Acetylcholinesterase/ACHE Protein, Human (CHO, His)
Based on 1 Customer Validation
Acetylcholinesterase (ACHE) protein is pivotal in neurotransmission, rapidly hydrolyzing acetylcholine in the synaptic cleft to terminate signal transduction at the neuromuscular junction. Beyond neurotransmitter regulation, ACHE is implicated in neuronal apoptosis, indicating a broader role in cellular processes associated with programmed cell death. Acetylcholinesterase/ACHE Protein, Human (CHO, His) is the recombinant human-derived Acetylcholinesterase/ACHE protein, expressed by CHO , with C-6*His labeled tag.
- Species: Human
- Source: CHO
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Storage:Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
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Tel: 609-228-6898 E-mail: [email protected] [email protected]
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Biological Activity
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Technical Parameters
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Product Properties
- Documentation
- Help & FAQs
Biological Activity
Description
Acetylcholinesterase (ACHE) protein is pivotal in neurotransmission, rapidly hydrolyzing acetylcholine in the synaptic cleft to terminate signal transduction at the neuromuscular junction. Beyond neurotransmitter regulation, ACHE is implicated in neuronal apoptosis, indicating a broader role in cellular processes associated with programmed cell death. Acetylcholinesterase/ACHE Protein, Human (CHO, His) is the recombinant human-derived Acetylcholinesterase/ACHE protein, expressed by CHO , with C-6*His labeled tag.
Background
Acetylcholinesterase (ACHE) protein plays a crucial role in neurotransmission by rapidly hydrolyzing the acetylcholine neurotransmitter in the synaptic cleft, thereby facilitating the termination of signal transduction at the neuromuscular junction. Beyond its essential function in neurotransmitter regulation, ACHE is implicated in neuronal apoptosis, suggesting a broader role in cellular processes related to programmed cell death.
Verified Bioactivity
Measured by its ability to cleave Acetylthiocholine that incubate at room temperature in kinetic mode for 5 minutes. The specific activity is > 500 nmol/min/μg.
MCE Validation Data
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Purity - SDS-PAGE
Purity - SDS-PAGE
Assay Procedure
Materials
Acetylcholinesterase/ACHE Protein, Human (CHO, His) (HY-P79277)
Assay buffer: 0.1 M Sodium Phosphate with 0.05% Brij-35, pH 7.5
DTNB (HY-15915): Dissolve in DMSO to 10 mM, then dilute to 100 μM with assay buffer
Substrate Mixture: First dilute ATC in DMSO to 20 mM, then dilute ATC to 200 μM with 100 μM DTNB to prepare the substrate mixture
Procedure
1. Dilute ACHE protein to 0.002 μg/mL and 0.02 μg/mL respectively with buffer.
2. Add 50 μL of ACHE protein buffer at different concentrations to a 96-well plate, then add 50 μL of substrate to initiate the reaction, with 3 replicates per group, and a blank control containing 50 μL of buffer and 50 μL of substrate mixture.
3. Zero the microplate reader using the OD value of the blank group, and read the absorbance at 405 nm in kinetic mode for 5 min.
4. Calculate the specific activity:
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Specific Activity (pmol/min/μg) = |
Adjusted Vmax* (OD/min) × well volume (L) × 1012 pmol/mol |
| ext. coeff **(M-1 cm-1) × path corr.*** (cm) × amount of enzyme (μg) |
* Adjusted for substrate blank
**Extinction coefficient: 13260 M-1 cm-1
*** Path correction: 0.32 cm
Per Well:
Human ACHE: 0.0001 μg
DTNB: 50 μM
ATC: 100 μM
Technical Parameters
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Species Human
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Source CHO
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Tag C-6*His
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Accession
P22303-1 (E32-L614)
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Molecular Construction
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N-term
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ACHE (E32-L614)
Accession # P22303 -
6*His
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C-term
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Protein Length
Full Length of Isoform-1
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Synonyms
ACHE; Apoptosis-Related Acetylcholinesterase; Prev. YT; ARACHE; Acetylcholinesterase; N-ACHE; Acetylcholinesterase (Cartwright Blood Group); ACEE; Yt Blood Group; AChE; N-Terminal Extended Acetylcholinesterase; Acetylcholinesterase (Yt Blood Group); Carbo
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AA Sequence
EGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL
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Molecular Weight
Approximately 60-80 kDa, based on SDS-PAGE under reducing conditions.
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Glycosylation
Yes
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Purity
≥ 95%, as determined by reducing SDS-PAGE.
Product Properties
Lyophilized powder.
1.Lyophilized from a 0.22 μm filtered solution of 20 mM Tris, 150 mM NaCl, pH 7.4.
2.Lyophilized from a 0.22 μm filtered solution of 20 mM Tris-HCl, 150 mM NaCl, pH 7.4, 8% trehalose.
Please refer to the lot-specific COA for specific buffer information.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.
<1 EU/μg, determined by LAL method.
It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH2O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).
Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
Room temperature in continental US; may vary elsewhere.
Documentation
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Data Sheet (239 KB)
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SDS (252 KB)
- English - EN (252 KB)
- Français - FR (252 KB)
- Deutsch - DE (252 KB)
- Norwegian - NO (252 KB)
- Español - ES (252 KB)
- Swedish - SV (252 KB)
- Italian - IT (252 KB)
- Korean - KR (252 KB)
- Portuguese - PT (252 KB)
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Handling Instructions (2659 KB)
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)
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