Technical Data
Filamin functions as a crosslinking protein forming a flexible link between two actin filaments. It is composed of two identical polypeptide chains each joined to the other at one end, with an actin binding site at the other. It is present in human platelets, lymphocytes, fibroblasts and smooth muscle actin.

Suitable for use in Western Blot, Immunoprecipitation, Immunohistochemistry and Immunofluorescence. Other applications have not been tested.

Recommended Dilution:
Western Blot: 1:250-1:1000
Immunoprecipitation: Suggested lysis buffer is PBS with 0.5% triton X-100 with proteinase inhibitors (note for full length filamin include calpain inhibitors). 5ul of antibody for
every 300-500ul of cell lysate (200-500ug/ml total protein is suggested. Incubation is 1hour at RT or overnight at 4șC; Protein A/G agarose beads or rabbit anti-mouse secondary capture antibody is recommended for best recovery. 4-10% acrylamide gels are recommended for full length filamin or the 80kD fragment visualization.
Immunofluorescence (ABC):1:50-1:200
Immunohistochemistry (paraffin): (lower dilutions) High temperature citrate buffer antigen retrieval technique recommended.
Optimal dilution determined by the researcher.

Recommended Positive Control Tissue:
Human or bovine skin

Storage and Stability:
May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
100ul-20°CBlue IceHumanMouse
Not determined
Human platelet protein
Supplied as a liquid. No preservatives added.
Recognizes unprocessed, full length human filamin (actin-binding protien, 270-280kD) as well as the 90kD C-term calpain cleavage fragment of filamin. Species Crossreactivity: bovine. Does not react with mouse or rat.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. J. Cellular Biochemistry (1996) 62: 383-396. 2. Free Rad. Bio. & Med. (1997) 22: 955-966. 3. Thromb Haemost. (1992). 3(67): 252-257. 4. Van der Ven, P., et al., J. Cell Biology (2000) 151: 235-247.