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Recombinant Streptomyces albus Valine dehydrogenase (vdh)

Recombinant Streptomyces albus Valine dehydrogenase (vdh) — Oxidative deamination of branched-chain amino acids. Purity >95%.

SKU: BCRECP-004717 Categories: ,

Product Specifications

Product SkuBCRECP-004717
Product DescriptionRecombinant Streptomyces albus Valine dehydrogenase (vdh) Protein is expressed from E.coli with C-terminal 6xHis-tagged. It contains 2-364aa. [Accession | O69056].
Uniprot No.O69056
Gene Namesvdh
PurityGreater than 95% as determined by SDS-PAGE.
Expression SystemE.coli
Expression Region2-364aa
SpeciesStreptomyces albus (strain ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 / NBRC 107858)
Tag InfoC-terminal 6xHis-tagged
Molecular weight45.2kDa
ActivityPlease contact us to obtain bioactivity data.
BufferIf the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.
StorageStore at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Research AreasOthers

Function

Oxidative deamination of branched-chain amino acids. Oxidizes L-valine and L-alpha-aminobutyric acid efficiently, and L-alanine and L-isoleucine less efficiently. D-valine and L-glutamate were not substrates for the enzyme.

Biological Context

Pathway: Amino-acid degradation; L-valine degradation

Product Specifications

Recombinant Streptomyces albus Valine dehydrogenase (vdh) is a recombinant protein, expressed in E.coli, covering amino acids 2-364aa, with C-terminal 6xHis-tagged tag, molecular weight 45.2kDa, purity Greater than 95% as determined by SDS-PAGE.. Suitable for ELISA and Western Blot applications.

Recommended applications depend on the target, product format, and product-specific validation data. Refer to the product datasheet or Certificate of Analysis (CoA), or contact BioCrest Sci for application guidance.

Biological Activity: Please contact us to obtain bioactivity data.

Storage: Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shipping & Lead Time: Availability, shipping conditions, and estimated lead time are confirmed in the formal quotation or order confirmation based on the product format, destination, and order requirements.

Protein Biology

Function

Oxidative deamination of branched-chain amino acids. Oxidizes L-valine and L-alpha-aminobutyric acid efficiently, and L-alanine and L-isoleucine less efficiently. D-valine and L-glutamate were not substrates for the enzyme. The catabolism of valine is the major source of fatty acid precursors for macrolide biosynthesis and a vital source of antibiotic precursors

Pathway

Amino-acid degradation; L-valine degradation

Gene: vdh  |  Organism: Streptomyces albus (strain ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 / NBRC 107858)

Frequently Asked Questions

How do I order or inquire about this product?

Submit the Online Inquiry form with your required quantity and specifications, or email sales@biocrestsci.com. Available sizes, pricing, stock status, documentation, and estimated lead time are confirmed in the formal quotation.

What is the shipping and delivery time?

Availability, dispatch timing, shipping conditions, and delivery estimates depend on the product format, destination, and order requirements. These details are confirmed in the formal quotation or order confirmation.

How should this product be stored?

Follow the storage and handling instructions in the product-specific datasheet and Certificate of Analysis (CoA). Requirements may vary by product form and formulation; contact BioCrest Sci if product-specific guidance is needed.

What quality controls are performed on your products?

Quality-control data such as identity, purity, endotoxin level, or biological activity are provided only when specified on this product page, the datasheet, or Certificate of Analysis (CoA). Biological activity is not implied unless explicitly stated.

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