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M0630

Manufactured by Merck Group
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Sourced in Bulgaria

M0630 is a laboratory equipment product from Merck Group. It is a centrifuge designed for general-purpose laboratory applications. The core function of M0630 is to separate components of a liquid mixture based on their relative differences in density.

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Lab products found in correlation

H2500, by Merck Group (3 mentions) Horseradish peroxidase streptavidin sa 5004, by Vector Laboratories (2 mentions) Ez run prestained protein ladder bp3603, by Thermo Fisher Scientific (2 mentions) Natural unstained protein ladder 161 0317, by Bio-Rad (2 mentions) B2787, by Bio-Rad (2 mentions) Supersignal west pico chemiluminescent substrate, by Thermo Fisher Scientific (2 mentions) Thermomixer, by Eppendorf (2 mentions) Biotinyl asp glu val asp aldehyde, by Bachem (2 mentions) C2506, by Merck Group (1 mentions) Lc ms grade solvents, by Thermo Fisher Scientific (1 mentions) Ammonium acetate, by Avantor (1 mentions) Myoglobin, by Merck Group (1 mentions) Ascorbic acid, by Merck Group (1 mentions) Ly294002, by Merck Group (1 mentions)

8 protocols using m0630

1

Equine Skeletal Muscle Proteins Purification

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Myoglobin from equine skeletal muscle (M0630), carbonic anhydrase
from bovine erythrocytes (C5024), and cytochrome c from equine heart
(C2506), 6-ethoxy-2-benzothiazolesulfonamide (ethoxzolamide) (333328)
and ammonium hydroxide (A6899) were purchased from Sigma-Aldrich (Dorset,
UK). LC/MS grade solvents were purchased from Fisher Scientific (Loughborough,
UK), ammonium acetate was purchased from J. T. Baker (Deventer, The
Netherlands).
Illes-Toth E, & Cooper H.J. (2019). Probing the Fundamentals of Native Liquid Extraction Surface Analysis Mass Spectrometry of Proteins: Can Proteins Refold during Extraction?. Analytical Chemistry, 91(19), 12246-12254.
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2

Preparation and Analysis of Homocysteinylated Myoglobin

Cited 1 time
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Horseradish peroxidase streptavidin (SA-5004) was from Vector Laboratories (Burlingame, CA, USA). SuperSignal West Pico chemiluminescent substrate was from Thermo Scientific (Rockford, IL, USA). Myoglobin from equine skeletal muscle (M0630) was from Sigma-Aldrich. N-Homocysteinylated myoglobin was prepared as we previously reported [64 (link)]. Biotinyl-Asp-Glu-Val-Asp-aldehyde (CAS registry number: 178603-73-1) was from Bachem Americas (N-1470, Torrance, CA, USA; see Figure S1 for its structure in Support Information). Rhodamine-aldehyde (10 mM) in 50% 200-proof ethanol was synthesized as previously described [64 (link)]. EZ-Run prestained protein ladder (BP3603) was from Fisher Scientific. Natural unstained protein ladder (161-0317) was from Bio-Rad. Biotinylated protein markers were from Sigma-Aldrich (B2787) and Bio-Rad (161-0319), respectively. All reagents were ACS grade and used as received without further purification. All incubations were carried out in an Eppendorf Thermomixer® (Eppendorf North America, Hauppauge, NY, USA) at 25 °C unless specified otherwise.
Zang T., Pottenplackel L.P., Handy D.E., Loscalzo J., Dai S., Deth R.C., Zhou Z.S, & Ma J. (2016). Comparison of Protein N-Homocysteinylation in Rat Plasma under Elevated Homocysteine Using a Specific Chemical Labeling Method. Molecules, 21(9), 1195.
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3

Ferrous Myoglobin-Mediated Renal Cell Injury

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myoglobin (M0630, Sigma Aldrich Corporation, St. Louis, MO, USA) and ascorbic acid (Sigma) were dissolved in Dulbecco’s Modified Eagle Medium(DMEM):Nutrient Mixture F-12 media(DMEM/F12, Gibco, Life Technologies Corporation, Carlsbad, CA, USA) to make the storage solution. The storage solution was diluted to a proper concentration just before each experiment. A concentration of 200 mM (i.e., 3.6 g/L) ferrous myoglobin was used in this study. Only reduced myoglobin is cytotoxic, but only metmyoglobin was commercially available, so the myoglobin and ascorbic acid solutions were mixed to make the ferrous myoglobin mediumas described in the literature32 (link). The final concentration of myoglobin was 200 mM, while ascorbic acid was 2 mM. The ascorbic acid had reduced myoglobin to ferrous status when the color changed from brown to reddish.
The following groups were evaluated: Con, HK-2 cells in normal media; Mb, HK-2 cells in ferrous myoglobin medium; Mb + MSCs, HK-2 cells in ferrous myoglobin medium co-culture with MSCs in 6- or 96-well transwell plates. Mb + MSCs + LY294002, HK-2 cells in ferrous myoglobin medium were co-culture with MSCs in 6- or 96-well transwell plates with the PI3K inhibitor, LY294002 (25 μmol/L) (Sigma).
Geng X., Hong Q., Wang W., Zheng W., Li O., Cai G., Chen X, & Wu D. (2017). Biological Membrane-Packed Mesenchymal Stem Cells Treat Acute Kidney Disease by Ameliorating Mitochondrial-Related Apoptosis. Scientific Reports, 7, 41136.
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4

