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C255

Recombinant Human Protein CutA/CUTA

10ug

1200

1080

现货

国产

C255

Recombinant Human Protein CutA/CUTA

50ug

3520

3168

现货

国产

C255

Recombinant Human Protein CutA/CUTA

500ug

12320

11088

现货

国产

C255

Recombinant Human Protein CutA/CUTA

1mg

17600

15840

现货

国产

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  • Catalog# C255
    Source E.coli
    Description Recombinant Human Protein CutA/CUTA is produced by our E. coli expression system. The target protein is expressed with sequence (Met1-Pro156) of Human CUTA fused with a His tag at the C-terminus.
    Names Protein CutA, Acetylcholinesterase-Associated Protein, Brain Acetylcholinesterase Putative Membrane Anchor, CUTA, ACHAP, C6orf82
    Accession # O60888
    Formulation Lyophilized from a 0.2 μm filtered solution of 20mM Tris-HCl, 1mM DTT, pH 8.0
    Shipping The product is shipped at ambient temperature.
    Reconstitution Always centrifuge tubes before opening. Do not mix by vortex or pipetting.
    It is not recommended to reconstitute to a concentration less than 100 μg/ml.
    Dissolve the lyophilized protein in 1X PBS.
    Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
    Storage Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks.
    Reconstituted protein solution can be stored at 4-7°C for 2-7 days.
    Aliquots of reconstituted samples are stable at < -20°C for 3 months.
    Purity Greater than 95% as determined by reducing SDS-PAGE.
    Endotoxin Less than 0.1 ng/μg (1 IEU/μg).
    Amino Acid Sequence
    MPALLPVASRLLLLPRVLLTMASGSPPTQPSPASDSGSGYVPGSVSAAFVTCPNEKVAKEIARAV VEKRLAACVNLIPQITSIYEWKGKIEEDSEVLMMIKTQSSLVPALTDFVRSVHPYEVAEVIALPV EQGNFPYLQWVRQVTESVSDSITVLPLEHHHHHH
    Background Protein CutA (CUTA) posseses a signal peptide and is widely expressed in brain. CUTA may forms part of a complex of membrane proteins attached to acetylcholinesterase (AChE). CUTA takes part in cellular tolerance to a broad range of divalent cations other than copper. Alternate transcriptional splice variants, both protein-coding and non-protein-coding, have been found.