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Glomo npf

Manufactured by GL Biochem

The Glomo-NPF is a laboratory equipment designed for the analysis of nucleic acids and proteins. It utilizes a specialized detection mechanism to quantify the presence and concentration of these biomolecules in a sample. The core function of the Glomo-NPF is to provide accurate and reliable data to support scientific research and analysis.

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2 protocols using glomo npf

1

Synthesis and Characterization of Glomo-NPF and Glomo-sNPF Peptides

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Glomo-NPF (NTRPTRNDEIANIEEALQYLQELENFYDGKARIRFamide), Glomo-sNPF-1 (AQRSPSLRLRFamide), Glomo-sNPF-2 (SPSLRLRFamide), Glomo-sNPF-3 (PQRLRFamide) and Glomo-sNPF-4 (PARLRFamide) (IGGI, 2014; Caers et al., 2015b) , were synthesized by GL Biochem Ltd. (Shangai). All peptides were purified by reversed-phase high performance liquid chromatography (HPLC) and verified with a matrix-assisted laser desorption/ionization tandem time-of-flight (MALDI TOF/TOF, Ultraflex II Bruker Daltonics) mass spectrometer.
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2

Synthesis and Characterization of Glomo-sNPF Peptides

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Glomo-sNPF-1 (AQRSPSLRLRFamide), Glomo-sNPF-2 (SPSLRLRFamide), Glomo-sNPF-3 (PQRLRFamide), Glomo-sNPF-4 (PARLRFamide) and Glomo-NPF (NTRPTRNDEIANIEEALQYLQELENFYDGKARIRFamide) were synthesized by GL Biochem Ltd. (Shangai). All peptides were purified by reversed-phase high performance liquid chromatography (HPLC), and their sequence was verified with a matrix-assisted laser desorption/ionization tandem time-of-flight (MALDI TOF/TOF, Ultraflex II Bruker Daltonics) mass spectrometer. (Nässel and Wegener, 2011) (link). Protein sequence alignments of Glomo-sNPFR with other dipteran sNPFRs demonstrate a high overall sequence identity and similarity, with the highest conservation in the transmembrane domains (supplementary data 2). For example, Glomo-sNPFR shares 66% sequence identity with Musdo-sNPFR, 64% with Anoga-sNPFR, 63% with Drome-sNPFR, and 59% with Aedae-sNPFR. In addition, the Glomo-sNPFR sequence harbors typical motifs of the rhodopsin-like GPCR family and multiple putative phosphorylation, palmitoylation and glycosylation sites (Figure 2).
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