Analytical Data
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Gene name
Plectin
- Application
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Alternative Names
HD1; PCN; EBS1; EBSO; PLEC1b; PLTN; Hemidesmosomal protein 1; Intermediate Filament Binding Protein 500kDa; Epidermolysis Bullosa Simplex 1(Ogna)
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q15149
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Expression Region
Asp175~Pro400
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Molecular Weight
32kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
Plectin, a versatile cytoskeletal linker protein, plays a crucial role in maintaining the structural integrity and organization of cells by bridging intermediate filaments with various cellular components, including microtubules and actin filaments. It is encoded by the PLEC gene located on chromosome 8, and mutations in this gene are associated with a variety of human diseases, including muscular dystrophies and epidermolysis bullosa. Given its importance in cellular mechanics and signaling, the study of recombinant Plectin has garnered significant attention. Researchers have been focusing on the molecular characterization, structural biology, and functional assays of recombinant Plectin to better understand its role in cellular architecture and pathology. By producing recombinant forms of Plectin, scientists aim to reveal insights into its interactions with cytoskeletal elements and other binding partners, which could lead to therapeutic strategies for diseases linked to its dysfunction. Recent advancements in protein engineering have enabled the generation of specific Plectin isoforms and functional domains useful for investigating its mechanistic properties in vitro and in vivo. This research not only enhances our understanding of Plectin’s biological functions but also paves the way for potential clinical applications, including gene therapy and the development of biomaterials that mimic Plectin’s functionality to promote cell adhesion and tissue regeneration.
