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Merck
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Key Documents

L6132

Sigma-Aldrich

L-Lysine–Agarose

lyophilized powder

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About This Item

MDL number:
MFCD00164292
UNSPSC Code:
12352202
NACRES:
NA.56

form

lyophilized powder

Quality Level

100

extent of labeling

~4 μmol per mL

technique(s)

affinity chromatography: suitable

matrix

Sepharose 4B

matrix activation

cyanogen bromide

matrix attachment

α-amino

matrix spacer

1 atom

suitability

suitable for chromatography

storage temp.

2-8°C

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Application

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.

Physical form

Lyophilized powder stabilized with lactose and dextran

Related product

Referencia del producto
Descripción
Precios

L5631

L-Lysine–Agarose, saline suspension

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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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
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
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
L Y Cheng et al.
Neurochemical research, 26(4), 425-438 (2001-08-10)
Phosphatases extracted from a human brain were resolved into two main groups, namely affi-gel blue-binding phosphatases and affi-gel blue-nonbinding phosphatases. Affi-gel blue binding phosphatases were further separated into four different phosphatase activities, designated P1-P4, and described previously. In the present
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