Transthyretin

Manufactured by Merck Group

Sourced in United States

Transthyretin is a laboratory product manufactured by Merck Group. It is a protein that functions as a transport protein in the body, carrying thyroid hormones and retinol (vitamin A) in the bloodstream. This product is primarily used for research and analytical purposes in various scientific and medical applications.

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Lab products found in correlation

8 protocols using transthyretin

Protein Purification and Characterization

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Ubiquitin (bovine), cytochrome c (equine), transthyretin (human), myoglobin (bovine) and urea were obtained from Sigma-Aldrich (St. Louis, MO, USA). Alpha synuclein (human, expressed in E. coli) was obtained from rPeptide. Calmodulin (human) and staphylococcal nuclease (Staphylococcus aureus) were expressed as described previously [33 ]. Solvents were purchased from Thermo Fisher Scientific (Pittsburg, PA). Proteins were cleaned up by using Bio-Spin 6 columns from Bio-Rad Laboratories (Hercules, CA).

Bashyal A., Sanders J.D., Holden D.D, & Brodbelt J.S. (2019). Top-Down Analysis of Proteins in Low Charge States. Journal of the American Society for Mass Spectrometry, 30(4), 704-717.

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Synthesis and Characterization of PCB Metabolites

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All PCBs and PCB metabolites (4-chlorobiphenyl (PCB 3), 3,3′-dichlorobiphenyl (PCB 11), 4′-chloro-biphenyl-3-ol (3′-OHPCB 3), 4′-chloro-biphenyl-4-ol (4′-OHPCB 3), 3,3′-dichloro-biphenyl-4-ol (4-OHPCB 11), 3,3′,4′,5-tetrachloro-biphenyl-4-ol (4′-OHPCB 79) and ammonium salts of 4-chloro-3′-sulfooxy-biphenyl (3′-PCB 3 sulfate), 4-chloro-4′-sulfooxy-biphenyl (4′-PCB 3 sulfate), 3,3′-dichloro-4-sulfooxy-biphenyl (4-PCB 11 sulfate), 2,4′-dichloro-4-sulfooxy-biphenyl (4-PCB 8 sulfate), 2,3′,5-trichloro-4′-sulfooxy-biphenyl (4′-PCB 26 sulfate) and 2,3′,4′-trichloro-4-sulfooxy-biphenyl (4-PCB 33 sulfate)) used in this study were provided by the Synthesis Core of the University of Iowa Superfund Research Program and synthesized and characterized as described elsewhere (Figure 2).^{31 (link), 32 (link)} PCB sulfates were synthesized as the ammonium salts.^{32 (link)} Flufenamic acid, 8-anilinonaphthalene-1-sulfonic acid (ANS), and transthyretin purified from human plasma (> 95%) were all acquired from Sigma Aldrich (St. Louis, MO). The purity of TTR was routinely confirmed by SDS-PAGE.

Grimm F.A., Lehmler H.J., He X., Robertson L.W, & Duffel M.W. (2015). Modulating Inhibitors of Transthyretin Fibrillogenesis via Sulfation: Polychlorinated Biphenyl Sulfates as Models. Chemico-biological interactions, 228, 1-8.

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Structural analysis of diverse proteins

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Triose phosphate isomerase (rabbit, TPI), avidin (chicken egg white, AVD), alcohol dehydrogenase (yeast, ADH), pyruvate kinase (rabbit muscle, PK), aldolase (rabbit muscle, ALD), transthyretin (human, TTR), Concanavalin A (jack bean, ConA), glutamate dehydrogenase (bovine liver, GDH) were purchased from Sigma Aldrich. A subset of these (TPI, AVD, ALD, TTR) were chosen for detailed IM-MS and CIU analysis, as they represent a broad cross-section of protein structures and stabilities. GDH was subjected to CXL treatment, but was not observed to undergo sufficient gas-phase unfolding following cross-linking, and thus not included in our CIU/CID analysis here. All other proteins listed were used for CCS calibration. Micro bio-spin columns with bio-gel P6 or P30 in a sodium chloride/citrate (SSC) buffer were purchased from Biorad.

Samulak B.M., Niu S., Andrews P.C, & Ruotolo B.T. (2016). Ion Mobility-Mass Spectrometry Analysis of Crosslinked Intact Multiprotein Complexes: Enhanced Gas-phase Stabilities and Altered Dissociation Pathways. Analytical chemistry, 88(10), 5290-5298.

