Rabbit Polyclonal Filensin antibody. Suitable for WB, IHC-P and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Recombinant Fragment Protein within Human BFSP1 aa 1-200.
View Alternative Names
Filensin, Beaded filament structural protein 1, Lens fiber cell beaded-filament structural protein CP 115, Lens intermediate filament-like heavy, CP115, LIFL-H, BFSP1
- IHC-P
Unknown
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Filensin antibody (AB126235)
ab126235, at a 1/500 dilution, staining Filensin in paraffin embedded U373 xenograft by Immunohistochemistry.
- WB
Unknown
Western blot - Anti-Filensin antibody (AB126235)
7.5% SDS PAGE
All lanes:
Western blot - Anti-Filensin antibody (ab126235) at 1/1000 dilution
All lanes:
HCT116 whole cell lysate at 30 µg
Predicted band size: 75 kDa
false
Reactivity data
Properties and storage information
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Purification technique
Storage buffer
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Filensin interacts with phakinin also called beaded filament structural protein 2 (BFSP2) forming a complex known as the beaded filament. This complex provides structural support to lens fiber cells essential for their long-term survival and functional maintenance. Filensin's role is vital for maintaining the mechanical properties and flexibility of lens cells ensuring the proper refractive function of the lens. Its expression and function are tightly regulated during lens development and differentiation.
Pathways
Filensin is part of the intermediate filament pathway influencing cell structure and mechanical stability. It associates with the cytoskeletal organization pathways playing a role in maintaining the shape and elasticity of lens fibers. Through these pathways Filensin interacts with proteins like vimentin and alpha-crystallin which are involved in maintaining lens cell integrity and preventing aggregation of lens proteins. These interactions are important for lens transparency and visual function.
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Target data
Publications (1)
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Frontiers in cell and developmental biology 12:1396890 PubMed38983788
2024
Applications
Unspecified application
Species
Unspecified reactive species
Product promise
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