Recombinant Rat Acetylcholinesterase (ACHE) Protein (His)

Beta LifeScience SKU/CAT #: BLC-01114P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Rat Acetylcholinesterase (ACHE) Protein (His)

Beta LifeScience SKU/CAT #: BLC-01114P
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Product Overview

Description Recombinant Rat Acetylcholinesterase (ACHE) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb P37136
Target Symbol ACHE
Synonyms (AChE)
Species Rattus norvegicus (Rat)
Expression System E.coli
Tag N-6His
Target Protein Sequence EGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL
Expression Range 32-614aa
Protein Length Full Length of Mature Protein
Mol. Weight 68.9 kDa
Research Area Cardiovascular
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft.
Subcellular Location Cell junction, synapse. Secreted. Cell membrane; Peripheral membrane protein.; [Isoform H]: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side.
Protein Families Type-B carboxylesterase/lipase family
Database References
Tissue Specificity Has been found in central nervous system and muscle. Found in embryonic liver and spleen but not in adult liver.

Gene Functions References

  1. sepsis decreased AChE activity by reducing its expression at the neuromuscular junction. PMID: 28849127
  2. Paraquat-induced death of hippocampal neurons was partially mediated by AChE variants inducing and cholinergic and gultamatergic transmission disruption. PMID: 28916328
  3. Quercetin improves memory and anxiogenic-like behavior in diabetic rats by preventing the increase in Ache activity seen in streptozocin induced diabetes. PMID: 27694000
  4. the induction of PRiMA-linked AChE in osteoblast should be independent to classical estrogen signaling pathway. PMID: 27019979
  5. This study showed that changes in AChE may, at least in part, to lead to memory impairment caused by galactose. Taken together, our results can help understand the etiopathology of classical galactosemia. PMID: 26948151
  6. Acetylcholinesterase activity was increased in rats subjected to mild hyperhomocysteinemia PMID: 24590316
  7. Hindlimb unloading (simulation of hypogravity) leads to an increase in functional activity of acetylcholinesterase on the background of reduced postsynaptic membrane area occupied by acetylcholine receptors. PMID: 25711085
  8. Under all studied experimental conditions, offspring brain acetylcholinesterase (AChE) activity was found to be significantly decreased due to maternal hypothyroidism PMID: 24632022
  9. AChE has an important role in modulation of early immune responses against Toxoplasma gondii infection. PMID: 24039284
  10. Spindle-shaped AChE-rich cells in the floccular stalk project to the flocculus, nodulus and uvula, but not to the cerebellar hemispheres. PMID: 24010172
  11. Tyrosine increased acetylcholinesterase in blood & all tested brain areas. Acute administration decreased its mRNA levels in hippocampus. Chronic administration did the same in the hippocampus. PMID: 23046746
  12. Acetylcholinesterase inhibitor huperazine A improved, or partly reversed, the Abeta-induced damage of neurite outgrowth. PMID: 23119107
  13. in the absence of pituitary growth hormone the postnatal proliferation of cholinergic synapses in the rat spinal cord where AChE activity is abundant, is markedly reduced PMID: 22922167
  14. Hypothyroidism significantly reduced both specific and total AChE activity in spinal cord of rat pups PMID: 22982053
  15. The results from the present study demonstrate a marked increase in AChE activity in all brain structures following the administration of a branched-chain amino acid pool. PMID: 22328136
  16. This study demonistrated that AChE positive neurons were stained lightly, then during later developmental periods the staining gradually increased and achieved adult level of intensity on the day P21 in spinal cord. PMID: 22028090
  17. During induction of the non-alcoholic fatty liver disease with CCl4 AChE activity was significantly increased compared to control in blood, liver and brain tissues. PMID: 21881966
  18. AChE activity can act as purinergic and cholinergic markers in lymphocytes PMID: 20832780
  19. effect of melatonin on neuroinflammation and acetylcholinesterase activity induced by LPS in rat brain PMID: 20450904
  20. These findings suggest that the restricted localization of PRiMA-linked G4 AChE at the nmjs could be contributed by the pre-synaptic motor neuron and/or the post-synaptic muscle fiber. PMID: 19680821
