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Citations & References (7)
Invitrogen™
UltraPure™ 1 M Tris-HCI Buffer, pH 7.5
UltraPure™ 1 M Tris-HCl Buffer, pH 7.5, is a premixed, pH-adjusted, sterile-filtered solution. Prepared as a 1 M concentrate, thisRead more
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| Catalog Number | Quantity |
|---|---|
| 15567027 | 1 L |
Catalog number 15567027
Price (USD)
73.65
Online Exclusive
80.50Save 6.85 (9%)
Each
In stock
Quantity:
1 L
Price (USD)
73.65
Online Exclusive
80.50Save 6.85 (9%)
Each
UltraPure™ 1 M Tris-HCl Buffer, pH 7.5, is a premixed, pH-adjusted, sterile-filtered solution. Prepared as a 1 M concentrate, this buffer can be diluted to the desired concentration and used in molecular biology or general biochemistry applications.
Performance and quality testing
No DNase, RNase, or protease activity detected.
Performance and quality testing
No DNase, RNase, or protease activity detected.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Concentration1 M
FormLiquid
Product LineUltraPure™
Product TypeTris-HCl Buffer
Quantity1 L
Shipping ConditionRoom Temperature
pHpH 7.5
Unit SizeEach
Contents & Storage
Store in refrigerator (2-8°C). UltraPure™ 1M Tris-HCl, pH 7.5 is guaranteed for 6 months from date of purchase unless otherwise indicated in product documentation.
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Lot #Certificate TypeDateCatalog Number(s)
3118254Certificate of AnalysisJul 04, 202515567027
3174001Certificate of AnalysisJun 04, 202515567027
3153788Certificate of AnalysisMay 02, 202515567027
3115912Certificate of AnalysisMar 23, 202515567027
3011192Certificate of AnalysisFeb 19, 202515567027
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SDSCitations & References (7)
Search citations by name, author, journal title or abstract text
Citations & References
Abstract
Electrochemical sensor for multiplex biomarkers detection.
Journal:Clin Cancer Res
PubMed ID:19509137
'Multiplexing assay of biomarkers at the point-of-care is an elusive goal for molecular diagnostics. Here, we report an electrochemical (EC) sensor for oral cancer detection based on the simultaneous detection of two salivary biomarkers: interleukin (IL)-8 mRNA and IL-8 protein. Under the multiplexing mode, the limit of detection of salivary
Size-based separations as an important discriminator in development of proximity ligation assays for protein or organism detection.
Journal:Electrophoresis
PubMed ID:20419707
'Proximity ligation is a powerful technique to measure minute concentrations of target protein with high specificity, and it has been demonstrated to be effective on a wide variety of protein targets. The proximity ligation assay (PLA) technique is shown to be compromised by the amplification of a nonspecific fluorescent product
Eps homology domain endosomal transport proteins differentially localize to the neuromuscular junction.
Journal:Skelet Muscle
PubMed ID:22974368
'Recycling of endosomes is important for trafficking and maintenance of proteins at the neuromuscular junction (NMJ). We have previously shown high expression of the endocytic recycling regulator Eps15 homology domain-containing (EHD)1 proteinin the Torpedo californica electric organ, a model tissue for investigating a cholinergic synapse. In this study, we investigated
Unlike CD4+ T-cell help, CD28 costimulation is necessary for effective primary CD8+ T-cell influenza-specific immunity.
Journal:Eur J Immunol
PubMed ID:22585421
The importance of costimulation on CD4(+) T cells has been well documented. However, primary CTLs against many infections including influenza can be generated in the absence of CD4(+) T-cell help. The role of costimulation under such
Enzymatic route to preparative-scale synthesis of UDP-GlcNAc/GalNAc, their analogues and GDP-fucose.
Journal:Nat Protoc
PubMed ID:20224564
Enzymatic synthesis using glycosyltransferases is a powerful approach to building polysaccharides with high efficiency and selectivity. Sugar nucleotides are fundamental donor molecules in enzymatic glycosylation reactions by Leloir-type glycosyltransferases. The applications of these donors are restricted by their limited availability. In this protocol, N-acetylglucosamine (GlcNAc)/N-acetylgalactosamine (GalNAc) are phosphorylated by N-acetylhexosamine
7 total citations