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Your Position: Home > Protein > Streptavidin > STN-NA118

Streptavidin Protein-Alexa Fluor™ 488 (MALS verified)

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  • Synonym
    Streptavidin,SA
  • Source
    Streptavidin Protein-Alexa Fluor 488(STN-NA118) is expressed from E. coli cells.
  • Molecular Characterization

    This protein carries no "tag".

    The protein has a calculated MW of 13.8 kDa. The protein migrates as 15 kDa under reducing (R) condition (SDS-PAGE).

  • Conjugate

    AF488

    Excitation Wavelength: 488 nm

    Emission Wavelength: 517 nm

  • Labeling
    The primary amines in the side chains of lysine residues and the N-terminus of the protein are conjugated with AF488 using standard chemical labeling method. The residual AF488 is removed by molecular sieve treatment during purification process.
  • Protein Ratio
    The AF488 to protein molar ratio is 1-2.
  • Purity

    >95% as determined by SDS-PAGE.

    >90% as determined by SEC-MALS.

  • Formulation

    Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.

    Contact us for customized product form or formulation.

  • Reconstitution

    Please see Certificate of Analysis for specific instructions.

    For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

  • Storage

    For long term storage, the product should be stored at lyophilized state at -20°C or lower.

    Please protect from light and avoid repeated freeze-thaw cycles.

    This product is stable after storage at:

    1. -20°C to -70°C for 12 months in lyophilized state;
    2. -70°C for 3 months under sterile conditions after reconstitution.
SDS-PAGE
Streptavidin SDS-PAGE

Streptavidin Protein-Alexa Fluor 488 on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 95%.

SEC-MALS
Streptavidin MALS images

The purity of Streptavidin Protein-Alexa Fluor 488 (Cat. No. STN-NA118) is more than 90% and the molecular weight of this protein is around 48-65 kDa verified by SEC-MALS.

  • Background
    Streptavidin is a 66KDa tetrameric protein purified from the bacterium Streptomyces avidinii, and exhibits high binding affinity to biotin. Each unit can bind one biotin. Horseradish peroxidase is metalloenzyme, a 44KDa glycoprotein. When incubate with substrates, it produces a coloured, fluorimetric, or luminescent derivatives, which can be detected and quantified. HRP conjugated Streptavidin is widely used for the detection and quantification of biotinylated proteins.
  • Clinical and Translational Updates

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