Recombinant Nepenthes distillatoria Aspartic proteinase nepenthesin-1 (X20S,X45S,X48S,X51S,X53S,X98S,X107S), partial

SKU: P69476

Size: 100ug. Other sizes are also available.

Activity: Not tested

Research Areas: Others

Uniprot ID: P69476

Gene Names: N/A

Alternative Name(s): (Nepenthesin-I)

Abbreviation: Recombinant Nepenthes distillatoria Nepenthesin-I protein (Mutant type), partial

Organism: Nepenthes distillatoria (Pitcher plant)

Source: E.coli

Expression Region: 1-164aa(X20N,X45C,X48C,X51C,X53N,X98C,X107S)

Protein Length: Partial

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

Target Protein Sequence: IGPSGVETTVYAGDGEYLMNLSIGTPAQPFSAIMDTGSDLIWTQCQPCTQCFNQSDPQGSSSFSTLPCGYGDSETQGSMGTETFTFGSVSIPNITFGCGEGPLPLPSQLDVAKYITLDLPIDPSAFDLCFQTPSDPSNLQIPTFVMHFDTGNSVVSFVSAQCGA

MW: 24.7 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: Extracellular proteinase found in the pitcher fluid of carnivorous plants. Digest prey for nitrogen uptake.

Reference: "Enzymic and structural characterization of nepenthesin, a unique member of a novel subfamily of aspartic proteinases." Athauda S.B.P., Matsumoto K., Rajapakshe S., Kuribayashi M., Kojima M., Kubomura-Yoshida N., Iwamatsu A., Shibata C., Inoue H., Takahashi K. Biochem. J. 381: 295-306(2004)

Function: