| 00:00:00 | Welcome |
| 00:00:57 | "Power in numbers" - Learn more about your protein's behaviour and stability in formulation by adding light scattering functionality to your SEC system. |
| 00:03:22 | Proteins |
| 00:04:26 | Size Exclusion Chromatography (SEC) |
| 00:05:29 | Conventional SEC |
| 00:05:42 | Conventional SEC |
| 00:07:33 | Beta-amylase: Conventional SEC |
| 00:08:18 | BSA: Column calibration |
| 00:09:51 | Limitation of available standards |
| 00:11:07 | Limitations of Conventional SEC |
| 00:13:22 | Light Scattering Detectors |
| 00:13:58 | Advanced Detection SEC |
| 00:14:30 | Malvern SEC range |
| 00:15:12 | How does Light scattering Give me Molecular Weight? |
| 00:15:25 | Light Scattering Theory |
| 00:15:50 | Light Scattering Theory |
| 00:16:45 | Isotropic Scatterers |
| 00:17:46 | RIGHT-ANGLE LIGHT SCATTERING (RALS) |
| 00:18:14 | Anisotropic Scatterers |
| 00:20:06 | Multi-Angle Light Scattering (MALS) |
| 00:20:42 | Multi-Angle Light Scattering (MALS) |
| 00:22:23 | For more information …… |
| 00:22:52 | SEC-mals application examples |
| 00:23:01 | Oligomerization Vs. Aggregation |
| 00:23:36 | BSA molecular weight using MALS |
| 00:25:21 | BSA measurements with MALS |
| 00:26:08 | BSA: Column calibration vs MALS |
| 00:26:44 | Pepsin aggregation |
| 00:27:51 | Pepsin aggregation |
| 00:28:33 | Immunoglobulin G |
| 00:28:50 | IgG molecular weight |
| 00:30:04 | IgG – How does sample loading effect the result? |
| 00:31:01 | Aprotinin |
| 00:31:56 | IgM |
| 00:32:59 | IgM - Lambda |
| 00:33:51 | IgM Lambda – Angular dependence |
| 00:34:41 | IgM – Kappa |
| 00:36:01 | Combined SLS & DLS |
| 00:36:49 | Introduction |
| 00:38:14 | Why Combine SLS and DLS? |
| 00:39:37 | Why combine SLS and DLS |
| 00:41:32 | Malvern Zetasizer µV |
| 00:43:15 | Multiple Analysis Modes |
| 00:45:38 | Application examples of zetasiZer µV |
| 00:45:50 | DLS in Batch Mode |
| 00:47:55 | DLS in Batch Mode |
| 00:49:42 | SLS in Batch Mode |
| 00:51:05 | Flow Mode SLS and DLS |
| 00:53:14 | Flow Mode SLS and DLS |
| 00:55:14 | Summary |
| 00:57:36 | Thank you |
When developing a formulation stability profile for a biotherapeutics, one of the primary techniques used to identify the oligomeric state and presence or absence of aggregates is size exclusion chromatography (SEC). Traditionally, this technique provides a quantitative analysis of a sample by relating the retention volume of peaks present in the chromatogram to a calibration curve providing a basic identification of the relative molecular weight of each of the peaks.