Clusterin (16Y5) Rabbit Monoclonal Antibody

Clusterin (16Y5) Rabbit Monoclonal Antibody

Size1:50μl Price1:$128
Size2:100μl Price2:$230
Size3:500μl Price3:$980
SKU: AMRe09072 Category: Rabbit Monoclonal Antibody Tags: , , , , ,

Datasheet

Summary

Production Name

Clusterin (16Y5) Rabbit Monoclonal Antibody

Description

Rabbit Monoclonal Antibody

Host

Rabbit

Application

WB,ELISA

Reactivity

Human,Mouse

 

Performance

Conjugation

Unconjugated

Modification

Unmodified

Isotype

IgG

Clonality

Monoclonal

Form

Liquid

Storage

Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles.

Buffer

Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% New type preservative N and 50% glycerol. Store at +4°C short term. Store at -20°C long term. Avoid freeze / thaw cycle.

Purification

Affinity purification

 

Immunogen

Gene Name

CLU

Alternative Names

CLI; AAG4; APOJ; CLU1; CLU2; KUB1; SGP2; APO-J; SGP-2; SP-40;TRPM2; TRPM-2; NA1/NA2;

Gene ID

1191

SwissProt ID

P10909

 

Application

Dilution Ratio

WB 1:500-1:2000

Molecular Weight

52kDa

 

Background

Clusterin (CLU, apolipoprotein J) is a multifunctional glycoprotein that is expressed ubiquitously in most tissues. Clusterin functions as a secreted chaperone protein that interacts with and stabilizes stress-induced proteins to prevent their precipitation. Research studies show that clusterin plays a protective role in Alzheimer’s disease by sequestering amyloid β(1-40) peptides to form long-lived, stable complexes, which prevents amyloid fibril formation. [Isoform 1]: Functions as extracellular chaperone that prevents aggregation of non native proteins (PubMed:11123922, PubMed:19535339). Prevents stress-induced aggregation of blood plasma proteins (PubMed:11123922, PubMed:12176985, PubMed:17260971, PubMed:19996109). Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro) (PubMed:12047389, PubMed:17412999, PubMed:17407782). Does not require ATP (PubMed:11123922). Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70 (PubMed:11123922). Does not refold proteins by itself (PubMed:11123922). Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation (PubMed:21505792). Protects cells against apoptosis and against cytolysis by complement (PubMed:2780565). 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 (PubMed:20068069). Promotes proteasomal degradation of COMMD1 and IKBKB (PubMed:20068069). Modulates NF-kappa-B transcriptional activity (PubMed:12882985). A mitochondrial form suppresses BAX- dependent release of cytochrome c into the cytoplasm and inhibit apoptosis (PubMed:16113678, PubMed:17689225). Plays a role in the regulation of cell proliferation (PubMed:19137541). An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5 (PubMed:22689054). Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (PubMed:24073260). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity).

 

Research Area