Recombinant Proteins

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Streptavidin

Streptavidin Recombinant

Streptavidin Streptomyces Avidinii Recombinant produced in E.Coli.
The molecular weight per tetramer is approximately 52kDa.
Shipped with Ice Packs
Cat. No.
BT3750
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

Streptavidin (37-159), His

Streptavidin (37-159 a.a) Recombinant, His Tag

Streptavidin Recombinant produced in E. coli is a single polypeptide chain containing 148 amino acids (37-159) and having a molecular mass of 15.6kDa. Streptavidin is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3826
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

Streptavidin Protein

Streptavidin

Streptavidin is a protein produced by Streptomyces avidinii and isolated by purification from fermentation broth. The pure, homogeneous protein shows predominantly one single band in SDS PAGE. Streptavidin consists of 4 identical subunits, each bearing an active binding site for biotin. Streptavidin has a molecular weight of 55kDa.
Shipped with Ice Packs
Cat. No.
BT3923
Source
Bacterium Streptomyces avidinii.
Appearance
Sterile Filtered lyophilized powder.

Streptavidin, His

Streptavidin Recombinant, His Tag

Recombinant Streptomyces Avidinii Streptavidin produced in E.Coli is a single, non-glycosylated polypeptide chain (25-183) containing a total of 167 amino acids and having a molecular mass of 17kDa. The Streptavidin protein is fused to an 8 aa N-terminal His-Tag and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3997
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

Streptavidin-NC

Streptavidin-NC Recombinant

Recombinant Streptavidin-NC produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 24kDa. Streptavidin-NC is engineered to bind to nitrocellulose.

Shipped with Ice Packs
Cat. No.
BT4096
Source
Escherichia Coli.
Appearance
Sterile Liquid formulation.
Definition and Classification

Streptavidin is a tetrameric protein isolated from the bacterium Streptomyces avidinii. It is known for its extraordinarily high affinity for biotin (vitamin B7 or vitamin H), with a dissociation constant (Kd) on the order of ≈10^-14 mol/L . Streptavidin is composed of four identical subunits, each capable of binding one molecule of biotin . This protein is extensively used in molecular biology and biotechnology due to its strong and specific binding to biotin .

Biological Properties

Streptavidin has several key biological properties:

  • High Affinity for Biotin: Streptavidin binds biotin with one of the strongest non-covalent interactions known in nature .
  • Tetrameric Structure: It forms a tetramer, with each subunit contributing to the biotin-binding site of its neighbor .
  • Stability: The streptavidin-biotin complex is highly stable, resistant to organic solvents, denaturants, detergents, proteolytic enzymes, and extremes of temperature and pH .
  • Expression Patterns and Tissue Distribution: Streptavidin is naturally produced by Streptomyces avidinii .
Biological Functions

The primary biological function of streptavidin is to bind biotin with high specificity and affinity . This interaction is utilized in various biotechnological applications, including:

  • Immune Responses: Streptavidin is used in immunological assays such as ELISA, western blotting, and immunohistochemistry .
  • Pathogen Recognition: It can be used to detect biotinylated molecules, aiding in the identification of pathogens .
Modes of Action

Streptavidin interacts with other molecules and cells primarily through its binding to biotin. The binding involves:

  • Hydrogen Bonds: Extensive hydrogen bonding with biotin contributes to the high affinity .
  • Multivalency: Each streptavidin tetramer can bind up to four biotin molecules, enhancing its binding capacity .
  • Downstream Signaling Cascades: The streptavidin-biotin interaction can be used to link various molecules, facilitating downstream signaling in experimental setups .
Regulatory Mechanisms

The expression and activity of streptavidin are regulated by:

  • Transcriptional Regulation: The gene encoding streptavidin is regulated at the transcriptional level in Streptomyces avidinii .
  • Post-Translational Modifications: Streptavidin undergoes post-translational modifications to achieve its mature form, which is essential for its high biotin-binding affinity .
Applications

Streptavidin has numerous applications in biomedical research and diagnostics:

  • Biomedical Research: It is used in various assays and techniques, including ELISA, western blotting, and immunohistochemistry .
  • Diagnostic Tools: Streptavidin-biotin interactions are employed in diagnostic assays to detect specific biomolecules .
  • Therapeutic Strategies: Streptavidin is used in targeted drug delivery and radioimmunotherapy .
Role in the Life Cycle

Streptavidin plays a crucial role throughout the life cycle of Streptomyces avidinii:

  • Development: It is produced during the growth phase of the bacterium .
  • Aging and Disease: The stability and high affinity of streptavidin for biotin make it a valuable tool in studying aging and disease processes .
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