Purity > 90% as determined by SDS-PAGE. MW: 27.8kDa. Partial: 23-224aa. N-terminal 6xHis-tagged. Homo sapiens (Human). Isoform 1 functions as Extracellular domain 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 complent. 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
Size
100ug
Concentration
n/a
Applications
RUO
Other Names
Aging-associated gene 4 protein; Apolipoprotein J; Apo-JComplement cytolysis inhibitor; CLIComplement-associated protein SP-40,40Ku70-binding protein 1NA1/NA2Testosterone-repressed prostate message 2; TRPM-2