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GeneBio Systems

Recombinant Rhipicephalus sanguineus Evasin-3

Recombinant Rhipicephalus sanguineus Evasin-3

SKU:P0C8E8

Regular price $1,239.30 CAD
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Size: 100ug. Other sizes are also available.

Activity: Not tested

Research Areas: Others

Uniprot ID: P0C8E8

Gene Names: N/A

Alternative Name(s): (EVA3)

Abbreviation: Recombinant Rhipicephalus sanguineus Evasin-3 protein

Organism: Rhipicephalus sanguineus (Brown dog tick) (Ixodes sanguineus)

Source: E.coli

Expression Region: 21-86aa

Protein Length: Full Length of Mature Protein

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

Target Protein Sequence: LVSTIESRTSGDGADNFDVVSCNKNCTSGQNECPEGCFCGLLGQNKKGHCYKIIGNLSGEPPVVRR

MW: 14.4 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: Stabilizes the aggregates of proteoglycan monomers with hyaluronic acid in the extracellular cartilage matrix.

Reference: "The brain link protein-1 (BRAL1): cDNA cloning, genomic structure, and characterization as a novel link protein expressed in adult brain." Hirakawa S., Oohashi T., Su W.-D., Yoshioka H., Murakami T., Arata J., Ninomiya Y. Biochem. Biophys. Res. Commun. 276: 982-989(2000)

Function:

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