Sbp biochemistry

  • How big is the SBP-tag?

    The SBP-tag sequence is 38 amino acids long and binds to streptavidin with an equilibrium dissociation constant of 2.5 nM..

  • What is SFB tag?

    We detail the S-, 2\xd7FLAG-, and Streptavidin-Binding Peptide (SBP)- tandem tags (SFB-tag) system for protein purification.
    This protocol can be used to identify protein interactors and establish a high-confidence protein-protein interaction network based on computational models..

  • What is streptavidin used for?

    Streptavidin is widely used in Western blotting and immunoassays conjugated to some reporter molecule, such as horseradish peroxidase.
    Streptavidin has also been used in the developing field of Nanobiotechnology, the use of biological molecules such as proteins or lipids to create nanoscale devices/structures..

  • What is the SBP protein tag?

    The Streptavidin-Binding Peptide (SBP)-Tag is a 38-amino acid sequence that may be engineered into recombinant proteins.
    Recombinant proteins containing the SBP-Tag bind to streptavidin and this property may be utilized in specific purification, detection or immobilization strategies..

  • SBP (for SQUAMOSA-pROMOTER BINDING PROTEIN) domain is a sequence specific DNA-binding domain found in plant proteins. .
    Members of family probably function as transcription factors involved in the control of early flower development. .
    They share a highly conserved DNA-binding domain that contains two zinc-binding
  • The Strep-tag is a nine-amino acid peptide (sequence: AWRHPQFGG) with high specificity and affinity towards the protein reagent streptavidin.
  • We detail the S-, 2\xd7FLAG-, and Streptavidin-Binding Peptide (SBP)- tandem tags (SFB-tag) system for protein purification.
    This protocol can be used to identify protein interactors and establish a high-confidence protein-protein interaction network based on computational models.
The Streptavidin-Binding Peptide (SBP)-Tag is a 38-amino acid sequence that may be engineered into recombinant proteins. Recombinant proteins containing the  ApplicationsProtein complex purificationProteomicsImaging

What is a substrate-binding protein (SBP)?

Substrate-binding proteins (SBPs) play an important role in solute uptake and signal transduction.
In 2010, Berntsson et al. classified the 114 organism-specific SBP structures available at that time and defined six protein clusters, based on their structural similarity.

What is selenium binding protein (SBP)?

The Selenium Binding Protein (SBP), which does not contain Se-Cys, is most probably involved in selenium metabolism.
SBP was initially isolated from mouse liver, as a cytosolic protein and named SBP56 (Bansal et al. 1989, 1990 ).

Why is SBP important in biochemistry?

A key advantage of SBP is that it can be eluted natively using biotin.
This is particularly relevant to enzymes such as:

  • condensin or for complexes whose assays require native conditions for activity.
    Therefore the SBP tag is of great utility to both proteomics analysis and in vitro biochemical assays.

    • Why is the SBP Tag used in protein purification?

    Because of the high affinity and specificity of the SBP tag to streptavidin, this system has been successfully applied for one-step affinity purification of proteins , , , for studying protein-protein interactions , and for developing improved tandem tags in protein studies , , , .

    Amino acid sequence

    The Streptavidin-Binding Peptide (SBP)-Tag is a 38-amino acid sequence that may be engineered into recombinant proteins.
    Recombinant proteins containing the SBP-Tag bind to streptavidin and this property may be utilized in specific purification, detection or immobilization strategies.

    Amino acid sequence

    The Streptavidin-Binding Peptide (SBP)-Tag is a 38-amino acid sequence that may be engineered into recombinant proteins.
    Recombinant proteins containing the SBP-Tag bind to streptavidin and this property may be utilized in specific purification, detection or immobilization strategies.

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