What is the best way to make your own lysis buffer for protein isolation?

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The best way to make own lysis buffer is to optimize the ingredient concentration to best suit the requirement. 
The best buffer for maintaining the native form of a protein is a non-denaturing buffer. It consists of:

1% Nonidet P-40 (NP-40) or Triton X-100
150 mM NaCl
50mM Tris-HCl (pH 8)
2mM EDTA (Optional)
Proteinase Inhibitor (Phenylmethylsulfonyl fluoride and/or dithiothreitol) 1mM

The best buffer for obtaining denatured protein is SDS lysis buffer. It consists of:

2% SDS
50mM Tris-HCl (pH 8)
10mM EDTA
10% Glycerol
Proteinase Inhibitor (Phenylmethylsulfonyl fluoride and/or dithiothreitol) 1mM

For obtaining sub-cellular proteins (mitochondrial or nuclear proteins), the best buffer would be radioimmunoprecipitation assay (RIPA) buffer. It consists of

150 mM NaCl
1% NP-40 or Triton X-100
50mM Tris-HCl (pH 8.0)
0.1% SDS
0.5% sodium deoxycholate
Proteinase Inhibitor (Phenylmethylsulfonyl fluoride and/or dithiothreitol) 1mM

Possible variations in the buffer constituents include varying detergent concentration, increasing salt concentration, or changing the detergents (such as saponin, CHAPS, digitonin, etc.,) in the protocol

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