Recombinant Sphingobium sp. Beta-etherase (ligE)

SKU: P27457

Size: 100ug. Other sizes are also available.

Activity: Not tested

Research Areas: Others

Uniprot ID: P27457

Gene Names: ligE

Alternative Name(s): (Beta-aryl ether cleaving enzyme)

Abbreviation: Recombinant Sphingobium sp. ligE protein

Organism: Sphingobium sp. (strain NBRC 103272 / SYK-6)

Source: E.coli

Expression Region: 2-281aa

Protein Length: Full Length of Mature Protein

Tag Info: C-terminal 6xHis-tagged

Target Protein Sequence: ARNNTITLYDLQLESGCTISPYVWRTKYALKHKGFDIDIVPGGFTGILERTGGRSERVPVIVDDGEWVLDSWVIAEYLDEKYPDRPMLFEGPTQKNLMKFLDNWLWSTAVGPWFRCYILDYHDLSLPQDRDYVRWSREQWFLGGQRLEDVQAGREDRLPLVPPTLEPFRRILAETKWLGGDQPNFADYSALAVFLWTASVARTPPLTEDDPLRDWLDRGFDLFDGLGRHPGMNPLFGLKLREGDPEPFVRQTGPAGAGGQALNKGPQTTKMPPRVAEKAD

MW: 38.8 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: Able to degrade various dimeric lignin compounds. Catalyzes the unique and reductive cleavage of arylglycerol-beta-aryl ether.

Reference: "Structural Basis of Stereospecificity in the Bacterial Enzymatic Cleavage of beta-Aryl Ether Bonds in Lignin." Helmich K.E., Pereira J.H., Gall D.L., Heins R.A., McAndrew R.P., Bingman C., Deng K., Holland K.C., Noguera D.R., Simmons B.A., Sale K.L., Ralph J., Donohue T.J., Adams P.D., Phillips G.N. Jr. J Biol Chem 291: 5234-5246(2016)

Function: