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L6132

Sigma-Aldrich

L-Lysine–Agarose

lyophilized powder

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About This Item

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

form

lyophilized powder

Quality Level

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

Product No.
Description
Pricing

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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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
M B Furie et al.
Journal of cell science, 88 ( Pt 2), 161-175 (1987-09-01)
Monolayers of bovine microvascular endothelial cells (BMECs) grown on connective tissue derived from human amniotic membrane were used to examine the transendothelial migration of human neutrophils in vitro. Neutrophils placed above these cultures migrated in response to a chemotactic gradient

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