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

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

• DataSheet
• Material Safety Data Sheets (MSDS)

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. When secreted, protects cells against apoptosis and against cytolysis by complement. Intracellular forms 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. Promotes apoptosis when in the nucleus. Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation (By similarity).

Clusterin

AGING-ASSOCIATED PROTEIN 4; D14UCLA3; CLU1; TRPM2; SGP2; COMPLEMENT LYSIS INHIBITOR; CLU2; SP-40; NA1/NA2; MGC24903; CLUSTERIN; SULFATED GLYCOPROTEIN 2; TRPM-2; APOJ; SGP-2; AAG4; CLUSTRIN; CLU; KUB1; CLI; SUGP-2; COMPLEMENT CYTOLYSIS INHIBITOR; APOLIPOPROTEIN J; AI893575; APO-J

Q549A5

Clu; Apoj; Msgp-2

Human Cells

A DNA sequence encoding the mouse CLU (NP_038520.2) (Met 1-Glu 448) was expressed, with a C-terminal polyhistidine tag.

Mouse

The full length of recombinant mouse CLU comprises 438 amino acids and has a calculated molecular mass of 50.8 kDa. The apparent molecular mass of the recombinant protein is approximately 32, 42 and 65 kDa in SDS-PAGE under reducing conditions, corresponding to the cleaved ? chain, ? chain and the full length respectively.

> 96 % as determined by SDS-PAGE