Mouse Glycophorin A / CD235a Protein, His Tag & Fc Tag-null-试剂-生物在线
Mouse Glycophorin A / CD235a Protein, His Tag & Fc Tag

Mouse Glycophorin A / CD235a Protein, His Tag & Fc Tag

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产品名称: Mouse Glycophorin A / CD235a Protein, His Tag & Fc Tag

英文名称: Mouse Glycophorin A / CD235a Protein, His Tag & Fc Tag

产品编号: CDA-M526x

产品价格: 0

产品产地: USA

品牌商标: ACROBiosystems

更新时间: null

使用范围: null

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分子量:50.9 kDa (Disulfide  linked heterodimer)

纯度:>90% as determined by SDS-PAGE.

内毒素:Less than 1.0 EU per μg of the Human Clusterin, His Tag by the LAL method.

Buffer:PBS, pH7.4

生物活性: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.

产品特性:rh CLUS / Clusterin is fused with 6 ×His tag at the C terminus, and has a calculated MW of 50.9 kDa (Asp23-Glu449, α chain 24.5kDa + β chain 27kDa). 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.

产品背景: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 Nglycosylated disulfidelinked heterodimer. DAG protein is predominantly expressed in adult 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. 
SDS-PAGE