Recombinant Escherichia coli Hygromycin-B 4-O-kinase (hph), Escherichia coli, E.coli, N-terminal 6xHis-tagged, 42.0kDa, purity >85% as determined by SDS-PAGE.
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Recombinant Escherichia coli Hygromycin-B 4-O-kinase (hph)

Recombinant Escherichia coli Hygromycin-B 4-O-kinase (hph) — The aminoglycoside phosphotransferases achieve inactivation of their antibiotic substrates by phosphorylation. Purity >85%.

SKU: BCRECP-003015 Categories: , ,
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Product Specifications

Product SkuBCRECP-003015
Product DescriptionRecombinant Escherichia coli Hygromycin-B 4-O-kinase (hph) Protein is expressed from E.coli with N-terminal 6xHis-tagged. It contains 1-341aa. [Accession | P00557].
Uniprot No.P00557
Gene Nameshph
PurityGreater than 85% as determined by SDS-PAGE.
Expression SystemE.coli
Expression Region1-341aa
SpeciesEscherichia coli
Tag InfoN-terminal 6xHis-tagged
Molecular weight42.0kDa
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

The aminoglycoside phosphotransferases achieve inactivation of their antibiotic substrates by phosphorylation. Only phosphorylates hygromycin and closely related compounds such as demethyl analogs and destomycin.

Product Specifications

Recombinant Escherichia coli Hygromycin-B 4-O-kinase (hph) is a recombinant protein from Escherichia coli, expressed in E.coli, covering amino acids 1-341aa, with N-terminal 6xHis-tagged tag, molecular weight 42.0kDa, purity Greater than 85% as determined by SDS-PAGE.. Suitable for ELISA and Western Blot applications.

SDS-PAGE: Single band at expected molecular weight confirming purity.

ELISA: Suitable as coating antigen or detection standard.

Western Blot: Compatible with standard Western Blot protocols.

Protein Interaction: Validated for SPR (Surface Plasmon Resonance) and BLI (Bio-Layer Interferometry) studies.

Shipping: Shipped at ambient temperature. Lyophilized protein is stable during transit.

Storage: Store lyophilized protein at -20°C to -80°C. Reconstituted protein should be aliquoted and stored at -80°C. Avoid repeated freeze-thaw cycles.

Shelf Life: 12 months from date of receipt when stored as recommended.

Shipping Time: Orders placed before 2 PM EST ship same day. International orders typically deliver within 5-10 business days.

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Protein Biology

Function

The aminoglycoside phosphotransferases achieve inactivation of their antibiotic substrates by phosphorylation. Only phosphorylates hygromycin and closely related compounds such as demethyl analogs and destomycin

Gene: hph  |  Organism: Escherichia coli  |  Synonyms: APH(4); Hygromycin B phosphotransferase; Hygromycin-B kinase

Frequently Asked Questions

How do I order or inquire about this product?

Fill out the Online Inquiry form with your required quantity and specifications. You can also email sales@biocrestsci.com. Our team typically responds within 4 business hours with a quote and availability confirmation.

What is the shipping and delivery time?

Orders placed before 2 PM EST ship the same day. Domestic (US) delivery typically takes 2-3 business days. International orders deliver within 5-10 business days. All products are shipped at ambient temperature with appropriate packaging to ensure stability.

How should I store this recombinant protein?

Lyophilized proteins should be stored at -20°C to -80°C upon receipt. After reconstitution, aliquot and store at -80°C. Avoid repeated freeze-thaw cycles. Shelf life is 12 months from date of receipt when stored as recommended.

What quality controls are performed on your products?

Each product undergoes SDS-PAGE purity analysis (typically >85-95%), endotoxin testing, and bioactivity validation. Products are validated for ELISA, Western Blot, and SPR/BLI applications as specified on this product page. A Certificate of Analysis (CoA) is available upon request.

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