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  • 产品名称：Clusterin(CLU)(AA228-449)(Active)protein(Histag)

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  • 产品厂商：ACROBiosystems
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简单介绍：
Clusterin(CLU)(AA228-449)(Active)protein(Histag)
详情介绍：
Characteristics rh CLUS / Clusterin is fused with 6 xHis tag at the C terminus, and has a calculated MW of 50.9 kDa (Asp23-Glu449, α chain 24.5 kDa + β chain 27 kDa). The recombinant rh CLUS / Clusterin (Asp23-Glu 449) was cleaved into α chain and β chain, which form a heterodimer linked by disulfide bonds. DTT reduced protein migrates as 39 kDa and 40 kDa bands in SDS-PAGE due to glycosylation, corresponding to the cleaved β chain, and α chain respectively.
Purity >90 % as determined by SDS-PAGE.
Sterility 0.22 μm filtered
Endotoxin Level Less than 1.0 EU per μg by the LAL method.
ProductDetails: Biological Activity Comment Biological Activity: Measured by its ability to induce clustering of human clear cell carcinoma epithelial cells Caki-2. Measured by its ability to inhibit DTT (Dithiothreitol) induced BSA precipitation.

SDS-PAGE: due to glycosylation, corresponding to the cleaved β chain, and α chain respectively.
Background Clusterin (CLU) is also known as dimeric acidic glycoprotein (DAG protein), testosterone repressed prostate message-2 (TRPM-2), sulfated glycoprotein-2 (SGP-2) and complement lysis inhibitor (CLI), is a secreted multifunctional glycoprotein protein which belongs to the clusterin family. Intracellular cleavages of the precursor of clusterin remove the signal peptide and generate comparably sized α and β chains which are secreted as an 80 kDa N-glycosylated disulfide-linked heterodimer. DAG protein is predominantly expressed in ***** testis, ovary, adrenal gland, liver, heart, and brain and in many epithelial tissues during embryonic development. Clusterin involve in several basic biological events such as cell death, tumor progression, and neurodegenerative disorders. Upregulation of clusterin mRNA and protein levels detected in diverse disease states and in in vitro systems have led to suggestions that it functions in membrane lipid recycling, in apoptotic cell death, and as a stress-induced secreted chaperone protein, amongst others.
Molecular Weight 50.9 kDa (Disulfide - linked heterodimer)
NCBI Accession NP_001822
UniProt P10909
Research Area Receptors, Cancer
Pathways Apoptosis, Negative Regulation of intrinsic apoptotic Signaling
Restrictions For Research Use only
Format Lyophilized
Reconstitution Please see Certificate of Analysis for specific instructions. For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
Buffer PBS, pH 7.4
Handling Advice Avoid repeated freeze-thaw cycles.
Storage -20 °C
Storage Comment No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C), After reconstitution under sterile conditions for 3 months (-70 °C).
Supplier Images
SDS-PAGE (SDS) image for Clusterin (CLU) (AA 228-449) (Active) protein (His tag) (ABIN2180885) Human Clusterin, His Tag on SDS-PAGE under reducing (R) condition. The gel was staine...
Background publications Leskov, Klokov, Li, Kinsella, Boothman: "Synthesis and functional analyses of nuclear clusterin, a cell death protein." in: The Journal of biological chemistry, Vol. 278, Issue 13, pp. 11590-600, 2003 (PubMed).

Keeshan, Santilli, Corradini, Perrotti, Calabretta: "Transcription activation function of C/EBPalpha is required for induction of granulocytic differentiation." in: Blood, Vol. 102, Issue 4, pp. 1267-75, 2003 (PubMed).

Santilli, Aronow, Sala: "Essential requirement of apolipoprotein J (clusterin) signaling for IkappaB expression and regulation of NF-kappaB activity." in: The Journal of biological chemistry, Vol. 278, Issue 40, pp. 38214-9, 2003 (PubMed).

Jones, Jomary: "Clusterin." in: The international journal of biochemistry & cell biology, Vol. 34, Issue 5, pp. 427-31, 2002 (PubMed).

Poon, Rybchyn, Easterbrook-Smith, Carver, Pankhurst, Wilson: "Mildly acidic pH activates the extracellular molecular chaperone clusterin." in: The Journal of biological chemistry, Vol. 277, Issue 42, pp. 39532-40, 2002 (PubMed).

Wong, Taillefer, Lakins, Pineault, Chader, Tenniswood: "Molecular characterization of human TRPM-2/clusterin, a gene associated with sperm maturation, apoptosis and neurodegeneration." in: European journal of biochemistry / FEBS, Vol. 221, Issue 3, pp. 917-25, 1994 (PubMed).