Human Clusterin/Apolipoprotein J/Apo-J (His Tag)

Human Clusterin/Apolipoprotein J/Apo-J (His Tag)

• DataSheet
• Material Safety Data Sheets (MSDS)

Isoform 1 functions as extracellular chaperone that prevents aggregation of nonnative proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. Secreted isoform 1 protects cells against apoptosis and against cytolysis by complement. Intracellular isoforms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity. Nuclear isoforms promote apoptosis. Mitochondrial isoforms suppress BAX-dependent release of cytochrome c into the cytoplasm and inhibit apoptosis. Plays a role in the regulation of cell proliferation. {PubMed:11123922, PubMed:12047389, PubMed:12176985, PubMed:12551933, PubMed:12882985, PubMed:16113678, PubMed:17260971, PubMed:17407782, PubMed:17412999, PubMed:17689225, PubMed:19137541, PubMed:19535339, PubMed:19996109, PubMed:20068069, PubMed:21505792}.

Clusterin

APOJ; CLI; KUB1

P10909

CLU; APOJ; CLI; KUB1; AAG4

Human Cells

A DNA sequence encoding the human CLU isoform long (NP_001822.2) (Met 1-Glu 501) was expressed, with a C-terminal polyhistidine tag.

Human

The full length of recombinant human CLU comprises 438 amino acids and has a calculated molecular mass of 51.5 kDa (24.5 + 27). The apparent molecular mass of the recombinant protein is approximately 37-39 kDa in SDS-PAGE under reducing conditions, corresponding to the cleaved ? chain, and ? chain respectively.

> 92 % as determined by SDS-PAGE