A1653

Manufactured by Merck Group

Sourced in United States

A1653 is a laboratory instrument designed for conducting various analytical procedures. It is capable of performing precise measurements and data analysis. The core function of A1653 is to provide accurate and reliable results for research and testing applications.

Automatically generated - may contain errors

Lab products found in correlation

Human serum albumin (hsa), by Merck Group (3 mentions) A3782, by Merck Group (2 mentions) G 5009, by Merck Group (1 mentions) A3311, by Merck Group (1 mentions) A3139, by Merck Group (1 mentions) Tmb substrate, by Thermo Fisher Scientific (1 mentions) Prism software, by GraphPad (1 mentions) Human serum, by Merck Group (1 mentions) Milli q gradient water purification system, by Merck Group (1 mentions) Sodium hydroxide (naoh), by Agilent Technologies (1 mentions) Na2hpo4 2h2o, by Merck Group (1 mentions) Human serum albumin (hsa), by Thermo Fisher Scientific (1 mentions) Bsa a3912, by Merck Group (1 mentions)

5 protocols using a1653

Deionized Protein Stock Preparation

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Stock solutions of d-BSA, deionized HSA (d-HSA) and deionized BGG (d-BGG) were prepared as described
previously [6 , 8 (link)]. BSA (A3311,
Sigma-Aldrich, St. Louis, MO, USA), HSA (A1653, Sigma-Aldrich) or BGG (G5009, Sigma-Aldrich) was dissolved in
CZB medium [9 (link)] deprived of BSA and EDTA at a concentration of 12%.
Approximately 3 g of mixed ion-exchange resin beads (501-X8(D); Bio-Rad Laboratories, Hercules, CA, USA) was
then added to 10 ml of each solution, and the mixture was incubated at room temperature with occasional
stirring. When they changed color from blue-green to gold, the BSA, HSA and BGG solutions were transferred to
fresh beads for a total of three exchanges. The supernatants were collected and stored at 4 C as stock
solutions.

ISAJI Y., YOSHIDA K., IMAI H, & YAMADA M. (2015). An intracytoplasmic injection of deionized bovine serum albumin immediately after somatic cell nuclear transfer enhances full-term development of cloned mouse embryos. The Journal of Reproduction and Development, 61(6), 503-510.

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Quantification of Protein Binding Interactions

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Human serum albumin (HSA, 1 μg/mL, A1653, Sigma-Aldrich) or murine serum albumin (MSA, 1 μg/mL, A3139, Sigma-Aldrich) in 1 × phosphate-buffered saline (PBS) was coated in 96-well enzyme-linked immunosorbent assay (ELISA) plates at 4 °C overnight. ABD035-immunoGN, dAb7h8-immunoGN, and immunoGN (1 mg/mL) were added and incubated for 2 h at 25 °C, followed by incubation with the anti-His antibody at 25 °C for 2 h. After being extensively washed six times with wash buffer (0.05 % Tween 20 in 1 × PBS), a secondary horseradish peroxidase (HRP)-conjugated antibody was added and detected using TMB substrate (Thermo Fisher Scientific, Waltham, MA, USA). Data were analyzed using GraphPad Prism software (version 8.0; GraphPad Software Inc., USA).

Xing Y., Zhang F., Yang T., Yin C., Yang A., Yan B, & Zhao J. (2024). Augmented antitumor immune responses of HER2-targeted pyroptotic induction by long-lasting recombinant immunopyroptotins. Heliyon, 10(9), e30444.

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Ruthenium(II) Complexes for Protein Binding

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[Ru^II(cym)(8-HQ)Cl] 1, [Ru^II(cym)(8-HQ)(PTA)](SO₃CF₃) 2, [Ru^II(cym)(PCA)Cl]Cl 3, and the internal standard [tris(acetylacetonato)cobalt(III)] [Co(acac)₃] were prepared according to literature procedures.^8–10^,²⁷ Water (18 MΩ) used throughout these experiments was obtained from a Millipore Milli-Q Gradient Water Purification System. Methanol was purchased from Macron Fine Chemicals^TM. The background electrolyte (BGE) for the CE studies was a 20 mM phosphate buffer (pH 7.4) which was prepared from H₂O (18 MΩ), NaH₂PO₄·2H₂O (99%, AK Scientific), and Na₂HPO₄·2H₂O (≥99.5%, Sigma-Aldrich). Reagents used for CE conditioning were NaOH (1.0 M, Agilent Technologies) and HCl (36.5-38%, J.T. Baker).
Protein interaction studies were carried out using HSA (≥99%, Sigma-Aldrich, A3782 fatty acid free) and Tf (≥98%, Sigma-Aldrich). Interactions with cell medium and human serum were investigated using αMEM cell culture medium (Life Technologies) spiked with 5% fetal bovine serum (FBS) (Moregate BioTech), and human serum (from human male AB plasma, US origin, sterile filtered, Sigma-Aldrich), respectively. HSA binding site displacement studies were conducted with Wf (≥97%, Sigma-Aldrich), Ds (≥99.5%, Sigma-Aldrich), and HSA (lyophilized powder, ≥96%, Sigma-Aldrich, A1653).

Riisom M., Eade L., Tremlett W.D, & Hartinger C.G. (2022). The aqueous stability and interactions of organoruthenium compounds with serum proteins, cell culture medium, and human serum. Metallomics: Integrated Biometal Science, 14(7), mfac043.

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Characterization of HSA-DHLA Interaction

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All chemicals used were of analytical grade and were purchased from Sigma (Burlington, Massachusetts, USA). Stock solution of HSA, purchased from Sigma (A-1653) and used without additional purification, was made by dissolving HSA in 10 mM PBS, pH 7.4. The concentration of HSA was determined by using bicinchoninic acid (BCA) assay kit (Thermo Fisher Scientific, Waltham, Massachusetts, USA). Stock solution (5 mM) of DHLA was prepared by suspending DHLA in 10 mM PBS and then adding a small volume of 1 M NaOH until full clarification of solution was reached (Perricone et al., 1999) (link). Trypsin was purchased from the Institute Torlak (Belgrade, Serbia) as a 0.25 % solution. All experiments were performed in triplicate at room temperature, using 10 mM PBS, pH 7.4, unless otherwise stated.

Gligorijević N., Šukalović V., Miljuš G., Nedić O., & Penezić A. (2020). Dihydro-alpha-lipoic acid binds to human serum albumin at Sudlow I binding site.

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Albumin and Cafestol Characterization

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HSA (A1653, 96-99%), HSA essentially fatty acid free (A3782, 99%), BSA (A3912, ≥ 96%) were purchased from Sigma-Aldrich Co. (St Louis, MO, USA) and used without further purification.
Their molecular weight were assumed to be 66.478 Da, 66.478 Da and 66.463 Da respectively.
Stock solutions of albumins were prepared by dissolving it in PBS (pH 7.4). All stock solutions were kept at 4 °C and then diluted to the required experimental sample concentrations (1.0 x 10 -6 M). Cafestol and 16OMC were provided by Illycaffè S.p.A. (AromaLab, TS, Italy). Cafestol and 16OMC stock solutions (1.25 mM, 2.5 mM e 5 mM) were prepared in DMSO.

Guercia E., Forzato C., Navarini L, & Berti F. (2016). Interaction of coffee compounds with serum albumins. Part II: Diterpenes. Food chemistry, 199.

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