Recombinant Pleurotus eryngii Versatile peroxidase VPL1 (vpl1)

SKU: Q9UR19

Size: 100ug. Other sizes are also available.

Activity: Not tested

Research Areas: Others

Uniprot ID: Q9UR19

Gene Names: vpl1

Alternative Name(s): (Versatile liquid phase peroxidase 1)

Abbreviation: Recombinant Pleurotus eryngii vpl1 protein

Organism: Pleurotus eryngii (Boletus of the steppes)

Source: E.coli

Expression Region: 31-361aa

Protein Length: Full Length of Mature Protein

Tag Info: N-terminal 10xHis-tagged and C-terminal Myc-tagged

Target Protein Sequence: ATCADGRTTANAACCVLFPILDDIQENLFDGAQCGEEVHESLRLTFHDAIGFSPTLGGGGADGSIIAFDTIETNFPANAGIDEIVSAQKPFVAKHNISAGDFIQFAGAVGVSNCPGGVRIPFFLGRPDAVAASPDHLVPEPFDSVDSILARMSDAGFSPVEVVWLLASHSIAAADKVDPSIPGTPFDSTPGVFDSQFFIETQLKGRLFPGTADNKGEAQSPLQGEIRLQSDHLLARDPQTACEWQSMVNNQPKIQNRFAATMSKMALLGQDKTKLIDCSDVIPTPPALVGAAHLPAGFSLSDVEQACAATPFPALTADPGPVTSVPPVPGS

MW: 42.0 kDa

Purity: Greater than 85% 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: A versatile ligninolytic peroxidase that combines the substrate specificity characteristics of the two other ligninolytic peroxidases, manganese peroxidase and lignin peroxidase.

Reference: "Molecular characterization of a novel peroxidase isolated from the ligninolytic fungus Pleurotus eryngii." Ruiz-Duenas F.J., Martinez M.J., Martinez A.T. Mol. Microbiol. 31: 223-235(1999)

Function: