Name: Two-dimensional gel of Spartina alterniflora
Description: Heat-stable proteins (95C for 40 min) were extracted from Spartina alterniflora, and separated on two-dimensinoal gels (pI 3-10 NL, 24 cm IPG).
Version: MIAPE: Gel Electrophoresis 1.4
1. General features
1.1.1 Date Stamp
2011-01-05
1.1.2 Responsible person or role
Affiliation: Louisiana State University, AgCenter
(i) Name: Wang, Yi
(ii) Postal address: Department of Plant Pathology and Crop Physiology
302 Life Sciences Building
Louisiana State University
Baton Rouge, LA 70803
(iii) Email address: ywang17@tigers.lsu.edu
1.1.3 Electrophoresis type
Two-Dimensional electrophoresis
2. Sample
2.1.1 Sample Name(s)
-
- Sample name: Heat stable proteins from Spartina alterniflora seeds
- Sample type: Test sample
2.1.2 Loading buffer
- 7M urea, 2M thiourea, 4% CHAPS (w/v) and 20mM dithiothreitol (DTT), 2% (w/v) IPG buffer NL 3-10. Rehydration buffer: 7 M urea, 2 M thiourea, 0.001% (w/v) bromophenol, 2% (w/v) CHAPS, 20 mM DTT and 0.5% (w/v) IPG buffer NL 3-10.
3. Gel matrix and electrophoresis protocol
3.1 Dimension details
3.1.1 Ordinal number for this dimension
First
3.1.2 Separation method employed
Isoelectric focusing (IEF)
3.2 Gel Matrix
3.2.1 Description of gel matrix
IPG strip
Denaturing
3.2.2 Gel manufacture
Gel was purchased precast.
Manufacturer: GE Healthcare
Model: Immobiline DryStrip pH 3-10 NL, 24 cm
Model number: 17-6002-45
Batch number: 10057246
3.2.3 Physical dimensions
X: 240 mm
Y: 3 mm
Z: 0.5 mm
3.2.4 Physiochemical property range and distribution
NL pH 3 - 10
3.2.5 Acrylamide concentration
4 %
3.2.6 Acrylamide : Crosslinker ratio
Crosslinker: Bisacrylamide
Ratio: 32:1
3.2.7 Additional substances in gel
No additional substance
3.2.8 Gel lane
53.2.9 Sample application
Lane 1
- Sample: Heat stable proteins from Spartina alterniflora seeds
- Volume of sample: 1000 µg
- Loading buffer: 7M urea, 2M thiourea, 4% CHAPS (w/v) and 20mM dithiothreitol (DTT), 2% (w/v) IPG buffer NL 3-10. Rehydration buffer: 7 M urea, 2 M thiourea, 0.001% (w/v) bromophenol, 2% (w/v) CHAPS, 20 mM DTT and 0.5% (w/v) IPG buffer NL 3-10.
- Volume of loading buffer: 30 µL
Lane 2
- Sample: Heat stable proteins from Spartina alterniflora seeds
- Volume of sample: 1000 µg
- Loading buffer: 7M urea, 2M thiourea, 4% CHAPS (w/v) and 20mM dithiothreitol (DTT), 2% (w/v) IPG buffer NL 3-10. Rehydration buffer: 7 M urea, 2 M thiourea, 0.001% (w/v) bromophenol, 2% (w/v) CHAPS, 20 mM DTT and 0.5% (w/v) IPG buffer NL 3-10.
- Volume of loading buffer: 30 µL
Lane 3
- Sample: Heat stable proteins from Spartina alterniflora seeds
- Volume of sample: 1000 µg
- Loading buffer: 7M urea, 2M thiourea, 4% CHAPS (w/v) and 20mM dithiothreitol (DTT), 2% (w/v) IPG buffer NL 3-10. Rehydration buffer: 7 M urea, 2 M thiourea, 0.001% (w/v) bromophenol, 2% (w/v) CHAPS, 20 mM DTT and 0.5% (w/v) IPG buffer NL 3-10.
- Volume of loading buffer: 30 µL
Lane 4
- Sample: Heat stable proteins from Spartina alterniflora seeds
- Volume of sample: 1000 µg
- Loading buffer: 7M urea, 2M thiourea, 4% CHAPS (w/v) and 20mM dithiothreitol (DTT), 2% (w/v) IPG buffer NL 3-10. Rehydration buffer: 7 M urea, 2 M thiourea, 0.001% (w/v) bromophenol, 2% (w/v) CHAPS, 20 mM DTT and 0.5% (w/v) IPG buffer NL 3-10.
- Volume of loading buffer: 30 µL
Lane 5
- Sample: Heat stable proteins from Spartina alterniflora seeds
- Volume of sample: 1000 µg
- Loading buffer: 7M urea, 2M thiourea, 4% CHAPS (w/v) and 20mM dithiothreitol (DTT), 2% (w/v) IPG buffer NL 3-10. Rehydration buffer: 7 M urea, 2 M thiourea, 0.001% (w/v) bromophenol, 2% (w/v) CHAPS, 20 mM DTT and 0.5% (w/v) IPG buffer NL 3-10.
- Volume of loading buffer: 30 µL
Loading method: rehydration loading.
Additional comment: Immobiline DryStrip IPGbox rehydration for 12 hours.
3.3 Protocol
3.3.1 Buffers
No buffer.
