Technical Data
C7506-15A
Cofilin
Description:
Cofilin is a small phosphoinositide-sensitive, actin-binding protein capable of depolymerizing actin filaments in vitro. Under certain conditions, it fragments the filaments and accelerates actin subunit dissociation from their

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

Recommended Dilution:
Western Blot: 1:1000. Detects a band at approximately 19kDa. Use whole extracts of human A-431 epidermoid carcinoma, rat PC-12 pheochromocytoma, and dog MDCK kidney cells, or purified recombinant chicken muscle cofilin.
Immunofluorescence: 1:1000 using NIH-NT3 fibroblasts
Optimal dilutions to be determined by the researcher.

Cellular Localization: Cytoplasmic and Nuclear

Storage and Stability:
May be stored at 4C for short-term only. For long-term storage and to avoid repeated freezing and thawing, aliquot and store at -20C. Aliquots are stable for at least 12 months at -20C. 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
PabIgGPurified
SizeStorageShippingSourceHost
50ul-20CBlue IceHumanRabbit
Concentration:
Not determined
Immunogen:
Synthetic peptide corresponding to amino acids 154-166 of human cofilin with N-terminal cysteine added, conjugated to maleimide-activated keyhole limpet hemocyanin (KLH). The corresponding immunizing sequence is identical in pig and rat non-muscle cofilin
Purity:
Purified
Form
Supplied as a liquid in PBS, pH 7.4, containing sodium azide
Specificity:
Recognizes human Cofilin. Species Crossreactivity: mouse, rat, chicken, canine and porcine.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Nishida, E., et al., Biochemistry, 23, 5307-5316 (1984).
2. Nishida, E., et al., Proc. Natl. Acad. Sci. (USA), 84, 5262-5266 (1987).
3. Moriyama, K., and Yahara, I., EMBO J., 18, 6752-6761 (1999).
4. Bamburg, R., Annu. Rev. Cell. Dev. Biol., 15, 185-230 (1999).
5. Carlier, M.F., et al., J. Cell Biol., 136, 1307-1322 (1997).
6. Maciver, S.K., et al., J. Cell. Biol., 278, 1611-1620 (1991).
7. Ohta, Y., et al., J. Biol. Chem., 264, 16143-16148 (1989).
8. Suzuki, K.T., et al., J. Biol. Chem., 270, 19551-19556 (1997).
9. Minamide, A., et al., Nature Cell Biol., 2, 628-636 (2000).
10. Arber, S., et al., Nature, 393, 805-809 (1998).