I want to quantify a protein of ~ 7 kDa ( not a recombinant or amplified) from the crude protein extract. The sequence of the protein is known and has only one UV absorbing aminoacid.
I agree with Pierre: WB quantification would be the best.
Theoretically, if you were to take similar size protein as a standard, build calibration curve and titrate your lysate (on the same gel), you would be able work out your protein concentration by simple CBB staining.
Additionally, if there is at least one tryptophan, you can try quantification using stain-free gels (BioRad for example) or you can prepare such yourself using trichloroethanol. But here your protein-standard must also have only one W in addition to being similar in size.