Anti-Clusterin, clone 1A11

Item number Size Datasheet Manual SDS Delivery time Quantity Price
ARG56936.50 50 µl - -

6 - 14 business days*

488.00€
 
Protein function: Isoform 1 functions as extracellular chaperone that prevents aggregation of... more
Product information "Anti-Clusterin, clone 1A11"
Protein function: 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. [The UniProt Consortium]
Keywords: Anti-CLU, Anti-APOJ, Anti-AAG4
Supplier: Arigo Biolaboratories
Supplier-Nr: ARG56936

Properties

Application: WB, FC, ICC, IF, IHC (paraffin)
Antibody Type: Monoclonal
Clone: 1A11
Conjugate: No
Host: Mouse
Species reactivity: human
Immunogen: Recombinant fragment around aa. 1-333 of Human Clusterin
Format: Purified

Handling & Safety

Storage: -20°C
Shipping: +4°C (International: +4°C)
Caution
Our products are for laboratory research use only: Not for administration to humans!
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