University of Massachusetts Amherst

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Sample Submission

 
This is what I need to do to submit a sample.
 
How to fill out the service request form?

Use Adobe Reader/Acrobat to fill out the request form electronically as use of most of the web browsers will disable its fillable feature. Fill out submitter and sample information parts completely. Check all suitable solvents from the list and include others into the "other" box. Choose appropriate ionization method (EI, FAB, MALDI, ESI, LC-ESI) and mass measurement accuracy (Low-Res or High-Res). Measurement accuracy expected at Low-Res is about +-0.05 Da for EI, FAB, ESI methods. Mass accuracy at High-Res is better than 5ppm and needed in general for publication purposes.Print out the form and attach your labeled sample at the top-right corner of the form (within "attach your sample here" box).

To drop off stable samples for service analysis, please deliver them with completed submission form to the lab in Conte Building Room B-162.

For samples that need refrigeration or freezing, please deliver directly to Dr. Eyles in the (LSL) Life Science Laboratories Room S503.  LSL is located at 240 Thatcher Road, Amherst MA 01003. Campus maps can be found here

Samples for FAB or EI MS

Samples should be relatively pure, with no salts or buffers present.

Sample quantity requirements: 0.5 - 1 mg dry

Samples for ESI and MALDI MS

Water, methanol, acetonitrile, tetrahydrofuran, propanol, ethanol, toluene, dichloromethane, nitromethane are ESI and MALDI compatible solvents.

Non-volatile solvents (e.g., dimethylformamide (DMF) or dimethyl sulfoxide (DMSO)) are NOT MS friendly. Please avoid using them. 

Protein samples for ESI or MALDI MS should be prepared using ultra-pure water (MilliQ 18MΩ cm, or LC-MS grade bottled water). Common buffers (Tris-HCl, HEPES, phosphate buffers) are NOT compatible with MS.  They contain non-volatile electrolytes, which cause suppression of ESI/MALDI signal and/or extensive adduct formation. Protein solutions must be buffer exchanged to ESI-friendly solvent systems (e.g., denaturing solvent: 50%:47% water/methanol and 3% acetic acid; up to 100 mM ammonium acetate or ammonium bicarbonate buffers for native proteins or non-covalent complex measurements) prior to mass analysis. Both standard dialysis by diffusion across cellulose tubing/resin-based column and centrifugal ultra-filtration (using centrifugal micro-concentrators) are reliable techniques with regard to MS standards for desalting, concentration, buffer exchange and removal of low molecular weight impurities.