Glucagon

Manufactured by Peptide Institute

Sourced in Japan

Glucagon is a laboratory product used for research purposes. It functions as a hormone that regulates blood glucose levels.

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Lab products found in correlation

4 protocols using glucagon

Glucagon-Mediated CREB Activation

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Glucagon and H-89 were purchased from the PEPTIDE INSTITUTE, INC. (Osaka, Japan) and Cyman Chemical (Ann Arbor, MI, USA), respectively. Aprotinin, pepstatin, and leupeptin were purchased from Sigma-Aldrich (St. Louis, MO, USA). Other chemicals were purchased from Nacalai Tesque (Tokyo, Japan). An anti-Glucagon receptor antibody was purchased from Abcam (Cambridge, UK). An anti-phospho-CREB antibody (Ser133), anti-CREB antibody, and anti-CBP antibody were purchased from Cell Signaling Technology (Danvers, MA, USA). An anti-lamin B antibody and anti-β-actin antibody were purchased from Santa Cruz Biotechnology (Santa Cruz, CA, USA). Peroxidase-conjugated rabbit anti-mouse, rabbit anti-goat, and goat anti-rabbit secondary antibodies were purchased from Dako-Japan (Tokyo, Japan).

Funakoshi-Tago M., Yu S., Kushida A., Takeuchi K, & Tamura H. (2020). Kampo medicines, Rokumigan, Hachimijiogan, and Goshajinkigan, significantly inhibit glucagon-induced CREB activation. Heliyon, 6(3), e03598.

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Enzymatic Activity Characterization Protocol

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Restriction and DNA-modifying enzymes were purchased from Takara Bio and New England Biolabs. Quick Taq HS DyeMix came from Toyobo. Oligonucleotide primers were synthesized by FASMAC. Leupeptin, Gly-Pro-MCA, His-Ala-MCA, Lys-Ala-MCA, Phe-Met-MCA, [(2S, 3S)-3-carboxyoxirane-2-carbonyl]-l-leucine (4-guanidinobutyl) amide hemihydrate, GLP-1, GIP, glucagon, oxyntomodulin, and substance-P were purchased from Peptide Institute. Gly-Phe-MCA and Ser-Tyr-MCA were obtained from Bachem. Other substrates not commercially available, that is, His-Ala-MCA, Gly-Ala-MCA, Tyr-Ala-MCA, Phe-Leu-MCA, HAED-MCA, HAEG-MCA, HAEF-MCA, YAED-MCA, LDKA-MCA, TDKA-MCA, and HAEGTF-MCA, were synthesized by Scrum. CCL3 and CXCL6 were provided by GenScript Japan. Bovine insulin, tosyl-l-lysyl-chloromethane hydrochloride, aprotinin, sitagliptin phosphate monohydrate, 3,4-dichloroisocoumarin, 4-(2-aminoethyl) benzenesulfonyl fluoride hydrochloride, and α-cyano-4-hydroxycinnamic acid were obtained from Sigma–Aldrich. Isoleucine thiazolidide hemifumarate (P32/98) was from FOCUS Biomolecules.

Ohara-Nemoto Y., Shimoyama Y., Ono T., Sarwar M.T., Nakasato M., Sasaki M, & Nemoto T.K. (2022). Expanded substrate specificity supported by P1′ and P2′ residues enables bacterial dipeptidyl-peptidase 7 to degrade bioactive peptides. The Journal of Biological Chemistry, 298(3), 101585.

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Synthetic Peptide Procurement for Research

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The synthetic peptides of GIP (1–42), GLP‐1 (7–36) amide, and glucagon were purchased from Peptide Institute (Osaka, Japan). GIP (1–30) amide and oxyntomodulin were purchased from Phoenix Pharmaceuticals (Burlingame, CA, USA).

Takeda Y., Fujita Y., Yanagimachi T., Maruyama N., Bessho R., Sakagami H., Honjo J., Yokoyama H, & Haneda M. (2020). Establishment of novel specific assay for short‐form glucose‐dependent insulinotropic polypeptide and evaluation of its secretion in nondiabetic subjects. Physiological Reports, 8(11), e14469.

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Labeling Peptides with Fluorescein

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Fifty μL of 10 -2 M fluorescein-5(6)-isothiocyanate (FITC, Sigma-Aldrich, MO, USA) dissolved in dimethylformamide was mixed with 50 μL of 10 -4 M GIP, GLP-1 or glucagon (Peptide Institute, Osaka, Japan) and, then 150 μL of Na 2 CO 3 /NaHCO 3 (0.1 M, pH 9.1) was added and continuously vortexed for 3 h in the dark at room temperature. The reaction mixture was then passed through a column prepacked with Sephadex G-25 Fine (GE Healthcare, Buckinghamshire, UK) saturated and eluted with 30 mM TES, 140 mM NaCl, 4 mM KCl (pH 7.4). Then the FITC labeled peptides were separated from unreacted FITC using the BioLogic TM LP System and Model 2110 Fraction Collector (Bio-Rad Laboratories, Hercules, CA, USA). Eluates were collected in fractions, each with a volume of 900 μL. The fraction with the highest fluorescence intensity determined at λex 485/ λem 528 was used for subsequent experiments.

Hoshiyama A., Fujimoto K., Konno R., Sasaki S., Momozono A., Kodera Y, & Shichiri M. (2019). Identification of plasma binding proteins for glucose-dependent insulinotropic polypeptide. Endocrine journal, 66(7).

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