GE17-0051-01
Sephadex® G-75 Superfine
Cytiva 17-0051-01, pack of 100 g
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About This Item
UNSPSC Code:
23151817
NACRES:
NA.56
feature
autoclavable In wet form (pH 7.0) at 120°C for 30 min
packaging
pack of 100 g
manufacturer/tradename
Cytiva 17-0051-01
particle size
10-40 μm
22-143 μm (wet)
working range
2-10
Related Categories
General description
Sephadex® G-75 Superfine is well established gel filtration medium for desalting and buffer exchange of large biomolecules, for specific cases requiring very high resolution.
Application
Sephadex® is a gel filtration medium prepared by crosslinking Dextran with epichlorohydrin. Different types of Sephadex® differ in their degree of cross-linking and hence in their degree of swelling and their molecular fractionation range. Sephadex® G-10 is one of five different G-types ranging from G-10 for small molecules to G-75 for larger molecules. Sephadex® G-50 is available in 4 different particle sizes (Course, Medium, Fine & Superfine) and Superfine has the smallest bead size for higher efficiency with shorter diffusion distances. Cource and Medium are are preferred for large scale group separations where high flow rates and Low operating pressures are required.
Features and Benefits
- Quickly desalts, removes contaminants and transfers to a new buffer in a single step.
- Classic gel filtration medium.
Storage and Stability
Please be aware this product may be shipped 90 days before the expiration date. For more information on the batch specific expiration date, please contact technical service.
Analysis Note
To view the Certificate of Analysis for this product, please visit www.cytiva.com.
Legal Information
Sephadex is a registered trademark of Cytiva
Storage Class Code
13 - Non Combustible Solids
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Hedgehog Acyltransferase Promotes Uptake of Palmitoyl-CoA across the Endoplasmic Reticulum Membrane.
James J Asciolla et al.
Cell reports, 29(13), 4608-4619 (2019-12-26)
Attachment of palmitate to the N terminus of Sonic hedgehog (Shh) is essential for Shh signaling. Shh palmitoylation is catalyzed on the luminal side of the endoplasmic reticulum (ER) by Hedgehog acyltransferase (Hhat), an ER-resident enzyme. Palmitoyl-coenzyme A (CoA), the
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