Category: Proteins & Peptides

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  • Brand: Abclonal
  • Brand: Invent
Reference: RP10191TLQ

The 20S proteasome has a barrel – shaped structure arranged as four heptomeric rings of αββα. In eukaryotes, each of α and β ring is composed of seven different proteins. The β1, β2 and β5 subunits have ‘caspase-like’, ‘trypsin-like’ and ‘chymotypsin-like’ activities, respectively. In 26S proteasome-mediated protein degradation, to entry the β chamber of the 20S proteasome that houses the proteolytic sites, a substrate protein has to pass through a substrate translocation channel consisting of the double-ring formed by six ATPases of PA700 and the α chamber formed by α subunits of the 20S proteasome.

Reference: RP10195D

This product is a native K6-linked diUb which can be used as a substrate for deubiquitinating enzymes. It can also be used to investigate linkage specificiy of proteins that contain ubiquitin-associated domains or ubiquitin-interacting motifs. This product is formed by chemical ligation.

Reference: RP10199DLQ

A single biotin moiety is conjugated on the N-terminus of ubiquitin. All lysine residues of ubiquitin are still available for formation of polyubiquitin chains. The extremely high binding affinity between biotin and streptavidin allows the use of N-terminal biotin-ubiquitin for the following in vitro assays: 1) rapid and efficient purification of polyubiquitinated substrate proteins; 2) monitoring substrate ubiquitination using an HRP-conjugated streptavidin antibody; and 3) setting up high throughput FRET assays to monitor substrate ubiquitination in assays screening E3 ubiquitin ligase inhibitors.

Reference: RP10201LQ

USP7 is a cysteine protease, belongs to the family of ubiquitin-specific proteases. USP7 was first discovered as a binding enzyme to the Herpes simplex viral protein. Studies have shown that USP7 could deubiquitinate the autoubiquitination of an E3 ligase called HDM2 that promotes ubiquitination and subsequent degradation of p53. The USP7/HDM2/p53 interaction results in higher protein levels of HDM2 and lower levels of p53. Because of its apparent role in different types of pathologies, including lung and liver cancer, it has become a possible target for drug therapies.

Reference: RP10211K

This kit is designed for two purposes: 1) identification of proteins that specially bind linear polyUb chains in whole cell or tissue lysates; 2) validation of direct interactions between linear polyUb chains and their binding proteins. The non-cleavable 6xHis-tagged linear Ub6 is resistant of deubiquitination when incubating with whole cell or tissue lysates, thus allowing maximally capture proteins that specifically bind linear polyUb chains. After binding, 6XHis-tagged non-cleavable linear Ub6 and the binding proteins can be enriched with Nickel XPure Agarose Resin (included). The bound proteins and the non-cleavable polyUb chains can be eluted from Ni resin using a buffer containing 250 mM imidazole (included) or by incubating with TEV protease (not included). Either of the elution method can significantly reduce the amounts of non-specific binding proteins when compared with elution using SDS sample buffer.

Reference: RP10223K

Immunoproteasome Activity Fluorometric Assay Kit II was designed for assaying the immunoproteasomes' chymotrypsin-like, trypsin-like and caspase-like activities in vitro using purified proteasomes, cell lysates or tissue extracts. The proteasome cleaves these fluorogenic substrates, and the released AMC fluorescence can be monitored using a plate reader or fluorometer at the excitation/emission wavelength of 360nm/460nm, respectively.?

Reference: RP10233K

This kit is designed for enrichment of cellular proteins conjugated with lysine 29/33-linked polyubiquitin chains using GST-TRABID (ZNF1). Polyubiquitinated proteins bound on GST-TRABID (ZNF1) can be precipi-tated using glutathione resin and eluted by a buffer containing 10 mM glutathione. Enriched polyubiqui-tinated proteins can be assayed by immunoblotting or mass spectrometry.