Protein Separation using various techniques


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If Protein A=50KDa & pI =3.5
Protein B=50KDa & pI=7.5
Protein C=25KDa & pI=5.5
Protein D=40KDa & pI=5.5
How will be the banding pattern of these proteins
1.Considering mass how it separates on SDS PAGE?
2.Considering only mass how it separates on NATIVE PAGE?
3.Considering both mass & charge how it separates NATIVE PAGE (Acidic & Basic gel)?
4.Considering pI how these separates on Isoelectric focusing ?

Finally which techniques better suites to separate all the above proteins without any of the proteins?