Thermal stability, ligand binding and allergenicity data of Mus m 1.0102 allergen and its cysteine mutants
The presented data were obtained with the lipocalin allergen Mus m 1.0102 and its cysteine mutants MM-C138A, MM-C157A and MM-C138,157A, whose structural features and unfold reversibility investigations are presented in the research article entitled “The allergen Mus m 1.0102: cysteine residues and m...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2020-04-01
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| Series: | Data in Brief |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2352340920302493 |
| _version_ | 1828761694688509952 |
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| author | Elena Ferrari Romina Corsini Samuele E. Burastero Fabio Tanfani Alberto Spisni |
| author_facet | Elena Ferrari Romina Corsini Samuele E. Burastero Fabio Tanfani Alberto Spisni |
| author_sort | Elena Ferrari |
| collection | DOAJ |
| description | The presented data were obtained with the lipocalin allergen Mus m 1.0102 and its cysteine mutants MM-C138A, MM-C157A and MM-C138,157A, whose structural features and unfold reversibility investigations are presented in the research article entitled “The allergen Mus m 1.0102: cysteine residues and molecular allergology” [1].The data were obtained by means of a Dynamic Light Scattering-based thermal stability assay, a Fluorescence-based ligand-binding assay and a basophil degranulation test, and describe proteins’ fold stability, ligand binding ability and allergenic potential, respectively. Analysis of the collected data produced the temperatures corresponding to the onset of the protein unfolding, the dissociation constants for N-Phenyl-1-naphthylamine ligand and the profiles of β-hexosaminidase release from RBL SX-38 cells, sensitized with the serum of selected allergic patients and incubated with increasing antigens concentrations.These data allow for comparison of the lipocalin allergen Mus m 1.0102 with its conserved cysteines mutants and, with regard to their potential application in allergy diagnostics and immunotherapy, they contribute to the process of recombinant allergen characterization and standardization. Keywords: Lipocalin allergen, Mus m 1 allergen, Thermal stability, Aggregation |
| first_indexed | 2024-12-11T01:32:55Z |
| format | Article |
| id | doaj.art-c80bcd3dc0754c8eaab8bb4ca00c34ac |
| institution | Directory Open Access Journal |
| issn | 2352-3409 |
| language | English |
| last_indexed | 2024-12-11T01:32:55Z |
| publishDate | 2020-04-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Data in Brief |
| spelling | doaj.art-c80bcd3dc0754c8eaab8bb4ca00c34ac2022-12-22T01:25:18ZengElsevierData in Brief2352-34092020-04-0129Thermal stability, ligand binding and allergenicity data of Mus m 1.0102 allergen and its cysteine mutantsElena Ferrari0Romina Corsini1Samuele E. Burastero2Fabio Tanfani3Alberto Spisni4Dept. Medicine and Surgery, University of Parma, via Gramsci 14, 43126 Parma, ItalyDept. Medicine and Surgery, University of Parma, via Gramsci 14, 43126 Parma, ItalyDiv. Immunology, IRCCS San Raffaele, Via Olgettina 60, 20132 Milano, ItalyDept. Life and Environmental Sciences, Marche Polytechnic University, via Brecce Bianche, 60131 Ancona, ItalyDept. Medicine and Surgery, University of Parma, via Gramsci 14, 43126 Parma, Italy; Corresponding author.The presented data were obtained with the lipocalin allergen Mus m 1.0102 and its cysteine mutants MM-C138A, MM-C157A and MM-C138,157A, whose structural features and unfold reversibility investigations are presented in the research article entitled “The allergen Mus m 1.0102: cysteine residues and molecular allergology” [1].The data were obtained by means of a Dynamic Light Scattering-based thermal stability assay, a Fluorescence-based ligand-binding assay and a basophil degranulation test, and describe proteins’ fold stability, ligand binding ability and allergenic potential, respectively. Analysis of the collected data produced the temperatures corresponding to the onset of the protein unfolding, the dissociation constants for N-Phenyl-1-naphthylamine ligand and the profiles of β-hexosaminidase release from RBL SX-38 cells, sensitized with the serum of selected allergic patients and incubated with increasing antigens concentrations.These data allow for comparison of the lipocalin allergen Mus m 1.0102 with its conserved cysteines mutants and, with regard to their potential application in allergy diagnostics and immunotherapy, they contribute to the process of recombinant allergen characterization and standardization. Keywords: Lipocalin allergen, Mus m 1 allergen, Thermal stability, Aggregationhttp://www.sciencedirect.com/science/article/pii/S2352340920302493 |
| spellingShingle | Elena Ferrari Romina Corsini Samuele E. Burastero Fabio Tanfani Alberto Spisni Thermal stability, ligand binding and allergenicity data of Mus m 1.0102 allergen and its cysteine mutants Data in Brief |
| title | Thermal stability, ligand binding and allergenicity data of Mus m 1.0102 allergen and its cysteine mutants |
| title_full | Thermal stability, ligand binding and allergenicity data of Mus m 1.0102 allergen and its cysteine mutants |
| title_fullStr | Thermal stability, ligand binding and allergenicity data of Mus m 1.0102 allergen and its cysteine mutants |
| title_full_unstemmed | Thermal stability, ligand binding and allergenicity data of Mus m 1.0102 allergen and its cysteine mutants |
| title_short | Thermal stability, ligand binding and allergenicity data of Mus m 1.0102 allergen and its cysteine mutants |
| title_sort | thermal stability ligand binding and allergenicity data of mus m 1 0102 allergen and its cysteine mutants |
| url | http://www.sciencedirect.com/science/article/pii/S2352340920302493 |
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