Aggregation of Purified Protein Reference Materials Characterized by Asymmetric Flow Field Flow Fractionation
This is a file containing aggregation data for two proteins that were thermomechanically aggregated. The aggregated proteins were separated by asymmetric flow field flow fractionation and separated protein fractions were detected and quantified by UV spectrophotometry and multi-angle light scattering. The UV spectrophotometry was used to quantify the amount of residual monomer, which is reported herein. The multi-angle light scattering was fitted to a relevant model to calculate the molecular weight of the aggregated protein, also reported herein. The protein aggregation was characterized as a function of time and also the azide (preservative) concentration, which is indicated as being relevant to the aggregation process. The data contained here is plotted in a manuscript submitted to the Journal of Pharmaceutical Sciences and presented as part of that scientific record.
Complete Metadata
| @type | dcat:Dataset |
|---|---|
| accessLevel | public |
| bureauCode |
[
"006:55"
]
|
| contactPoint |
{
"fn": "Sean Lehman",
"hasEmail": "mailto:sean.lehman@nist.gov"
}
|
| description | This is a file containing aggregation data for two proteins that were thermomechanically aggregated. The aggregated proteins were separated by asymmetric flow field flow fractionation and separated protein fractions were detected and quantified by UV spectrophotometry and multi-angle light scattering. The UV spectrophotometry was used to quantify the amount of residual monomer, which is reported herein. The multi-angle light scattering was fitted to a relevant model to calculate the molecular weight of the aggregated protein, also reported herein. The protein aggregation was characterized as a function of time and also the azide (preservative) concentration, which is indicated as being relevant to the aggregation process. The data contained here is plotted in a manuscript submitted to the Journal of Pharmaceutical Sciences and presented as part of that scientific record. |
| distribution |
[
{
"title": "DOI Access for Aggregation of Purified Protein Reference Materials Characterized by Asymmetric Flow Field Flow Fractionation",
"accessURL": "https://doi.org/10.18434/M32270"
},
{
"title": "Aggregation of Purified Protein Reference Materials Characterized by Asymmetric Flow Field Flow Fractionation",
"format": ".xslx",
"mediaType": "application/vnd.openxmlformats-officedocument.spreadsheetml.sheet",
"description": "Data of aggregated NIST BSA (927f) and NISTmAb (8670) protein particles characterized by asymmetric flow field flow fractionation with UV spectrophotometry and mutli-angle static light scattering. Data is the monomer concentration and aggregate molecular weight calculated from this analysis.",
"downloadURL": "https://data.nist.gov/od/ds/mds2-2270/Protein%20Aggregation%20Summary%20Data.xlsx"
},
{
"title": "SHA256 File for Aggregation of Purified Protein Reference Materials Characterized by Asymmetric Flow Field Flow Fractionation",
"mediaType": "text/plain",
"downloadURL": "https://data.nist.gov/od/ds/mds2-2270/Protein%20Aggregation%20Summary%20Data.xlsx.sha256"
}
]
|
| identifier | ark:/88434/mds2-2270 |
| issued | 2020-08-21 |
| keyword |
[
"Biosciences and Health",
"electrical sensing zone",
"flow imaging",
"light obscuration",
"particle",
"protein aggregate",
"protein particle",
"subvisible particle",
"visible particle"
]
|
| landingPage | https://data.nist.gov/od/id/mds2-2270 |
| language |
[
"en"
]
|
| license | https://www.nist.gov/open/license |
| modified | 2020-07-23 00:00:00 |
| programCode |
[
"006:045"
]
|
| publisher |
{
"name": "National Institute of Standards and Technology",
"@type": "org:Organization"
}
|
| rights | https://www.nist.gov/topics/data/public-access-nist-research/copyright-fair-use-and-licensing-statements-srd-data-and |
| theme |
[
"Bioscience:Bioprocessing"
]
|
| title | Aggregation of Purified Protein Reference Materials Characterized by Asymmetric Flow Field Flow Fractionation |
