F1043
Monoclonal Anti-Filensin antibody produced in mouse
clone FIL-7B10, ascites fluid
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About This Item
UNSPSC Code:
12352203
MDL number:
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.
shipped in
dry ice
storage temp.
−20°C
Gene Information
human ... BFSP1(631)
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)
Western Blotting (1 paper)
Biochem/physiol Actions
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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