Preparation of Anaerobic Protein Samples

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Equine heart cytochrome c (C2506), lysozyme from chicken egg white (L6876), bovine serum albumin (A7638) and equine skeletal muscle myoglobin (M0630) were purchased in lyophilized form from Sigma-Aldrich. Samples were prepared to 2, 5, 20 or 200 µM concentration by dissolving in 10 mM phosphate buffer at pH 7.3, and divided into 1 ml aliquots. Low oxygen samples were further prepared by cycling into a nitro­gen environment in a Coy Anaerobic Chamber and allowed to equilibrate overnight. Dissolved oxygen levels as measured using a Milwaukee MW600 sensor inside the chamber showed that, upon first entering the anaerobic chamber, samples contained 14–17 mg L−1 dissolved oxygen, and after equilibrating overnight in the chamber, contained 1–3 mg L−1. The low oxygen protein samples were drawn up one at a time into a gas-tight glass luer-lock Hamilton syringe, wrapped with parafilm, double-bagged inside the anaerobic chamber, and brought immediately to beamline 3.2.1 for data collection.
Kristensen L.G., Holton J.M., Rad B., Chen Y., Petzold C.J., Gupta S, & Ralston C.Y. (2021). Hydroxyl radical mediated damage of proteins in low oxygen solution investigated using X-ray footprinting mass spectrometry. Journal of Synchrotron Radiation, 28(Pt 5), 1333-1342.
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5

Homocysteinylated Myoglobin Labeling Protocol

Cited 1 time
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Horseradish peroxidase streptavidin (SA-5004) was from Vector Laboratories (Burlingame, CA, USA). SuperSignal West Pico chemiluminescent substrate was from Thermo Scientific (Rockford, IL, USA). Myoglobin from equine skeletal muscle (M0630) was from Sigma-Aldrich. N-Homocysteinylated myoglobin was prepared as we previously reported [64 (link)]. Biotinyl-Asp-Glu-Val-Asp-aldehyde (CAS registry number: 178603-73-1) was from Bachem Americas (N-1470, Torrance, CA, USA; see Figure S1 for its structure in Support Information). Rhodamine-aldehyde (10 mM) in 50% 200-proof ethanol was synthesized as previously described [64 (link)]. EZ-Run prestained protein ladder (BP3603) was from Fisher Scientific. Natural unstained protein ladder (161-0317) was from Bio-Rad. Biotinylated protein markers were from Sigma-Aldrich (B2787) and Bio-Rad (161-0319), respectively. All reagents were ACS grade and used as received without further purification. All incubations were carried out in an Eppendorf Thermomixer® (Eppendorf North America, Hauppauge, NY, USA) at 25 °C unless specified otherwise.
Zang T., Pottenplackel L.P., Handy D.E., Loscalzo J., Dai S., Deth R.C., Zhou Z.S, & Ma J. (2016). Comparison of Protein N-Homocysteinylation in Rat Plasma under Elevated Homocysteine Using a Specific Chemical Labeling Method. Molecules, 21(9), 1195.
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6

Bovine Hemoglobin and Equine Myoglobin Analysis

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Hemoglobin (from bovine blood, H2500) and myoglobin (from equine skeletal muscle, M0630) were purchased from Sigma-Aldrich (Sofia, Bulgaria, FOT Ltd.-representative). The pure gases and gas mixtures (CO, CO2, NO, O2) required were purchased from Messer Bulgaria (Sofia, Bulgaria).
Dyankov G., Borisova E., Belina E., Kisov H., Angelov I., Gisbrecht A., Strijkova V, & Malinowski N. (2020). A Surface Plasmon Resonance Biosensor Based on Directly Immobilized Hemoglobin and Myoglobin. Sensors (Basel, Switzerland), 20(19), 5572.
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7

Intravenous Hemoglobin and Myoglobin Administration in Dehydrated Mice

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Intravenous administration of hemoglobin or myoglobin (180 or 250 mg/100 g body weight, respectively, catalog nos. H2500 and M0630, Sigma Aldrich, St. Louis, MO) was performed in C57BL/6J mice after 16–18 hours of dehydration. For these studies, kidney tissues were harvested for gene expression assessments 24 hours after these injections. In additional studies, hemin (hemin ferriprotoporphyrin IX chloride, 50 or 100 µmol/kg, IP) was administered to C57BL/6J mice at 6 and 24 hours before kidneys harvest.
Nath K.A., Singh R.D., Croatt A.J., Ackerman A.W., Grande J.P., O'Brien D.R., Garovic V.D., Adams C.M., Tchkonia T, & Kirkland J.L. (2024). Induction of p16Ink4a Gene Expression in Heme Protein–Induced AKI and by Heme: Pathophysiologic Implications. Kidney360, 5(4), 501-514.
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8

Bovine Hemoglobin and Equine Myoglobin Protocol

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Hb (from bovine blood, H2500) and Mb (from equine skeletal muscle, M0630) were purchased from Sigma-Aldrich (Sofia, Bulgaria, FOT Ltd.-representative).
Dyankov G., Genova-Kalou P., Eftimov T., Ghaffari S.S., Mankov V., Kisov H., Veselinov P., Hikova E, & Malinowski N. (2023). Binding of SARS-CoV-2 Structural Proteins to Hemoglobin and Myoglobin Studied by SPR and DR LPG. Sensors (Basel, Switzerland), 23(6), 3346.
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