Clusterin (D7N2K) XP® Rabbit mAb #34642
- WB
- IHC
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 35-42, 65, 75 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IHC-Immunohistochemistry
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunohistochemistry (Paraffin) | 1:400 |
Storage
Protocol
Specificity / Sensitivity
Species Reactivity:
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser396 of human Clusterin protein.
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 (1,2). 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 (3-5). In addition to the secreted protein, several intracellular isoforms are localized to the nucleus, mitochondria, cytoplasm, and ER. The subcellular distribution of these multiple isoforms leads to the diversity of clusterin functions. Additional studies report that clusterin is involved in membrane recycling, cell adhesion, cell proliferation, apoptosis, and tumor survival (6-9). The clusterin precursor is post-translationally cleaved into the mature clusterin α and clusterin β forms. Clusterin α and β chains create a heterodimer through formation of disulfide bonds (10).
- Poon, S. et al. (2000) Biochemistry 39, 15953-60.
- Poon, S. et al. (2002) FEBS Lett 513, 259-66.
- Yerbury, J.J. et al. (2007) FASEB J 21, 2312-22.
- Narayan, P. et al. (2012) Nat Struct Mol Biol 19, 79-83.
- Desikan, R.S. et al. (2014) JAMA Neurol 71, 180-7.
- Rosenberg, M.E. and Silkensen, J. (1995) Int J Biochem Cell Biol 27, 633-45.
- Wilson, M.R. and Easterbrook-Smith, S.B. (2000) Trends Biochem Sci 25, 95-8.
- Trougakos, I.P. and Gonos, E.S. (2002) Int J Biochem Cell Biol 34, 1430-48.
- Shannan, B. et al. (2006) Cell Death Differ 13, 12-9.
- de Silva, H.V. et al. (1990) Biochemistry 29, 5380-9.
限制使用
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