Aprotinin

Manufactured by GoldBio

Aprotinin is a serine protease inhibitor used in laboratory research. It functions by inhibiting the activity of various proteases, including trypsin, plasmin, and kallikrein. Aprotinin is commonly used to prevent protein degradation in cell and tissue samples.

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Lab products found in correlation

Leupeptin, by GoldBio (4 mentions) Pepstatin, by GoldBio (2 mentions) Antipain dihydrochloride, by Thermo Fisher Scientific (2 mentions) Fastdigest restriction enzyme, by Thermo Fisher Scientific (1 mentions) Anti mouse irdye 680rd, by LI COR (1 mentions) Nanoglow luciferase assay, by Promega (1 mentions) E coli krx cells, by Promega (1 mentions) Anti rabbit irdye 800cw, by LI COR (1 mentions) Nanobit, by Promega (1 mentions) Diprotin a, by Bachem (1 mentions) Glutathione sepharose beads, by GoldBio (1 mentions) Leupeptin, by Thermo Fisher Scientific (1 mentions) Isopropyl β d 1 thiogalactopyranoside (iptg), by GoldBio (1 mentions) F9 6 1000 lex rotor, by Thermo Fisher Scientific (1 mentions) F20 12 50 lex rotor, by GoldBio (1 mentions) Dithiothreitol (dtt), by Merck Group (1 mentions) Pfu ultra dna polymerase, by Agilent Technologies (1 mentions) γ 32p gtp, by PerkinElmer (1 mentions) F1804, by Merck Group (1 mentions)

7 protocols using aprotinin

Peptide Synthesis and Epigenetic Assays

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All cloning reagents were obtained from New England Biolab (Gibson assembly Master Mix, Q5-mutagenesis kit) or Thermo Scientific (Fast Digest restriction enzymes). Reagents and building blocks for the solid phase peptide synthesis (SPPS) were from Anaspec, P3Bio, ChemPep, or Aaptec. The Chem Matrix Rink Amide resin was from Sigma. Solvents for SPPS, HPLC, and LC/MS, buffering agents, and additives were from Sigma or Fisher Scientific. Antibiotics, IPTG, DTT, and protease inhibitors (leupeptin, pepstatin, aprotinin, AEBSF) were from Gold Bio. KRX E.coli cells, NanoBit, and NanoGlow luciferase assay components were from Promega, and L-rhamnose was from Chem-Implex. tRNA from yeast was purchased from Sigma. Corning 384 Well Low Volume Black Round Bottom Polystyrene NBS Microplates were from Sigma. Anti-Histone H3 (acetyl K18) antibody - ChIP Grade (ab1191) was from Abcam, Anti-Histone H3 (acetyl K9) antibody (ab4441) was from Abcam. Secondary antibodies IRDye 680RD anti-mouse and IRDye 800CW anti-rabbit were from Li-Cor.

Kuznetsov V.I., Liu W.H., Klein M.A, & Denu J.M. (2022). Potent activation of NAD+-dependent deacetylase Sirt7 by nucleosome binding. ACS chemical biology, 17(8), 2248-2261.

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Assembly of SDS-resistant SNARE Complex

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The SNARE motifs were mixed in equimolar ratios in the following order: synaptobrevin-2 (29–93), SNAP-25A(141–203), SNAP-25A(11–82) and syntaxin-1A (191–253), in the presence of 1 M NaCl. The mixture contained the following protease inhibitors (protease inhibitor cocktail A): Antipain Dihydrochloride 0.016 mg/ml (Thermo Fischer Scientific: 50488492); Leupeptin 0.33 mg/ml (Gold Bio: L01025); Aprotinin 0.08 mg/ml (Gold Bio: A655100). The assembly reaction was incubated at room temperature overnight while rotating. The SNARE motifs that did not incorporate into complex were removed by concentration-dilution at room temperature using 30 kDa molecular weight cutoff (MWCO) Amicon centrifugation filters. The almost quantitative formation of SDS-resistant SNARE complex was verified by SDS-PAGE and Coomassie blue staining.

Voleti R., Bali S., Guerrero J., Smothers J., Springhower C., Acosta G.A., Brewer K., Albericio F, & Rizo J. (2021). Evaluation of the tert-butyl group as a probe for NMR studies of macromolecular complexes. Journal of biomolecular NMR, 75(8-9), 347-363.

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Foal Blood Sampling for Metabolic Markers

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Blood samples were collected at time 0 (before carbohydrate administration) and at 5, 10, 15, 30, 45, 60, 90, 120, 150, and 180 minutes. After 180 minutes, all foals were unmuzzled, allowed to nurse from the mare ad libitum, and additional blood samples in most (n = 22) foals were collected at 195 and 210 minutes.
Blood samples (4 mL) were placed in prechilled ethylenediaminetetraacetic acid (EDTA) tubes containing aprotinin (GoldBio, St Louis, Missouri) and diprotin A (Bachem, Torrance, California). aprotinin (500 kU/mL of blood) was added to inhibit protease‐mediated degradation of peptide hormones and diprotin A (50 μmol/mL of blood) is a dipeptidyl peptidase‐4 (DPP‐4) protease inhibitor added to decrease degradation of GIP and GLP‐1. The EDTA‐aprotinin‐DPP‐4 inhibitor tubes immediately were placed on ice for at least 20 minutes. Tubes were centrifuged at 1000g for 10 minutes at 4°C. Within 6 hours of collection, plasma was aliquoted and stored at −80°C until analysis. Blood samples for CBC and IgG concentrations were processed within 4 hours of collection.

