FFPE-FASP™ Protein Digestion Kit

De-paraffinization and Uncrosslinking. Unbiased Extraction and Complete Solubilization. Same-As-Fresh Quantification.

FFPE Tissue Proteomics with FASP

Filter-Aided Sample Prep (FASP) is the enabling technology behind quantitative mass spectrometry analysis of archived tissues. Based on a spin-filter sample preparation method initially described by Manza, et al., and developed further and extended to FFPE tissue processing by Ostasiewicz, et al., this method features unbiased extraction, complete proteome solubilization, and highly efficient digestion. The resulting filtrate is free of detergents, large molecules, and other substances that would interfere with mass spectrometry analysis of the proteome.

Same-as-Fresh Quantification

FFPE tissue proteomes can now be quantified and analyzed by mass spectrometry. An extensive, quantitative mass spectrometry comparison study described by Ostasiewicz, et al. found no significant differences between the proteomes of fresh and FFPE tissue samples processed using FFPE-FASP. Proteins, peptides, and post-translational modifications were quantitatively preserved. Results were unaffected by hematoxylin staining, laser capture microdissection, or tissue storage time.

Our Offer

The FFPE-FASP Protein Digest Kit is now available at the introductory price of just $49 and contains the protocols and FASP materials you need to de-paraffinize, un-crosslink, extract, reduce, solubilize, acetylate, clean up, digest, and filter-purify the resulting peptides from eight FFPE archive tissue samples.

Your purchase also comes with our 30-day money-back guarantee. If youre dissatisfied with the FFPE-FASP Protein Digestion Kit for any reason, just send any unused materials back to us and we’ll refund your money promptly.

REFERENCES

Sample preparation and digestion for proteomic analyses using spin filters. Manza LL, Stamer SL, Ham AJ, Codreanu SG, Liebler DC. Proteomics. 2005 May ; 5(7): 1742-5

Proteome, phosphoproteome, and N-glycoproteome are quantitatively preserved in formalin-fixed paraffin-embedded tissue and analyzable by high-resolution mass spectrometry. Ostasiewicz P, Zielinska DF, Mann M, Wisniewski JR. J Proteome Res. 2010 Jul 2; 9(7): 3688-700