Information for Peptide: EQVANSAFVER from HS90B_HUMAN

1. Biological Peptide

1.1 Native Sequence

    K.EQVANSAFVER.V

1.2 Peptide Properties

Start	Stop	MW	m/z for 2+	m/z for 3+	pI
492	502	1248.61	625.31	417.21	4.53

1.3 Fragment Ion Table

AA	b Ion Series	b Ion Mass	y Ion Series	y Ion Mass
E	b		y
Q	b		y
V	b		y
A	b		y
N	b		y
S	b		y
A	b		y
F	b		y
V	b		y
E	b		y
R	b		y

2. Synthetic Peptide

2.1 Synthetic (Internal Standard) Peptide Sequence

EQVANSAFV(C5N1)ER (Modification: Stable Isotope on v9 (U-13C, 15N) )

2.2 Peptide Properties

MW	m/z for 2+	m/z for 3+	pI
1254.62	628.32	419.22	4.53

2.3 Fragment Ion Table

AA	b Ion Series	b Ion Mass	y Ion Series	y Ion Mass
E	b		y
Q	b		y
V	b		y
A	b		y
N	b		y
S	b		y
A	b		y
F	b		y
V	b		y
E	b		y
R	b		y

2.4 Peptide Synthesis Report

Click to view/download synthesis report for EQVANSAFVER

2.5 QqQ MS/MS

Transition Table:

Transition	m/z of Transition	Collision Energy
y4	556.31	24.0
y5	627.35	24.0
y6	714.36811	24.0
y7	828.42	24.0
y8	899.44815	24.0
y9	998.51656	24.0

2.6 Calibration Curve of Standard

Description: NONE

 

Experiment Description: Cells from AML line U937 were lysed in 8M urea/ 100mM ammonium bicarbonate buffer on ice. The equivalent of 100,000 cells were loaded onto a SDS gel. The protein of interest was excised and ingel digestion with trypsin was performed after reduction and alkylation with TCEP and IAA. 1/4 of the resulting digest was then analyzed on a Thermo Scientific TSQ mass spectrometer.

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