Rings L.M., Swink J.M., Dunbar L.K., Burns T.A, & Toribio R.E. (2019). Enteroinsular axis response to carbohydrates and fasting in healthy newborn foals. Journal of Veterinary Internal Medicine, 33(6), 2752-2764.

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Ataxin-3 Purification Workflow

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Ataxin-3^Q55 was purified as described previously (63 (link)). GST-ATXN3^Q55 was grown in BL21 cells to an OD₆₀₀ of 0.6 and induced with 1mM IPTG (GoldBio) overnight at 16°C. Cells were spun down at 7,000rpm (Thermo Scientific F9–6×1000 LEX rotor) and resuspended in NETN buffer (50mM Tris, pH 7.5, 150mM NaCl, 0.5% IGEPAL CA-630) containing aprotinin (GoldBio), leupeptin (Alfa Aesar), PMSF (Grainger), and DTT (Sigma). For lysis, cells were tumbled at 4°C for 30min and sonicated 3 times for 30s. Lysates were spun down at 12,000 rpm (Thermo Scientific F20–12×50 LEX rotor) for 10min and the supernatant was added to glutathione sepharose beads (GoldBio) and tumbled at 4°C for over 1h. Beads were then washed 3 times with NETN and washed 3 more times with PBS. Protein was eluted off the beads by incubating with HRV 3c protease overnight at 4°C.

Zimonjic D.B., Kelley M.J., Rubin J.S., Aaronson S.A, & Popescu N.C. (1997). Fluorescence in situ hybridization analysis of keratinocyte growth factor gene amplification and dispersion in evolution of great apes and humans. Proceedings of the National Academy of Sciences of the United States of America, 94(21), 11461-11465.

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Assembling SNARE Protein Complex

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The SNARE motifs were mixed in the equimolar ratio in following order: synaptobrevin-2 (29–93), SNAP-25A(141–203), SNAP-25A(11–82) and syntaxin-1A (191–253), in the presence of 1 M NaCl. The mixture contained the following protease inhibitors (protease inhibitor cocktail A): Antipain Dihydrochloride 0.016 mg/ml (Thermo Fischer Scientific: 50488492); Leupeptin 0.33 mg/ml (Gold Bio: L01025); Aprotinin 0.08 mg/ml (Gold Bio: A655100). The assembly reaction was incubated in room temperature overnight while rotating. The SNARE motifs that did not incorporate into complex were removed by concentration-dilution at room temperature using 30 kDa molecular weight cutoff (MWCO) Amicon centrifugation filters.

Voleti R., Jaczynska K, & Rizo J. (2020). Ca2+-dependent release of synaptotagmin-1 from the SNARE complex on phosphatidylinositol 4,5-bisphosphate-containing membranes. eLife, 9, e57154.

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Recombinant Protein Expression and Purification

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Unless otherwise indicated, all chemical reagents were obtained from Sigma or Fisher Scientific. Fluorescein di-β-D-galactopyranoside (FDG) was from Marker Gene Technologies, and the protein inhibitor mixture was from Sigma (catalog no. S8830). Leupeptin, pepstatin, and aprotinin were from Gold Biotechnology. All restriction endonucleases and E. coli strain BL21(DE3) were from Thermo Scientific. E. coli strain DH5α was purchased from New England Biolabs. Pfu ultra DNA polymerase used for site-directed mutagenesis was purchased from Agilent. [γ-³²P]GTP was from Perkin Elmer. Mouse monoclonal antibodies raised against α-tubulin (T6074), FLAG tag (F1804) or His-tag (H1029) were from Sigma. Mouse monoclonal antibody raised against hemagglutinin (HA) tag (clone 12CA5, #11583816001) was obtained from Roche. Mouse monoclonal antibody raised against MYC-tag (9B11, #2276) was from Cell Signaling. Rabbit polyclonal antibody raised against Gαs (C-18, sc-383) was purchased from Santa Cruz Biotechnology. Goat anti-rabbit Alexa Fluor 680 (A21077) and goat anti-mouse IRDye 800 (#926–32210) secondary antibodies were from Life technologies and LiCor, respectively.

Garcia-Marcos M., Parag-Sharma K., Marivin A., Maziarz M., Luebbers A, & Nguyen L.T. (2020). Optogenetic activation of heterotrimeric G-proteins by LOV2GIVe, a rationally engineered modular protein. eLife, 9, e60155.

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Arterial and Venous Blood Sampling

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Arterial blood samples (2 mL) were analyzed immediately with a blood gas analyzer (CCA-TS2 blood gas analyzer, Opti Medical Systems) to determine sodium concentration. Venous blood samples were collected into EDTA-containing tubes and plain serum clot tubes. The protease inhibitor aprotinin (Goldbio, Gold Biotechnology) was added to each EDTA blood collection tube individually to allow for AVP sample preservation (500 kU/mL of whole blood) a week before the anesthetic event, and tubes were stored at 4 °C until sample collection. Samples were chilled on ice until all samples for each anesthetic event had been collected; the samples from each anesthetic event were then processed together within 24 hours of collection. The samples were centrifuged at 1,000 g for 15 minutes, and the serum and plasma were aliquoted into 1.5-mL microcentrifuge tubes and frozen at -80 °C until analysis.

Schnuelle M.L., Hopster K., Toribio R.E, & Hurcombe S.D. (2022). Effects of 7.2% hypertonic saline solution on cardiovascular parameters and endogenous arginine vasopressin secretion in euvolemic isoflurane-anesthetized horses. American journal of veterinary research, 83(9).

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