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The Canine 20S Proteasome is able to degrade substrates in an ATP-independent manner. It can be activated chemically with SDS (0.035%) or by the addition of PA28. Reaction conditions will need to be optimized for each specific application. We recommend an initial Canine 20S Proteasome concentration of 0.5-5 nM.

Source

Canine reticulocyte-derived 20S Proteasome protein

Predicted Molecular Mass

700 kDa

Product Datasheets

Product Datasheet

COA

SDS

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins.Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration.The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard.In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

E-358

Formulation	X mg/ml (X μM) in 50 mM HEPES pH 7.6, 150 mM NaCl, 1mM DTT
Shipping	The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage:	Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 12 months from date of receipt, -70 °C as supplied. 3 months, -70 °C under sterile conditions after opening.

Reconstitution Calculator

Background: 20S Proteasome

The 20S Proteasome is the catalytic core component of the multi-complex 26S Proteasome that selectively degrades intracellular proteins. It is commonly associated with regulatory complexes, which include the 19S Proteasome, the PA28 alpha/beta complex, or the PA28 gamma complex (1). The 20S Proteasome is composed of 28 subunits arranged into four stacked rings (2,3). The outer rings, containing seven subunits each, are composed of closely-related but non-identical alpha subunits. The amino-terminal tails of the alpha subunits form a gate that restricts substrate entry into the catalytic core. The inner rings, also containing seven subunits each, are composed of closely-related but non-identical beta subunits. The amino-terminal tails of six of the beta subunits, three per ring, have proteolytic activity. Inhibition of 20S Proteasome proteolytic core activity using small molecule inhibitors is a valuable tool for the functional study of a variety of proteins and for therapeutic intervention (4). The 20S Proteasome can be activated chemically by the addition of detergent or by the proteinaceous activator PA28 Activator alpha (5).

This product has been purified from canine erythrocytes.

References