GeneBio Systems
Recombinant Aspergillus terreus Blasticidin-S deaminase (bsd)
Recombinant Aspergillus terreus Blasticidin-S deaminase (bsd)
SKU:P0C2P0
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Size: 100ug. Other sizes are also available.
Activity: Not tested
Research Areas: Microbiology
Uniprot ID: P0C2P0
Gene Names: bsd
Alternative Name(s):
Abbreviation: Recombinant Aspergillus terreus bsd protein
Organism: Aspergillus terreus
Source: Yeast
Expression Region: 1-130aa
Protein Length: Full Length
Tag Info: C-terminal 6xHis-tagged
Target Protein Sequence: MPLSQEESTLIERATATINSIPISEDYSVASAALSSDGRIFTGVNVYHFTGGPCAELVVLGTAAAAAAGNLTCIVAIGNENRGILSPCGRCRQVLLDLHPGIKAIVKDSDGQPTAVGIRELLPSGYVWEG
MW: 14.5 kDa
Purity: Greater than 90% as determined by SDS-PAGE.
Endotoxin: Not test
Biological_Activity:
Form: Liquid or Lyophilized powder
Buffer: If 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, pH 8.0.
Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.
Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.
Relevance: Catalyzes the deamination of the cytosine moiety of the antibiotics blasticidin S, cytomycin and acetylblasticidin S.
Reference: "Expression, purification, and characterization of blasticidin S deaminase (BSD) from Aspergillus terreus: the role of catalytic zinc in enzyme structure." Kimura M., Sekido S., Isogai Y., Yamaguchi I. J. Biochem. 127: 955-963(2000)
Function:
