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Merck
CN

F1043

Sigma-Aldrich

Monoclonal Anti-Filensin antibody produced in mouse

clone FIL-7B10, ascites fluid

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MDL编号:
UNSPSC代码:
12352203
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生物来源

mouse

偶联物

unconjugated

抗体形式

ascites fluid

抗体产品类型

primary antibodies

克隆

FIL-7B10, monoclonal

分子量

antigen 115 kDa

包含

15 mM sodium azide

种属反应性

bovine, sheep, human

请勿与下列物质发生反应

mouse, chicken, rat

技术

immunohistochemistry (frozen sections): suitable
indirect immunofluorescence: 1:400 using bovine lens frozen sections
microarray: suitable
western blot: suitable

同位素/亚型

IgG1

UniProt登记号

运输

dry ice

储存温度

−20°C

基因信息

human ... BFSP1(631)

免疫原

human and bovine lens filament enriched fraction (plasma membrane-cytoskeleton complex).

应用

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)

生化/生理作用

The antibody recognizes an epitope located within either the rod or the N-terminal non-(α) helical domain of the filensin molecule. May be used in immunoblotting where it specifically detects both the full-length filensin (115 kDa), the processed fragment, and a variety of breakdown products in the mol. wt. range of 28-69 kDa. Does not react with cultured lens epithelial cells nor with normal human skin, psoriatic or tumoral skin (basal cell carcinoma).

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Shih-Ping Su et al.
Molecular vision, 17, 2798-2807 (2012-01-06)
It is well established that levels of soluble α-crystallin in the lens cytoplasm fall steadily with age, accompanied by a corresponding increase in the amount of membrane-bound α-crystallin. Less well understood, is the mechanism driving this age-dependent membrane association. The
A Sandilands et al.
European journal of cell biology, 67(3), 238-253 (1995-07-01)
Filensin is a lens-specific intermediate filament protein, expressed in the lens fiber cells but not the lens epithelium. Using antibodies to filensin and the other lens intermediate filament proteins, vimentin and CP49, the codistribution of filensin with CP49 and independence
Shih-Ping Su et al.
Biochimica et biophysica acta, 1814(5), 647-656 (2011-03-31)
The optical properties of the lens are dependent upon the integrity of proteins within the fiber cells. During aging, crystallins, the major intra-cellular structural proteins of the lens, aggregate and become water-insoluble. Modifications to crystallins and the lens intermediate filaments

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