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G10120

Sigma-Aldrich

Sephadex® G-10

Medium

Synonym(s):

Gel filtration resin, Sephadex G-10 Medium

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About This Item

CAS Number:
MDL number:
UNSPSC Code:
23151817
NACRES:
NA.56

technique(s)

protein array: suitable

matrix active group

phase

swelling

1 g swells to 2-3 mL

application(s)

life science and biopharma

compatibility

Cytiva

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General description

Sephadex G-10 is a well-established gel filtration resin specifically designed for desalting and buffer exchange of peptides and small biomolecules. It boasts the smallest exclusion limit within the Sephadex range, making it highly effective in these applications. Sephadex itself is a gel filtration resin that is created through the crosslinking of dextran with epichlorohydrin. The various types of Sephadex exhibit different degrees of cross-linking, leading to variations in swelling properties and molecular fractionation range. Sephadex G-10 falls into the category of G-types, alongside four other types, ranging from G-10 for small molecules to G-75 for larger molecules.

Application

Sephadex® G-10 has been used as a size exclusion material for the separation of the conjugated N-glycans from the surplus dye. It has also been used in desalting for reducing salt concentration for anion-exchange (AEx), cation-exchange (CEx) chromatography.
Sephadex® G-10 has been used for the reconstitution of membrane proteins into a giant proteoliposome.

Biochem/physiol Actions

Sephadex G-10 serves as a gel filtration medium for gel filtration chromatography and protein chromatography. Its versatility is demonstrated by its applications in cancer studies and its ability to determine fluoride levels in diverse samples, including tap water, river water, and green tea samples.

Features and Benefits

  • Desalts, removes contaminants, and transfers to a new buffer in one step.
  • Suitable for buffer exchange and cleanup of biological samples,
  • Effective for peptides, small proteins, and oligosaccharides with a molecular weight larger than 700.
  • Efficiently removes salts, dyes, and radioactive labels.
  • Lowest exclusion limit of 700 molecular weight in the Sephadex G-range

Legal Information

Sephadex is a registered trademark of Cytiva

comparable product

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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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M Muirhead et al.
International journal of cell cloning, 8(6), 392-408 (1990-11-01)
We have cloned a stromal cell from mouse bone marrow selected on the basis of its ability to promote the growth of an Abelson virus-transformed pre-B cell line. These stromal cells have smooth muscle features, and the ultrafiltrate of stromal
Kwang Wook Hyun et al.
Peptides, 27(6), 1173-1178 (2005-11-18)
This study describes the extraction and characterization of a platelet aggregation inhibitory peptide from Inonotus obliquus. Ethanol extract from I. obliquus ASI 74006 mycelia showed the highest platelet aggregation inhibitory activity (81.2%). The maximum platelet aggregation inhibitory activity was found
H Han et al.
Nucleic acids research, 22(14), 2837-2844 (1994-07-25)
Different helical conformations of DNA (D), RNA (R), and DNA.RNA (DR) hybrid double and triple helices have been detected using affinity cleavage analysis. Synthetic methods were developed to attach EDTA.Fe to a single nucleotide on RNA as well as DNA
Jana Schwarzer et al.
Electrophoresis, 29(20), 4203-4214 (2008-10-18)
Glycoproteins, such as monoclonal antibodies as well as recombinant and viral proteins produced in mammalian cell culture play an important role in manufacturing of many biopharmaceuticals. To ensure consisting quality of the corresponding products, glycosylation profiles have to be tightly
Miniaturized parallel screens to identify chromatographic steps required for recombinant protein purification
Rege K and Heng M
Nature Protocols (2010)

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