Proteasome 26S (human), (purified)

High integrity preparation for use in proteasome research.



BML-PW9310-0050	50 µg	300.00 USD

Highly purified preparation of ‘26S’ proteasomes useful for carrying out in vitro protein degradation studies with suitably ubiquitinylated protein substrates.

Product Specification

Formulation:	Suspended in TSD buffer, pH 7.0 / 35% glycerol.

Source/Host:	Isolated from human erythrocytes. Consists of a high purity mixture of ‘26S’ proteasomes singly (26S) and doubly (30S) capped with 19S regulatory subunit complexes in the ratio of 40% single cap : 60% double capped at the time of preparation.

Long Term Storage:	-80°C

Use/Stability:	When ready for use the enzyme should be thawed by standing on ice. If the enzymatic acitivity of the 26S proteasome is to be measured, it should be used immediately after thawing since the enzyme complex is labile. After dissociaton of the 26S complex the 20S proteasome activity is relatively stable.

Background / Technical Information:	Please click here for the comprehensive product datasheet.

A - Typical results from substrate overlay (carried out in buffer containing ATP and an ATP-regenerating system) and Coomassie staining of non denaturing gel of products isolated according to the purification shown alongside. Protein concentration is ~15-20µg per lane.. B – Coomassie staining of denaturing gel showing presence of proteasomal subunits.

A typical example of a sucrose density gradient separation and purification of 20S, 26S and 30S proteasome derived from human erythrocytes together with electron micrographs of the individual complexes. The protein concentration used for micrography is best at ~2.5µg/mL.

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Product Literature References

Reconstitution of hybrid proteasomes from purified PA700-20 S complexes and PA28alphabeta activator: ultrastructure and peptidase activities: F. Kopp et al.; J. Mol. Biol. 313, 465 (465), Abstract;

Studies on the activation by ATP of the 26 S proteasome complex from rat skeletal muscle: B. Dahlmann et al.; Biochem. J. 309 , 195 (195), Abstract;