3.3.2 Electrophoresis conditions
Running temperature: 20 °C
Hold: 500 V, 2 h
Hold: 1000 V, 2 h
Gradient: 1000-8000 V, 2 h
Hold: 8000 V, 3 h
Gradient: 8000-10000 V, 1 h
Hold: 10000 V, 1 h
4. Inter-dimension Process
4.1 Protocol
4.1.1 Step name
reduction
4.1.2 Inter dimension buffer
50 mM Tris-HCl (pH 8.8), 6 M urea, 30% glycerol (v/v), 2% SDS (w/v), 0.002% (w/v) bromophenol
4.1.3 Additional reagents
0.5% DTT (w/v)
4.1.4 Equipment
Manufacturer: unknown
Model: Equilibrium tray 12 wells
Model number: unknown
4.1.5 Protocol
Temperature: 22 °C.
Duration: 30 min.
Protocol:
Strips immersed in individual wells of a rehydration tray and kept shaking for 30 minutes.
4.1.1 Step name
alkylation
4.1.2 Inter dimension buffer
50 mM Tris-HCl (pH 8.8), 6 M urea, 30% glycerol (v/v), 2% SDS (w/v), 0.002% (w/v) bromophenol
4.1.3 Additional reagents
1.25% Iodoacetamide (w/v)
4.1.4 Equipment
Manufacturer: unknown
Model: Equilibrium tray 12 wells
Model number: unknown
4.1.5 Protocol
Temperature: 22 °C.
Duration: 40 min.
Protocol:
Strips immersed in individual wells of a rehydration tray and kept shaking for 40 minutes.
3. Gel matrix and electrophoresis protocol
3.1 Dimension details
3.1.1 Ordinal number for this dimension
Second
3.1.2 Separation method employed
Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE)
3.2 Gel Matrix
3.2.1 Description of gel matrix
slab gel
Denaturing
3.2.2 Gel manufacture
Gel was manufactured using the following receipe:
A recipe to prepare 1200 ml of 12.5% polyacrylamide gels [150.0 g acrylamide, 4.032 g bis-acrylamide, 1.5 M Tris-HCl pH 8.8, 10% SDS (w/v), 10% APS (w/v) and 340 µl TEMED] (the stirred gel solution was degassed under vacuum for 20 minutes, and APS and TEMED were not added until gels were ready to pour) was used to make 12 gels.
3.2.3 Physical dimensions
X: 260 mm
Y: 200 mm
Z: 1 mm
3.2.4 Physiochemical property range and distribution
logarithmic apparent molecular mass 100 - 6 kDa
3.2.5 Acrylamide concentration
12.5 %
3.2.6 Acrylamide : Crosslinker ratio
Crosslinker: Bisacrylamide
Ratio: 37.2:1
3.2.7 Additional substances in gel
No additional substance
3.2.8 Gel lane
53.2.9 Sample application
Loading method: IPG strip.
Additional comment: IPG strip was placed on top of the slab gel and held in place with Agarose Sealing Solution (0.5% agarose in 1x SDS Electrophoresis Buffer).
3.3 Protocol
3.3.1 Buffers
1x SDS running buffer: 2.5 mM Tris-base pH 8.3, 19.2 mM glycine and 0.01 % (w/v) SDS.
2x SDS topping buffer: 5 mM Tris-base pH 8, 38.4 mM glycine and 0.02% (w/v) SDS.
3.3.2 Electrophoresis conditions
Running temperature: 18 °C
Hold: 40 V, 1 h
Hold: 110 V, 13 h
5. Detection
5.1 Direct detection
5.1.1 Name of direct detection_process
Colloidal Coomassie Blue G-250 staining (Blue silver staining)
5.1.2 Direct detection agents
2% H3PO4, 10% (NH4)2SO4, 20% methanol and 0.1% Coomassie G-250.
The preparation of the staining recipe (10 L) was by sequentially addition as follows: 235 ml of phosphoric acid (85%, w/v) was added to 2 L of distilled water; 1 kg of ammonium sulfate powder was added to 4 L of distilled water. After they were fully dissolved, phosphoric acid and ammonium sulfate solutions were combined and poured into the staining tank together with 1.5 L of distilled water. Ten grams of Coomassie Brilliant Blue G-250 were dissolved in 500 ml distilled water, and then added to staining tank. Two liters of methanol were not added to staining tank until the gel staining began.
5.1.3 Additional reagents and buffers
No additional reagents or buffer
5.1.4 Equipment
Manufacturer: Bio-Rad
Model: Dodeca Stainer
Model number: #165-3401
5.1.5 Direct detection protocol
Temperature: 22 °C.
Duration: 4 d.
Protocol:
The staining took place for 2-3 days, and gels were de-stained with distilled water until the background was clear (8-10 hours in most cases).
6. Image Acquisition
6.1 Acquisition Equipment
6.1.1 Type of equipment
Professional scanner6.1.2 Name of equipment
Manufacturer: UMAX
Model: UTA
Model number: 1100
6.1.3 Software
Manufacturer: UMAX
Model: Magicscan
Model number: 4.5
6.1.4 Calibration
Yes (automatic)
6.1.5 Equipment specific parameters
Default (vendor) parameters.6.2 Acquisition Protocol
6.2.1 Image acquisition process
The gel images were acquired in 16 bit grayscale with a resolution of 300 dpi and were saved in tiff format. No filters or image processing tools were used during acquisition.6.2.2 Reference to gel matrix
There is only one gel in this document.
7. Image
7.1.1 Image name (or id)
SA Gel #1 - #5 (format: TIFF)
7.1.2 Dimensions
Width: 2196 px
Height: 2954 px
7.1.3 Resolution
300 dpi
7.1.4 Bit-depth
16-bit (HighColor)7.1.5 Image location
sa #1.tif7.1.6 Standard image orientation
Yes