Reggie 2)
Description:
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).

Applications:
Suitable for use in Western Blot. Other applications not tested.

Recommended Dilution:
Western Blot: 1:500
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4°C for short-term only. For long-term storage, aliquot and store at -20°C. Aliquots are stable for at least 12 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
TypeIsotypeCloneGrade
MabIgG6k179Supernatant
SizeStorageShippingSourceHost
100ul 4°C (-20°C Glycerol)Blue IceHumanRabbit
Concentration:
As reported
Immunogen:
A synthetic peptide corresponding to residues in human Flotillin-1.
Purity:
Supernatant
Form
Supplied as a liquid in 50mM Tris-Glycine, pH 7.4, 0.15M sodium chloride, 0.01% sodium azide, 0.05% BSA, 40% glycerol.
Specificity:
Recognizes human Flotillin-1. Species Crossreactivity: Mouse
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1.Tavernarakis, N., Driscoll, M., and Kyrpides, N. C. (1999) Trends Biochem. Sci. 24, 425–427 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