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Invitrogen™
NuPAGE™ LDS Sample Buffer (4X)
NuPAGE LDS Sample Buffer (4X) is used to prepare protein samples for denaturing gel electrophoresis with Bis-Tris or Tris-Acetate gels.Read more
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| Catalog Number | Quantity |
|---|---|
| NP0007 | 10mL |
| NP0008 | 250mL |
Catalog number NP0007
Price (EUR)
26,65
Online Exclusive
28,16Save 1,51 (5%)
Each
-
Quantity:
10mL
Price (EUR)
26,65
Online Exclusive
28,16Save 1,51 (5%)
Each
NuPAGE LDS Sample Buffer (4X) is used to prepare protein samples for denaturing gel electrophoresis with Bis-Tris or Tris-Acetate gels. It contains lithium dodecyl sulfate, pH 8.4, which allows for maximum activity of the reducing agent.
See all available buffers and reagents available for SDS-PAGE
NuPAGE LDS Sample Buffer contains Coomassie G250 and Phenol Red as tracking dyes instead of bromophenol blue. Coomassie G250 gives a sharp dye front with both MES and MOPS SDS running buffers and migrates much closer to the moving ion front than bromophenol blue. Bromophenol blue runs more slowly than some peptides with MES SDS Running Buffer. This ensures that small peptides do not run off the gels.
To use: Heat the sample in a 1X dilution (reduced or non-reduced) at 70°C for 10 minutes for optimal results.
Note: NuPAGE LDS Sample Buffer should be brought to room temperature (25°C) prior to use. It is a highly viscous and concentrated solution containing twice the amount of LDS compared to the amount of SDS in typical sample buffers. NuPAGE LDS Sample Buffer also contains a higher concentration glycerol.
See all available buffers and reagents available for SDS-PAGE
NuPAGE LDS Sample Buffer contains Coomassie G250 and Phenol Red as tracking dyes instead of bromophenol blue. Coomassie G250 gives a sharp dye front with both MES and MOPS SDS running buffers and migrates much closer to the moving ion front than bromophenol blue. Bromophenol blue runs more slowly than some peptides with MES SDS Running Buffer. This ensures that small peptides do not run off the gels.
To use: Heat the sample in a 1X dilution (reduced or non-reduced) at 70°C for 10 minutes for optimal results.
Note: NuPAGE LDS Sample Buffer should be brought to room temperature (25°C) prior to use. It is a highly viscous and concentrated solution containing twice the amount of LDS compared to the amount of SDS in typical sample buffers. NuPAGE LDS Sample Buffer also contains a higher concentration glycerol.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
BufferSample Loading Buffers
Concentration4 X
Gel CompatibilityNuPAGE™ Gels
Product LineNuPAGE™
Product TypeLDS Sample Buffer
Quantity10mL
Shipping ConditionApproved for shipment at Room Temperature or on Wet Ice
Gel TypeNuPAGE
Unit SizeEach
Contents & Storage
Sample Buffer (4X) containing lithium dodecyl sulfate (LDS) at pH 8.5 with SERVA Blue G250 and phenol red.
Store at 4°C to 25°C.
Store at 4°C to 25°C.
Introducing iBlot 3 Western Blot Transfer System
Featuring higher throughput and built-in cooling for consistent protein transfer
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Lot #Certificate TypeDateCatalog Number(s)
3197456Certificate of AnalysisJun 04, 2025NP0007
3154062Certificate of AnalysisMay 16, 2025NP0007
3161011Certificate of AnalysisMay 09, 2025NP0008
3146929Certificate of AnalysisMar 21, 2025NP0008
3136399Certificate of AnalysisMar 10, 2025NP0007
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Safety Data Sheets
SDSProduct Information
Frequently asked questions (FAQs)
DTT is not stable, so it must be added and the reduction performed just prior to loading your samples.
Find additional tips, troubleshooting help, and resources within our Protein Gel 1D Electrophoresis Support Center.
Precipitation of the LDS or SDS at 4 degrees C is normal. Bring the buffer to room temperature and mix until the LDS/SDS goes into solution. If you do not want to wait for it to dissolve, you can store the sample buffer at room temperature.
Find additional tips, troubleshooting help, and resources within our Protein Gel 1D Electrophoresis Support Center.
While they are both Bis-Tris based gels, the chemistries are very different since Bolt gels are optimized for western blotting. Another key difference is the wedge well design of the Bolt gels, which allows larger sample volumes to be loaded.
Find additional tips, troubleshooting help, and resources within our Protein Gel 1D Electrophoresis Support Center.