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IM-MS Analysis of Purified Aurora A

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IM-MS analysis was performed on a Waters Synapt G2-Si instrument. Purified Aurora A was buffer exchanged into 50 mM NH₄OAc (LC grade, Sigma) as previously described [69 (link)]. Typically, 1–3 μl of 2–5 μM sample was analysed using borosilicate emitters (Thermo ES 387). Spraying voltage was adjusted to 1.1–1.8 kV, sampling cone was 20 V. Pressure in the travelling wave (T-wave) ion mobility cell was 2.78 mbar (nitrogen), wave height was kept at 30 V, wave velocity at 750 m/s. In order to experimentally determine collision cross section (CCS), drift time through the T-wave mobility cell was performed using β-lactoglobulin A (Sigma L7880), avidin (Sigma A9275), transthyretin (Sigma P1742), concanavalin A (Sigma C2010) and serum albumin (Sigma P7656) according to standard protocols. The exact hard sphere scattering (EHSS) model implemented in the Mobcal software was used to calculate CCS values on the basis of X-ray structures, as described previously [69 (link)].

Tsuchiya Y., Byrne D.P., Burgess S.G., Bormann J., Baković J., Huang Y., Zhyvoloup A., Yu B.Y., Peak-Chew S., Tran T., Bellany F., Tabor A.B., Chan A.E., Guruprasad L., Garifulin O., Filonenko V., Vonderach M., Ferries S., Eyers C.E., Carroll J., Skehel M., Bayliss R., Eyers P.A, & Gout I. (2019). Covalent Aurora A regulation by the metabolic integrator coenzyme A. Redox Biology, 28, 101318.

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Determination of Protein CCS by IM-MS

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To experimentally determine CCS, the measured drift time through the T-wave mobility cell of β-lactoglobulin A (Sigma L7880), avidin (Sigma A9275), transthyretin (Sigma P1742), concanavalin A (Sigma C2010) and serum albumin (Sigma P7656) was calculated according to standard protocols [54 (link)]. The exact hard sphere scattering (EHSS) model implemented in the Mobcal software was used to calculate CCS values on the basis of X-ray structures [55 (link)].

Byrne D.P., Vonderach M., Ferries S., Brownridge P.J., Eyers C.E, & Eyers P.A. (2016). cAMP-dependent protein kinase (PKA) complexes probed by complementary differential scanning fluorimetry and ion mobility–mass spectrometry. Biochemical Journal, 473(19), 3159-3175.

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Proteolytic Cleavage of Plasma Proteins

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Apolipoprotein A-IV, clusterin, α-2-antiplasmin, kininogen, and transthyretin (2 μg; Sigma-Aldrich, St. Louis, MO, USA) were incubated with HF3 (200 ng) (1:10 (w/w) enzyme-to-substrate ratio) in 0.05 M Tris-HCl, pH 8.0, 1.0 mM CaCl₂ for 2 h at 37 °C. Apoliprotein E (4 μg; Sigma-Aldrich, St. Louis, MO, USA) was incubated with HF3 (400 ng) (1:10 (w/w) enzyme-to-substrate ratio) in the same buffer. A sample of each protein was incubated without enzymes under identical conditions. Reactions were stopped by adding a Laemmli sample buffer, and subjected to SDS-PAGE.

Bertholim L., Chaves A.F., Oliveira A.K., Menezes M.C., Asega A.F., Tashima A.K., Zelanis A, & Serrano S.M. (2021). Systemic Effects of Hemorrhagic Snake Venom Metalloproteinases: Untargeted Peptidomics to Explore the Pathodegradome of Plasma Proteins. Toxins, 13(11), 764.

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Transthyretin and HDL Isolation from Human Serum

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Transthyretin (Prealbumin from human serum) was purchased as a lyophilised powder from Sigma Aldrich, Victoria, Australia. High-density lipoprotein (HDL) from human plasma was purchased as a solution from Sigma Aldrich, Victoria, Australia. Unless otherwise stated reagents were from Sigma Aldrich, Victoria, Australia.

Landers K.A., d'Emden M.C, & Richard K. (2019). Scavenger Receptor Class B Member 1 Independent Uptake of Transthyretin by Cultured Hepatocytes Is Regulated by High Density Lipoprotein. Journal of Lipids, 2019, 7317639.

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Carbonic Anhydrase Inhibition Assay

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Carbonic anhydrase (CA, from bovine erythrocytes), Bovine serum albumin (BSA, from bovine), Transthyretin (TTR, from human plasma), and other chemicals were purchased from Sigma-Aldrich chemical Co. S-allyl l-cysteine (SAC) was purchased from Cayman Chemicals. Methyl Glyoxal (MGO), Glyoxal (GO), Fructose, 8-Anilinonaphthalene-1-sulfonic acid (ANS), Dinitrophenyl hydrazine (DNPH), p-Nitrophenyl acetate (p-NPA), 2-Thiobarbituric acid (TBA) and N-acetyl l-cysteine (NAC) were also obtained from Sigma Chemical Co.

Bhattacharya R., Saini S., Ghosh S., Roy P., Ali N., Parvez M.K., Al-Dosari M.S., Mishra A.K, & Singh L.R. (2023). Organosulfurs, S-allyl cysteine and N-acetyl cysteine sequester di-carbonyls and reduces carbonyl stress in HT22 cells. Scientific Reports, 13, 13071.

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