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Merck

L6132

Sigma-Aldrich

L-Lysin-Agarose

lyophilized powder

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About This Item

MDL-Nummer:
UNSPSC-Code:
12352202
NACRES:
NA.56

Form

lyophilized powder

Kennzeichnungsgrad

~4 μmol per mL

Methode(n)

affinity chromatography: suitable

Matrix

Sepharose 4B

Matrixaktivierung

cyanogen bromide

Matrixanbindung

α-amino

Matrix-Spacer

1 atom

Eignung

suitable for chromatography

Lagertemp.

2-8°C

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Anwendung

L-lysine-agarose is used in protein chromatography, affinity chromatography and amino acid resins. L-lysine-agarose has been used to study mitogen-activated protein kinase (MAPK) cascades in abscisic acid (ABA) signal transduction pathways as well as to study the regulation of phosphorylation of tau protein in the brain.

Physikalische Form

Lyophilisiertes Pulver stabilisiert mit Lactose und Dextran

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Produkt-Nr.
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Preisangaben

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)


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V J Christiansen et al.
Arteriosclerosis, thrombosis, and vascular biology, 17(1), 164-171 (1997-01-01)
Deposition of the terminal complement proteins (C5b-9) on human endothelial cells can result in cell lysis or nonlytic alterations of cell function including procoagulant responses. Because regulation of fibrinolysis is a central endothelial function and because C9 contains a carboxyl-terminal
P Saxena et al.
Investigative ophthalmology & visual science, 41(6), 1473-1481 (2000-05-08)
With age, human lens crystallins become more pigmented, oxidized, modified by ascorbate oxidation and advanced glycation end products (AGEs), and bind copper. The hypothesis was tested that the major AGE and ascorbylation product in the human lens, N(epsilon)-carboxymethyl-L-lysine (CML), has
J Tao et al.
Proceedings of the National Academy of Sciences of the United States of America, 89(7), 2723-2726 (1992-04-01)
A single arginine residue within the basic region of the human immunodeficiency virus Tat protein mediates specific binding of Tat peptides to a three-nucleotide bulge in TAR RNA. It has been proposed that arginine recognizes TAR by forming a network
J Tao et al.
Biochemistry, 35(7), 2229-2238 (1996-02-20)
Specific binding of the human immunodeficiency virus Tat protein to its RNA site (TAR) is mediated largely by a single arginine residue located within a basic region of the protein. Many essential features of the interaction can be mimicked by
Sau-Ching Wu et al.
The Journal of biological chemistry, 278(20), 18199-18206 (2003-03-21)
To develop a fast-acting clot dissolving agent, a clot-targeting domain derived from the Kringle-1 domain in human plasminogen was fused to the C-terminal end of staphylokinase with a linker sequence in between. Production of this fusion protein in Bacillus subtilis

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