1 1

ACHE/Acetylcholinesterase His Tag Protein, Human

ACHE/Acetylcholinesterase His Tag Protein, Human

Catalog Number: UA011275 Brand: UA BIOSCIENCE
Share:
Price:
$415 USD
$415 USD
Size:

For shipping services or bulk orders, you may request a quotation.
Secure checkout with
View full details

Product Details

Product Specification


Species Human
Synonyms ARACHE,apoptosis-related acetylcholinesterase,N-ACHE
Accession P22303-1
Amino Acid Sequence

Glu32-Leu614 with His Tag at the C-Terminus
Expression System HEK293
Molecular Weight

65-80kDa (Reducing)
Purity ＞90% by SDS-PAGE
Conjugation Unconjugated
Tag His Tag
Physical Appearance Lyophilized powder
Storage Buffer

PBS, PH7.4, 5% trehalose
Reconstitution

Reconstitute at 0.1-1 mg/ml according to the size in ultrapure water after rapid centrifugation.
Stability & Storage

· 12 months from date of receipt, lyophilized powder stored at -20 to -80℃.
· 3 months, -20 to -80℃ under sterile conditions after reconstitution.
· 1 week, 2 to 8℃ under sterile conditions after reconstitution.
· Please avoid repeated freeze-thaw cycles.
Reference

1.Rawat K, Tewari D, Bisht A, Chandra S, Tiruneh YK, Hassan HM, Al-Emam A, Sindi ER, Al-Dies AM. Identification of AChE targeted therapeutic compounds for Alzheimer's disease: an in-silico study with DFT integration. Sci Rep. 2024 Dec 5;14(1):30356.
2.Reynoso-García MF, Nicolás-Álvarez DE, Tenorio-Barajas AY, Reyes-Chaparro A. Structural Bioinformatics Applied to Acetylcholinesterase Enzyme Inhibition. Int J Mol Sci. 2025 Apr 17;26(8):3781.

Background

Acetylcholinesterase (AChE), also known as acetylhydrolase, is a crucial serine hydrolase that efficiently terminates signal transmission at neuromuscular junctions and cholinergic synapses by rapidly hydrolyzing acetylcholine (ACh) in the synaptic cleft. Beyond its fundamental role in neurotransmitter regulation, AChE has been found to participate in neuronal apoptosis and other cellular processes, suggesting a broader involvement in programmed cell death. In neurodegenerative diseases such as Alzheimer's disease, acetylcholine deficiency is closely associated with cognitive decline, making AChE an important therapeutic target. Currently, acetylcholinesterase inhibitors (AChEIs) are widely used in clinical practice for the targeted treatment of Alzheimer's disease and other forms of dementia.

Protocol

 

Experimental Method

Principle: Detect the ability of ACHE protein to cleave Acetylthiocholine.

Materials

  1. Assay buffer: 0.1 M Sodium Phosphate, 0.05% (w/v) Brij-35, pH 7.5

  2. ACHE/Acetylcholinesterase His Tag Protein, Human (SPA1701)

  3. Substrate: Acetylthiocholine (ATC) (A5626)

  4. 5’,5’-Dithiobis (2-nitrobenzoic acid) (DTNB) (D8130)

  5. 96 Well Clear Plate (701311)

  6. Plate reader (PerkinElmer, 405 nm)

Procedure

  1. Dilute ACHE protein to 0.02 μg/mL in assay buffer.

  2. Dilute substrate to 200 μM in assay buffer containing 100 μM DTNB.

  3. Add 50 μL of diluted ACHE protein to the clear plate. Include a control group with assay buffer instead of ACHE protein.

  4. Add 50 μL of substrate/DTNB mixture to initiate the reaction.

  5. Read the signal at 405 nm in kinetic mode for 10 minutes.

  6. Calculate specific activity:

Specific Activity (pmol/min/µg) =

Adjusted Vmax* (OD/min) x well volume (L) x 109 nmol/mol

ext. coeff** (M--1cm--1) x path corr.*** (cm) 

x amount of enzyme (μg)

*Substrate blank correction

**Extinction coefficient 13260 M⁻¹cm⁻¹

***Path length correction 0.32 cm

Picture

SDS-PAGE

2μg (R: reducing condition, N:non-reducing condition).