STBD1 Human
Description
STBD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Starch Binding Domain 1 (SBD1) is a specialized protein domain that plays a crucial role in the binding and metabolism of starch. This domain is often utilized in recombinant protein technology to enhance the purification and functionality of proteins. The human recombinant version of SBD1 has been engineered to facilitate various biotechnological applications, particularly in the field of protein purification.
SBD1 is characterized by its ability to bind specifically to starch molecules. This binding is mediated through a carbohydrate-binding module (CBM), which is a common feature in proteins involved in carbohydrate metabolism. The CBM allows SBD1 to interact with starch granules, making it an effective tool for targeting and manipulating starch in various biological processes .
One of the primary applications of SBD1 is in the purification of recombinant proteins. By fusing SBD1 to a target protein, researchers can exploit its starch-binding properties to isolate and purify the protein of interest. This method offers several advantages over traditional purification techniques, including:
- Cost-effectiveness: Starch is an inexpensive and readily available material, making it a cost-effective matrix for protein purification.
- Efficiency: The strong binding affinity of SBD1 for starch ensures efficient capture and recovery of the target protein.
- Versatility: SBD1 can be used to purify a wide range of proteins from different sources .
The mechanism by which SBD1 facilitates protein purification involves the following steps:
- Fusion Protein Expression: The gene encoding the target protein is fused with the gene encoding SBD1, resulting in the expression of a fusion protein.
- Binding to Starch: The fusion protein is mixed with a starch-containing matrix, allowing SBD1 to bind to the starch granules.
- Washing and Elution: The matrix is washed to remove non-specifically bound proteins, and the fusion protein is subsequently eluted using a suitable buffer .
Recent studies have demonstrated the potential of SBD1 in various biotechnological applications. For instance, researchers have successfully used SBD1 to purify proteins from crude bacterial extracts using raw starch from different sources such as rice, corn, potato, and barley . This highlights the versatility and effectiveness of SBD1 as an affinity tag for recombinant protein purification.
