ACHE Human
HEK293 Cells.
AChE, ACEE, ACES_HUMAN, Acetylcholinesterase, ACHE, ARACHE, N-ACHE, VT, Acetylcholinesterase isoform E4-E6
Sterile Filtered colorless solution.
Greater than 95.0% as determined by SDS-PAGE.
Description
ACHE Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (32-614 a.a) containing a total of 592 amino acids, having a molecular mass of 65.6 kDa.
ACHE is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Product Specs
Acetylcholinesterase (ACHE), a member of the type-B carboxylesterase/lipase family, is an enzyme responsible for breaking down the neurotransmitter acetylcholine, as well as other choline esters. In the process of neurotransmission, ACHE plays a crucial role in terminating the signal transmission. After acetylcholine is released from the presynaptic neuron into the synaptic cleft and binds to ACH receptors on the post-synaptic membrane to transmit the nerve signal, ACHE, located on the post-synaptic membrane, hydrolyzes ACH, thereby ending the signal transmission.
Recombinant human ACHE, produced in HEK cells, is a single, glycosylated polypeptide chain with a molecular weight of 65.6 kDa. The chain consists of 592 amino acids (32-614 a.a). The ACHE protein has a 6 amino acid His-tag fused at its C-terminus and undergoes purification using proprietary chromatographic methods.
The product is a colorless solution that has been sterilized by filtration.
The ACHE solution has a concentration of 0.25mg/ml and contains 10% Glycerol and Phosphate-Buffered Saline with a pH of 7.4.
For optimal storage, keep the ACHE vial at 4°C if you plan to use it within 2-4 weeks. For longer storage, it should be frozen at -20°C. To ensure stability during long-term storage, adding a carrier protein (0.1% HSA or BSA) is recommended. Avoid repeatedly freezing and thawing the product.
The purity of the ACHE is determined by SDS-PAGE analysis and is greater than 95.0%.
The specific activity of ACHE is determined by measuring the amount of enzyme required to cleave 1 nmole of acetylthiocholine per minute at a pH of 7.5 and a temperature of 25°C. This activity is greater than 6,000 nmol/min/ug.
AChE, ACEE, ACES_HUMAN, Acetylcholinesterase, ACHE, ARACHE, N-ACHE, VT, Acetylcholinesterase isoform E4-E6
HEK293 Cells.
DGSEGREDAE LLVTVRGGRL RGIRLKTPGG PVSAFLGIPF AEPPMGPRRF LPPEPKQPWS GVVDATTFQS VCYQYVDTLY PGFEGTEMWN PNRELSEDCL YLNVWTPYPR PTSPTPVLVW IYGGGFYSGA SSLDVYDGRF LVQAERTVLV SMNYRVGAFG FLALPGSREA PGNVGLLDQR LALQWVQENV AAFGGDPTSV TLFGESAGAA SVGMHLLSPP SRGLFHRAVL QSGAPNGPWA TVGMGEARRR ATQLAHLVGC PPGGTGGNDT ELVACLRTRP AQVLVNHEWH VLPQESVFRF SFVPVVDGDF LSDTPEALIN AGDFHGLQVL VGVVKDEGSY FLVYGAPGFS KDNESLISRA EFLAGVRVGV PQVSDLAAEA VVLHYTDWLH PEDPARLREA LSDVVGDHNV VCPVAQLAGR LAAQGARVYA YVFEHRASTL SWPLWMGVPH GYEIEFIFGI PLDPSRNYTA EEKIFAQRLM RYWANFARTG DPNEPRDPKA PQWPPYTAGA QQYVSLDLRP LEVRRGLRAQ ACAFWNRFLP KLLSATDTLD EAERQWKAEF HRWSSYMVHW KNQFDHYSKQ DRCSDLHHHH HH
Product Science Overview
Recombinant human acetylcholinesterase (rhAChE) is a fast-acting enzyme with a molecular weight of approximately 67,796 Da per subunit, forming a homodimer with a total molecular weight of 135,792 Da . Each subunit consists of 556 residues, resulting in a total of 1,112 residues for the dimer . The enzyme’s primary structure includes a high number of aromatic residues, along with positively and negatively charged residues, which are integral to its function .
The secondary structure of rhAChE contains 12 β-sheets, 14 α-helices, and 74 random coils . The tertiary structure features an α/β hydrolase fold, a common motif in many hydrolytic enzymes, providing a stable scaffold for the active site . This fold consists of a mostly parallel, eight-stranded β-sheet surrounded by α-helices .
AChE’s primary role is to terminate cholinergic neurotransmission by hydrolyzing acetylcholine, thus preventing continuous stimulation of neurons . This function is vital for maintaining the balance and proper functioning of the nervous system. Additionally, AChE is involved in neuronal apoptosis, further highlighting its importance in neural health .
Recombinant human acetylcholinesterase has been extensively studied for its potential therapeutic applications, particularly in treating neurological disorders such as Alzheimer’s disease . AChE inhibitors are used to slow down the breakdown of acetylcholine in the brain, thereby enhancing cholinergic transmission and potentially alleviating symptoms of dementia .
