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Conditions of optimal ACHAP Enzyme performance should be determined experimentally by the investigator.
Price/availability/specifications subject to change without notice. Unless otherwise indicated, our catalog and customized products are for research use only and not intended for human or animal diagnostic or therapeutic use.
Phone: 1-617-401-8149
Fax: 1-617-606-5019
Email: message@sydlabs.com
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Introduction
CUTA, also known as Acetylcholinesterase-associated protein, ACHAP, Brain acetylcholinesterase putative membrane anchor and C6orf82, belongs to the CutA family. CUTA posses 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.
BP001162-C255: Recombinant Human Acetylcholinesterase-associated protein (ACHAP)
Source: E. coli-derived.
Recombinant Human Acetylcholinesterase-associated protein (ACHAP) is expressed with sequence (Met1-Pro156) of Human CUTA fused with a His tag at the C-terminus.
Purity: > 95% by reducing SDS-PAGE.
Endotoxin: < 0.1 ng/ug (1 EU/ug).
Formulation: Lyophilized from a 0.2 um filtered solution of 20 mM Tris-HCl, 1 mM DTT, pH 8.0.
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 ug/ml. Dissolve the lyophilized protein in 1X PBS. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Shipping: The product is shipped with ice pack. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70°C as supplied.
1 month, 2 to 8°C under sterile conditions after reconstitution.
3 months, -20 to -70°C under sterile conditions after reconstitution.
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