Technical Data
Dystrophin, Rod Domain
Dystrophin is a member of the spectrin/alpha-actinin family of actin-binding, triple helix rod-containing proteins. It is absent or greatly reduced in individuals with the X-linked recessive Duchenne’s muscular dystrophy disorder, as well as in mice with the mdx (murine muscular dystrophy) mutation.

Suitable for use in Western Blot, Immunohistochemistry and EM Gold. Other applications not tested.

Recommended Dilution:
Western Blot: 1:100-1:250
Immunohistochemistry(Fresh frozen, unfixed tissue): Neat 1:20
Not recommended for use on paraffin embedded tissue.
EM Gold: Undiluted 90 minute incubation at 25°C. Light fixation with 2% formaldehyde + 0.001% glutaraldehyde for 1 hour. Use 2.3M sucrose as cryoprotectant.
Optimal dilutions to be determined by the researcher.

Expected Staining Pattern:
Light microscopy: Continuous rim of labeling at the periphery of muscle fibers
Western Blot: Strong double bands at ~400kD and metabolites of lower molecular mass
E.M. Gold: Close to the cytoplasmic face of the plasma membrane.

Positive Control:
Snap frozen normal human or rat striated muscle.

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 after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
1ml-20°CBlue IceHumanMouse
Not Determined
Bacterial fusion protein
Supplied as a liquid in PBS, 1% BSA, 15mM sodium azide.
Recognizes mid rod domain of human dystrophin between aa1181-1388. Reacts with skeletal, cardiac and smooth muscle dystrophin. Reacts on blots with the brain isoform. No reactivity with mdx mouse tissue or DMD/BMD patients who have a gene deletion. Does not react with chicken dystrophin. Species Crossreactivity: mouse, rat, rabbit and canine
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Cullen, M.J. et al., Proceedings of the Royal Society (1990) 240:197–210. 2. England, S.B., et al., Nature (1990) 324:180–182. 3. Nicholson, L.V.B., et al., Journal of Neurological Sciences (1989) 94:125–136. 4. Nicholson, L.V.B., et al., Journal of Neurological Sciences (1989) 94:137–146. 5. Nicholson, L.V.B., et al., Acta Neuropathologica (1990) 80:239–250. 6. Nordenskjold, M., et al., Human Genetics (1990) 84:207–209. 7. Norman, A.M., et al., Archives of Disease in Childhood (1989) 64:1501–1503. 8. Nicholson, L.V.B. et al., Acta. Neurol. Scand.(1992) 86:8–14. 9. Voit, T. et al., Neuropediatrics (1991) 22:152–162. 10. Slater, C.R., et al. Journal of Neurological Sciences (1991) 101:187–192.