  21. the importance of post-transcriptional mechanisms in regulating AChE expression in differentiating neurons and implicate HuD as a key trans-acting factor in these events PMID: 12468554
  22. The activity of this protein is completely suppressed by the administration of LD50 of phosphacol. PMID: 12629810
  23. AChE is necessary for normal dendrite and axon formation in hippocampal neurones and suggest that it may also play a role in excitatory synapse development, plasticity, and remodelling. PMID: 12799140
  24. Local increment in neuronal AChE concentration in the mammalian hippocampus, such as in amyloid deposits, may play a role in triggering neuropathological and behavioral changes such as those observed in Alzheimer disease brains PMID: 12969266
  25. In this study we show an effect of AChE that could contribute to the increased deposition of Amyloid beta PMID: 14678761
  26. AChE is involved in regulating cell-matrix interactions in bone PMID: 15454088
  27. Nearly all AChE-immunoreactive neurons in the Lateral hypothalamus express immunoreactivity for either melanin concentrating hormone or for orexin PMID: 15488307
  28. rats subjected to ovariectomy presented a significant increase in brain Na+, K+-ATPase, AChE and CAT activities, but did not change the oxidative stress parameters PMID: 15869839
  29. Results suggest that the presence of acetylcholinesterase protein doesn't correlate with catalytic activity, and the diffuse cytoplasmic and plasma membrane localization of AChE is a property of neuronal cell types. PMID: 16052514
  30. action of P2Y1 receptor could lead Ache gene activation in cultured cortical neurons PMID: 16429571
  31. Lead acetate decreased brain AChE activity of rats in dose/age dependent manner. PMID: 16678265
  32. The SH-amino acids seem to affect the hippocampal enzyme indirectly, possibly by lipid(s)-protein modifications(s) and Hci by inducing oxidative stress, since no effect was observed on pure AChE activity PMID: 16773467
  33. Results suggest that interferon-beta may act through inhibition of acetylcholinesterase, and ethidium bromide could be considered an inhibitor of AChE activity by interfering with cholinergic neurotransmission in the different brain regions. PMID: 16871442
  34. In the cerebellum, hyperthyroidism provoked a significant decrease in both the AChE and the Na(+), K(+)-ATPase activities PMID: 17165152
  35. findings provide evidence for intra- and supramodal influences of the neonatal removal of retinal input on neural activity- and use-dependent modifications of cortical AChE activity PMID: 17280650
  36. In choline-deprived (CD) newborn rats,ANTIOXIDANT STATUS and AChE and Na(+),K(+)-ATPase activities were significantly reduced by 23%, 24% and 50%, respectively, in the brains of both sexes. PMID: 17484629
  37. Low concentrations of aspartame metabolites had no effect on AChE activity, whereas high or toxic concentrations decreased enzyme activity. PMID: 17580119
  38. that the 55-kDa AChE may be involved in different biological processes such as neural development, tumor progression, and angiogenesis. PMID: 17606622
  39. These findings suggest that cell surface AChE, possibly in a novel signalling complex containing APP and perlecan, contributes to a generalised mechanism for polarised membrane protrusion and migration in all adherent cells. PMID: 17948252
  40. Repeated exposure to low dose malathion increased brain AChE activity and altered antioxidant levels. PMID: 18341513
  41. Data show that acetylcholine esterase enzyme activity shows a significant decrease in cerebral cortex and a increase in the muscle of experimental hypoxic neonatal rats. PMID: 18406032
  42. Although the mechanisms of action of GAA on AChE activity and on memory are unclear, these findings suggest that the accumulation of GAA found in patients with GAMT-deficiency may be one of the mechanisms involved in neural dysfunction. PMID: 18437545
  43. Tanshinone modulates AChE and NOS proteins concentrations in the hippocampus of AD rats. This may have therapeutic potential in AD rats. PMID: 18980714
  44. Protein CutA undergoes an unusual transfer into the secretory pathway and affects the folding, oligomerization, and secretion of acetylcholinesterase. PMID: 19049969
  45. cell death due to paraoxon not AChE dependent PMID: 19378919
  46. Data show that after denervation, the expression of PRiMA, AChE(T) and G(4) AChE decreased markedly in the spinal cord, and in fast- and slow-twitch muscles. PMID: 19490106

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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