Information for Peptide: ALDFNTR from SHC1_HUMAN

1. Biological Peptide

1.1 Native Sequence

    R.ALDFNTR.T

1.2 Peptide Properties

Start Stop MW m/z for 2+ m/z for 3+ pI
178 184 835.42 418.72 279.48 5.88

1.3 Fragment Ion Table

AA b Ion Series b Ion Mass y Ion Series y Ion Mass
A b y
L b y
D b y
F b y
N b y
T b y
R b y

2. Synthetic Peptide

2.1 Synthetic (Internal Standard) Peptide Sequence

ALDF(C9N1)NTR (Modification: Stable isotope on F4 (13-UC9, 15N) )

2.2 Peptide Properties

MW m/z for 2+ m/z for 3+ pI
845.45 423.73 282.82 5.88

2.3 Fragment Ion Table

AA b Ion Series b Ion Mass y Ion Series y Ion Mass
A b y
L b y
D b y
F b y
N b y
T b y
R b y

2.4 Peptide Synthesis Report

Click to view/download synthesis report for ALDFNTR

2.5 QqQ MS/MS

Transition Table:

Transition m/z of Transition Collision Energy
y3 390.21 18.0
y4 547.28 18.0
y5 662.3 18.0
y6 775.39 18.0

2.6 Calibration Curve of Standard

Description: NONE

 

Experiment Description: Cells from Melanoma cell lines were lysed in RIPA buffer. The equivalent of 200,000 cells were loaded onto an SDS gel. The protein of interest was excised and ingel digestion with trypsin was performed after reduction and alkylation with TCEP and IAA. 1/6 of the resulting digest was then analyzed on a Thermo Scientific TSQ mass spectrometer. Internal standard was injected concurrently.

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