Bovine brain calmodulin

Manufactured by Merck Group

Bovine brain calmodulin is a calcium-binding protein found in the brain of cattle. It plays a key role in the regulation of various cellular processes by binding to and activating other proteins in response to changes in calcium levels.

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Lab products found in correlation

L ng nitroarginine methyl ester l name, by Merck Group (1 mentions) Ethylenediaminetetraacetic acid edta, by Merck Group (1 mentions) Ethylene glycol tetraacetic acid (egta), by Merck Group (1 mentions) 15n4 arg, by Cambridge Isotopes (1 mentions) L citrulline, by Cambridge Isotopes (1 mentions) 15n nitrite, by Cambridge Isotopes (1 mentions) Cell culture reagents, by Thermo Fisher Scientific (1 mentions) 4 2 hydroxyethyl 1 piperazineethanesulfonic acid hepes, by Merck Group (1 mentions) Millipore water, by Merck Group (1 mentions)

2 protocols using bovine brain calmodulin

Nitric Oxide Synthesis Assay Protocol

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ARG [as L-arginine HCl], CIT [as L-citrulline], 4-(2-Hydroxyethyl)-1 piperazineethanesulfonic acid (HEPES), CaCl₂·4H₂O, bovine brain calmodulin, (6R)-5,6,7,8-tetrahydro-l-biopterin (BH₄), NADPH, ethylene diamine tetraacetic acid (EDTA), ethylene glycol tetraacetic acid (EGTA), and L-N^G-Nitroarginine methyl ester (L-NAME) were purchased from Sigma (St. Louis, MO). ¹⁵N₄-ARG [as its HCl, (U-¹⁵N₄, 98%)], the internal standard for ARG, ¹³C₆-ARG [as ARG:HCl (U-¹³C₆, 98%)], the internal standard for CIT, D₄-CIT [as L-citrulline (4,4,5,5-D₄, 96.5 %)], and ¹⁵N-nitrite [as NaNO₂ (¹⁵N, 98%+)] were obtained from Cambridge Isotope Laboratories, Inc. These compounds were used without further purification. Cell culture reagents were purchased from Invitrogen.

Shin B.S., Fung H.L., Upadhyay M, & Shin S. (2015). Estimation of nitric oxide synthase activity via LC-MS/MS determination of 15N3-citrulline in biological samples. Rapid communications in mass spectrometry : RCM, 29(5), 447-455.

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Purification and Characterization of Baa Peptide

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The bovine brain calmodulin used in the study was purchased from Sigma-Aldrich and used without further purification. Millipore water (18 MΩ cm) was used to prepare all aqueous solutions. All other amino acids used in the peptide synthesis were purchased from Novabiochem. The basic, amphiphilic α-helix (Baa) were synthesized by a standard Fmoc-protocol and purified by preparative RP-HPLC. The identity of the product was verified by MALDI-TOF mass spectrometry.

Chen Y.T., Chao W.C., Kuo H.T., Shen J.Y., Chen I.H., Yang H.C., Wang J.S., Lu J.F., Cheng R.P, & Chou P.T. (2016). Probing the polarity and water environment at the protein-peptide binding interface using tryptophan analogues. Biochemistry and Biophysics Reports, 7, 113-118.

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