/CLU重组蛋白(Sulfated glycoprotein

英文名称：

Recombinant Mesocricetus auratus Clusterin (CLU)

品名简称：

Recombinant Mesocricetus auratus CLU protein

货号：

CSB-EP005595MRG

规格:

20μg

价格：

2328

LC-MS/Western Blot：

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SDS-PAGE：

(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

纯度：

Greater than 85% as determined by SDS-PAGE.

内毒素：

Not test

生物活性：

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基因名：

CLU

Uniprot No.：

P14683

别名：

(Sulfated glycoprotein 2)(SGP-2)(Fragment)

种属：

Mesocricetus auratus (Golden hamster)

蛋白长度：

Full Length

来源：

E.coli

分子量：

29.5 kDa

表达区域：

1-191aa

氨基酸序列：

NRRPHFLYPKSRLIRSLLPPPHYGPLSFHDMFQPFLEMIHQAQQAMDVQFHSPAFQFPDMDLLREGEDDRAVCKEIRHNSTGCLKMKGQCEKCQEILSVDCSANNPAQAHLRQELNDSLQVAERLTQRYNELLHSLQTKMLNTSSLLEQLNEQFNWVSQLANLTQGEDQYYLRVSTVTTHSSDSEVPSRVT

蛋白标签：

N-terminal 10xHis-tagged and C-terminal Myc-tagged

产品提供形式：

Liquid or Lyophilized powder

缓冲液：

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

储存条件：

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

保质期：

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.

货期：

13-23 business days

注意事项：

Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.

功能1：

Functions as extracellular chaperone that prevents aggregation of non native 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. When secreted, protects cells against apoptosis and against cytolysis by complement. 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. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity. Following stress, promotes apoptosis. Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation. An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity. Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3. Plays a role in the clearance of immune complexes that arise during cell injury.

功能2：

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文献：

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研究领域：

Cancer

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