The neutral operating pH of the NuPAGE Gels and buffers provides following advantages over the Laemmli system:
-Longer shelf life of 8-12 months due to improved gel stability
-Improved protein stability during electrophoresis at neutral pH resulting in sharper band resolution and accurate results (Moos et al, 1998)
-Complete reduction of disulfides under mild heating conditions (70 degrees C for 10 min) and absence of cleavage of asp-pro bonds using the NuPAGE LDS Sample buffer (pH > 7.0 at 70 degrees C)
-Reduced state of the proteins maintained during electrophoresis and blotting of the proteins by the NuPAGE Antioxidant
Please refer to the following paper: Moos M Jr, Nguyen NY, Liu TY (1988) Reproducible High Yield Sequencing of Proteins Electrophoretically Separated and Transferred to an Inert Support. J Biol Chem 263:6005-6008.
Find additional tips, troubleshooting help, and resources within our Protein Gel 1D Electrophoresis Support Center.
The composition of the 1X NuPAGE LDS Sample Buffer is as follows:
141 mM Tris base
106 mM Tris HCl
2% LDS
10% Glycerol
0.51 mM EDTA
0.22 mM SERVA Blue G
0.175 mM Phenol Red
pH 8.5
To prepare 10 mL of 4 X NuPAGE LDS Sample Buffer, dissolve the following reagents to 8 mL ultrapure water:
Tris HCl 0.666 g
Tris Base 0.682 g
LDS 0.800 g
EDTA 0.006 g
Glycerol 4 g
SERVA Blue G (1 solution) 0.75 mL
Phenol Red (1 solution) 0.25 mL
Mix well and adjust the volume to 10 mL with ultrapure water.
Store at +4. The buffer is stable for 6 months when stored at +4°C.
Find additional tips, troubleshooting help, and resources within our Protein Gel 1D Electrophoresis Support Center.
Citations & References (9)
Search citations by name, author, journal title or abstract text
Citations & References
Abstract
Characterization of four murine homologs of the human ov-serpin monocyte neutrophil elastase inhibitor MNEI (SERPINB1).
Journal:J Biol Chem
PubMed ID:12189154
'The human ov-serpin monocyte neutrophil elastase inhibitor (MNEI) is encoded by a single gene SERPINB1. It is a highly efficient inhibitor of neutrophil granule proteases. Four murine genes with high sequence identity with MNEI were identified and fully sequenced, and these were named EIA, EIB, EIC, and EID. EIA, EIB
Novel Modulation of Neuronal Nicotinic Acetylcholine Receptors by Association with the Endogenous Prototoxin lynx1.
Journal:Neuron
PubMed ID:11906696
We previously identified lynx1 as a neuronal membrane molecule related to snake alpha-neurotoxins able to modulate nAChRs. Here, we show that lynx1 colocalizes with nAChRs on CNS neurons and physically associates with nAChRs. Single-channel recordings show that lynx1 promotes the largest of three current amplitudes elicited by ACh through alpha(4)beta(2)
Apolipoprotein A-I is a selective target for myeloperoxidase-catalyzed oxidation and functional impairment in subjects with cardiovascular disease.
Journal:J Clin Invest
PubMed ID:15314690
In recent studies we demonstrated that systemic levels of protein-bound nitrotyrosine (NO(2)Tyr) and myeloperoxidase (MPO), a protein that catalyzes generation of nitrating oxidants, serve as independent predictors of atherosclerotic risk, burden, and incident cardiac events. We now show both that apolipoprotein A-I (apoA-I), the primary protein constituent of HDL, is
In vivo functional assay of a recombinant aquaporin in Pichia pastoris.
Journal:Appl Environ Microbiol
PubMed ID:16461705
The water channel protein PvTIP3;1 (alpha-TIP) is a member of the major intrinsic protein (MIP) membrane channel family. We overexpressed this eukaryotic aquaporin in the methylotrophic yeast Pichia pastoris, and immunogold labeling of cellular cryosections showed that the protein accumulated in the plasma membrane, as well as vacuolar and other
Spermidine but not spermine is essential for hypusine biosynthesis and growth in Saccharomyces cerevisiae: Spermine is converted to spermidine in vivo by the FMS1-amine oxidase.
Journal:Proc Natl Acad Sci U S A
PubMed ID:14617780
In our earlier work we showed that either spermidine or spermine could support the growth of spe2Delta or spe3Delta polyamine-requiring mutants, but it was unclear whether the cells had a specific requirement for either of these amines. In the current work, we demonstrate that spermidine is specifically required for the
9 total citations