cOmplete, Mini
Protease Inhibitor Cocktail Tablets supplied in EASYpacks Application Used for the inhibition of serine, cysteine, and metalloproteases in bacterial, mammalian, yeast, and plant cell extracts in small volumes. Benefits Simplify protection. Proteins are protected against a multitude of proteases by simply adding a Complete Tablet to aqueous protein isolation buffer. Use a convenient tablet. Tablets combining different pr…
Protease Inhibitor Cocktail Tablets supplied in EASYpacks
Application
Used for the inhibition of serine, cysteine, and metalloproteases in bacterial, mammalian, yeast, and plant cell extracts in small volumes.
Benefits
- Simplify protection.
Proteins are protected against a multitude of proteases by simply adding a Complete Tablet to aqueous protein isolation buffer. - Use a convenient tablet.
Tablets combining different protease inhibitors, with or without EDTA, are available for either 10 ml or 50 ml of lysate. - Eliminate weighing small amounts.
Sufficient amounts of various inhibitors are conveniently supplied in a tablet form. - Insist on a versatile product.
Proteases are inhibited in extracts from almost any tissue or cell type, including animals, plants, yeast, bacteria, or fungi.
Product Description
Starting concentration: 1 tablet contains protease inhibitors sufficient for a 10-ml cell extract.
Specificity: Mixture of several protease inhibitors with broad inhibitory specificity. For the inhibition of serine, cysteine, and metalloproteases in bacterial, mammalian, yeast, and plant cell extracts.
Solubility/Stability: Soluble in aqueous buffers, or add directly to extraction media. Alternatively, prepare 7x stock solutions in 1.5 ml water or 100 mM phosphate buffer, pH 7.0. Stock solution is stable for 1-2 weeks at +2 to +8°C or at least 12 weeks at -15 to -25°C. Can be used in thiol-containing solutions at room temperature.
Note: Inhibition efficiency is quickly and sensitively tested with the Universal Protease Substrate (Cat. Nos. 11 080 733 001 or 11 734 334 001).
Androgen Receptor Controls EGFR and ERBB2 Gene Expression at Different Levels in Prostate Cancer Cell Lines
Prostate cancer is the most commonly diagnosed non-cutaneous malignancy in men in developed countries. At diagnosis most prostate cancers are androgen dependent, meaning their growth, survival and progression are driven by the androgen-activated androgen receptor. This application note describes a study on androgenic regulation of EGFR and ERBB2 expression in prostate cancer cell lines presenting different androgen sensitivities. Inhibition of local androgen production could be an efficient way to stop the progression of prostate cancer, similar to treatment of breast cancers using aromatase inhibitors.
