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MedChemExpressModel Proctolin -57966-42-4

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Proctolin is an endogenous pentapeptide that acts as an excitatory neuromodulator.
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Proctolin

MCE China:Proctolin

Brand:MedChemExpress (MCE)

Cat. No.HY-P0275

CAS:57966-42-4

Purity:98.62%

Storage:Sealed storage, away from moisture Powder -80°C 2 years -20°C 1 year *In solvent : -80°C, 6 months; -20°C, 1 month (sealed storage, away from moisture)

Shipping:Room temperature in continental US; may vary elsewhere.

Description:Proctolin is an endogenous pentapeptide that acts as an excitatory neuromodulator.

In Vitro:Proctolin can increase the frequency of action potentials, increase the amplitude of muscle contraction, and initiate activity in quiescent systems[1]. In the arthropods, Proctolin acts as a neuromodulator and possibly as a neurohormone. It does not appear to function as a conventional neurotransmitter[2]. Proctolin is a pentapeptide with the mature peptide of RYLPT, and it is the first insect neuropeptide to be sequenced and chemically characterized. The first identification of a Proctolin precursor gene is CG7105 in D. melanogaster. Although a previous study showed that Proctolin is absent in B. mori, this pentapeptide is recently identified in a proteomic analysis of B. mori wings. However, the Bombyx Proctolin gene does not produce a mature peptide because cleavage sites are not present at the N-terminal and C-terminal of the RYLPT sequence, and a similar gene is observed in C. suppressalis. Therefore, a true Proctolin has been considered to be not observed in B. mori and C. suppressalis[3].

Sequence:Arg-Tyr-Leu-Pro-Thr

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References:

[1]. McGrath LL, et al. De novo transcriptome assembly for the lobster Homarus americanus and characterization of differential gene expression across nervous system tissues. BMC Genomics. 2016 Jan 16;17:63.  [Content Brief]

[2]. Orchard I, et al. Proctolin: a review with emphasis on insects. J Neurobiol. 1989 Jul;20(5):470-96.  [Content Brief]

[3]. Xu G, et al. Identification and expression profiles of neuropeptides and their G protein-coupled receptors in the rice stem borer Chilo suppressalis. Sci Rep. 2016 Jun 29;6:28976.  [Content Brief]

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