Information for Peptide: GECVPGEQEPEPILIPR from AMBP_HUMAN
1. Biological Peptide
1.1 Native Sequence
R.GECVPGEQEPEPILIPR.V
1.2 Peptide Properties
| Start | Stop | MW | m/z for 2+ | m/z for 3+ | pI |
|---|---|---|---|---|---|
| 186 | 202 | 1861.92 | 931.97 | 621.65 | 4.09 |
1.3 Fragment Ion Table
| AA | b Ion Series | b Ion Mass | y Ion Series | y Ion Mass |
|---|---|---|---|---|
| G | b | y | ||
| E | b | y | ||
| C | b | y | ||
| V | b | y | ||
| P | b | y | ||
| G | b | y | ||
| E | b | y | ||
| Q | b | y | ||
| E | b | y | ||
| P | b | y | ||
| E | b | y | ||
| P | b | y | ||
| I | b | y | ||
| L | b | y | ||
| I | b | y | ||
| P | b | y | ||
| R | b | y |
2. Synthetic Peptide
2.1 Synthetic (Internal Standard) Peptide Sequence
(NONE)
2.2 Peptide Properties
(NONE)
2.3 Fragment Ion Table
(NONE)
2.4 Peptide Synthesis Report
(NONE)
2.5 QqQ MS/MS
2.6 Calibration Curve of Standard
Description: NONE
Experiment Description: Control urine was processed via ultrafiltration according to Moffitt Proteomics protocol and subjected to in-solution digestion with trypsin, following thermal denaturation, reduction, and alkylation.
2.7 LC-MRM Analysis of Biological and Standard Peptides Illustrates Elution Times
2.8 Pseudo MS/MS Comparison of Transition Patterns for Biological/Standard Peptides
