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GeneBio Systems

Recombinant Dendroaspis polylepis polylepis Kunitz-type serine protease inhibitor dendrotoxin E

Recombinant Dendroaspis polylepis polylepis Kunitz-type serine protease inhibitor dendrotoxin E

SKU:P00984

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Size: 100ug. Other sizes are also available.

Activity: Not tested

Research Areas: Others

Uniprot ID: P00984

Gene Names: N/A

Alternative Name(s): (DTX-E)(Venom basic protease inhibitor E)

Abbreviation: Recombinant Dendroaspis polylepis polylepis DTX-E protein

Organism: Dendroaspis polylepis polylepis (Black mamba)

Source: Mammalian cell

Expression Region: 1-59aa

Protein Length: Full Length

Tag Info: C-terminal hFc1-tagged

Target Protein Sequence: LQHRTFCKLPAEPGPCKASIPAFYYNWAAKKCQLFHYGGCKGNANRFSTIEKCRHACVG

MW: 35.5 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: Serine protease inhibitor that inhibits trypsin (Kd=1 nM) and chymotrypsin (Kd=100 nM). May also inhibit voltage-gated potassium channels (Kv). Binds transition metal ions such as copper and cobalt.

Reference: "Snake venoms. The amino-acid sequence of trypsin inhibitor E of Dendroaspis polylepis polylepis (black mamba) venom." Joubert F.J., Strydom D.J. Eur. J. Biochem. 87: 191-198(1978)

Function:

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