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S5a; 26S Proteasome Regulatory Subunit S5a; ASF; Macropain; Mcb1; PSMD4; pUB-R5; Rpn10; 26S Proteasome Non-ATPase Regulatory Subunit 4

Protein

E. coli

Human angiocidin (Accession Nr. P55036).

Human

Agarose

Liquid. In 50mM HEPES, pH 7.5, 250mM NaCl, 1mM sodium azide.

Use: This affinity resin can be used for the enrichment, isolation and identification of ubiquitinated proteins, 26S substrates or proteins that contain ubiquitin-like domains. Equilibrate resin by washing with 5-10ml desired start buffer. Binding and elution of material is dependent on individual experimental conditions. Storage: The agarose can be re-used for at least 5-10 applications if properly maintained. After use, clean resin with 5ml 50mM Tris pH 9.0, 1M KCl. Remove cleaning solution by washing resin with 5ml storage buffer.

Manufactured by Boston Biochem

BLUE ICE

+4°C

+4°C

Do not freeze.

Stable for at least 3 months after receipt when stored at +4°C.

No

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Angiocidin, also known as S5a or anti-secretory factor (ASF), is classified under the gene PSMD4, but is often referred to by a different name depending on the context in which it is described. S5a and ASF have identical 377 amino acid (aa) sequences, while angiocidin is described as having an additional Gly255Glu256Arg257 sequence in its C-Terminus. The human protein shares 96% and 99% aa sequence identity with its mouse and rat orthologs, respectively. Structurally, it contains a N-terminal von Willebrand Factor type A domain and two C-terminal ubiquitin-interacting motifs (UIM). It acts as a ubiquitin-binding protein where it is most commonly referred to as S5a or in yeast as Rpn10. It is part of the 19S regulatory subunit of the 26S Proteasome where its UIM recognizes poly-ubiquitinated proteins destined for degradation. As a part of the proteasome complex, it may also recognize the ubiquitin-like modifier FAT10. Free cytoplasmic forms also exist where its ubiquitination is catalyzed by a range of ubiquitin E3 ligases from different classes. Therefore, experimentally Angiocidin may act as a useful substrate to monitor the activity of (E3) ligases, independent of their specific mechanisms of action. In cancer biology, where it is often referred to as angiocidin, it is shown to slow tumor progression. It is found in the extracellular matrix of certain tumor subtypes, and it may act by suppressing angiogenesis or by directly inhibiting tumor cell growth. It also is found in several biological fluids where it is known primarily as ASF. It suppresses fluid secretion in response to enterotoxin and may act as an anti-inflammatory factor.