C reactive protein crp

Manufactured by Merck Group

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C-reactive protein (CRP) is a laboratory test that measures the level of this protein in the blood. CRP is produced by the liver and its levels increase in response to inflammation in the body.

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Lab products found in correlation

Victor x5 multilabel plate reader, by PerkinElmer (1 mentions) Leptin, by Thermo Fisher Scientific (1 mentions) Adiponectin, by R&D Systems (1 mentions) Ammonium acetate, by Merck Group (1 mentions) M nitrobenzyl alcohol, by Merck Group (1 mentions) Hplc grade water, by Merck Group (1 mentions) Triethylammonium acetate, by Merck Group (1 mentions) Human hemoglobin hb, by Merck Group (1 mentions)

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CRP (25 citations) Crp protein (2 citations)

2 protocols using c reactive protein crp

Serum Biomarker Quantification

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Blood was collected by cardiac puncture. Serum was separated and enzyme-linked immunosorbent assays were used to quantify adiponectin (R&D Systems Inc., Minneapolis, MN, USA), CD163 (Cusabio Biotech, Cedarlane Laboratories Ltd, Burlington, ON, Canada), C-reactive protein (CRP; EMD Millipore Corporation, Billerica, MA, Canada), interleukin 6 (IL-6; R&D Systems Inc.), leptin (Life Technologies Inc.), plasminogen activator inhibitor-1 (Oxford Biomedical Research, Cedarlane Laboratories Ltd), resistin (Bertin Pharma, Cayman Chemical Company, Ann Arbor, MI, USA) and tumor necrosis factor (TNF; R&D Systems Inc.) according to the manufacturer's instructions. Absorbance was read at 450 nm in a VICTOR X5 Multilabel Plate Reader (PerkinElmer Inc., Waltham, MA, USA).

Campioli E., Martinez-Arguelles D.B, & Papadopoulos V. (2014). In utero exposure to the endocrine disruptor di-(2-ethylhexyl) phthalate promotes local adipose and systemic inflammation in adult male offspring. Nutrition & Diabetes, 4(5), e115-.

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Protein Analysis by Nano-ESI

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Ammonium acetate, triethylAmmonium acetate (Sigma, St. Louis, MO), and m-nitrobenzyl alcohol (Aldrich) were dissolved in HPLC grade water (Millipore, Burlington, MA) to concentrations of 100 mM. Bovine Cu/Zn superoxide dismutase (SOD) was obtained from MP Biomedicals (Santa Ana, CA), streptavidin (SA) from ProteoChem (Hurricane, UT), human hemoglobin (Hb) from Sigma Aldrich (St. Louis, MO), transthyretin (TTR) from Lee BioSolutions (Maryland Heights, MO), and C-reactive protein (CRP) from EMD Millipore (Burlington, MA). Each protein was diluted to a 50 μM stock of the protein monomer in 100 mM Ammonium acetate and passed through a size exclusion spin column (BioRad, Hercules, CA) for purification. Samples analyzed by nano-ESI were prepared as described previously by Wysocki and coworkers.¹⁶ Briefly, each protein was diluted to 4–10 μM monomer in three types of solutions: “standard” native solutions containing 100 mM Ammonium acetate; charge-reducing solutions containing 20 mM triethylAmmonium acetate (TEAA) and 80 mM Ammonium acetate; and supercharging solutions containing 20 mM m-nitrobenzyl alcohol (m-NBA) and 80 mm Ammonium acetate. All protein solutions had a final pH of approximately 7.

Sipe S.N, & Brodbelt J.S. (2019). Impact of charge state on 193 nm ultraviolet photodissociation of protein complexes. Physical chemistry chemical physics : PCCP, 21(18), 9265-9276.

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