Rat Acetylcholinesterase (AChE) Protein

Este producto es parte de AChE - Acetylcholinesterase
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2626€ (1 mg)

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935106861
info@markelab.com
name
Rat Acetylcholinesterase (AChE) Protein
category
Proteins and Peptides
provider
Abbexa
reference
abx065084
tested applications
WB, SDS-PAGE

Description

Recombinant Acetylcholinesterase (AchE) is a recombinant Rat protein produced in a Prokaryotic expression system (E. coli).

Documents del producto

Instrucciones
Data sheet
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Product specifications

Category
Proteins and Peptides
Immunogen Target
Acetylcholinesterase (AChE)
Host
E. coli
Origin
Rat
Conjugation
Unconjugated
Observed MW
Molecular Weight: Calculated MW: 20.2 kDa
Concentration: Prior to lyophilization: 200 µg/ml
Sequence Fragment: Gly157-Pro332
Tag: N-terminal His tag
Expression
Recombinant
Purity
> 95%
Size 1
1 mg
Size 2
5 mg
Form
Lyophilized To keep the original salt concentration, we recommend reconstituting to the original concentration prior to lyophilization (see Concentration) in ddH2O. If a lower concentration is required, dilute in PBS, pH 7.4. If a higher concentration is required, the product can be reconstituted directly in PBS, pH 7.4, though please note that this will change the overall salt concentration. The stock concentration should be between 0.1-1.0 mg/ml. Do not vortex.
Tested Applications
WB, SDS-PAGE
Buffer
Prior to lyophilization: PBS, pH 7.4, containing 0.01% Sarcosyl, 1 mM DTT, 5% Trehalose and Proclin-300.
Availability
Shipped within 1-2 months.
Storage
Store at 2-8 °C for up to one month. Store at -80 °C for up to one year. Avoid repeated freeze/thaw cycles.
Dry Ice
No
UniProt ID
P37136
Alias
YT,ACEE,ARACHE,N-ACHE
Background
Protein AChE
Status
RUO
Note
This product is for research use only.   Not for human consumption, cosmetic, therapeutic or diagnostic use.

Descripción

Acetylcholinesterase (AChE) is an enzyme that plays a critical role in the nervous system by breaking down the neurotransmitter acetylcholine. AChE is a globular protein, typically found as a tetramer composed of four subunits. Each subunit contains a catalytic site responsible for the enzymatic breakdown of acetylcholine. Acetylcholine is involved in transmitting signals across synapses, which are the gaps between nerve cells. After acetylcholine has transmitted its signal, AChE rapidly breaks it down into its constituent parts: choline and acetate. This breakdown process is crucial for terminating the signal transmission and allowing the nerve cell to return to its resting state . AChE is found primarily at cholinergic synapses, where acetylcholine is released as a neurotransmitter. These synapses are abundant in the central nervous system (CNS) and the peripheral nervous system (PNS). At neuromuscular junctions, AChE is particularly important for allowing muscles to relax after contraction. When a motor neuron releases acetylcholine to signal muscle contraction, AChE quickly degrades the acetylcholine, allowing the muscle to relax. AChE activity can be regulated through various mechanisms, including gene expression, post-translational modifications, and interactions with other proteins. Dysregulation of AChE activity has been implicated in various neurological disorders, including Alzheimer's disease and myasthenia gravis.

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