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F1043

Sigma-Aldrich

Monoclonal Anti-Filensin antibody produced in mouse

clone FIL-7B10, ascites fluid

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About This Item

MDL number:
MFCD00677365
UNSPSC Code:
12352203

biological source

mouse

conjugate

unconjugated

antibody form

ascites fluid

antibody product type

primary antibodies

clone

FIL-7B10, monoclonal

mol wt

antigen 115 kDa

contains

15 mM sodium azide

species reactivity

bovine, sheep, human

should not react with

mouse, chicken, rat

technique(s)

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

isotype

IgG1

UniProt accession no.

Q12934

shipped in

dry ice

storage temp.

−20°C

Gene Information

human ... BFSP1(631)

Specificity

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).

Immunogen

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

Application

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

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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.
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
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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