L7634
α-Lactose-Agarose
saline suspension
Synonym(s):
alpha-lactose resin
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About This Item
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biological source
bovine milk
form
saline suspension
technique(s)
affinity chromatography: suitable
matrix
6% beaded agarose
matrix activation
divinyl sulfone
matrix attachment
hydroxyl
matrix spacer
5 atoms
capacity
6-25 mg/mL binding capacity (lectin from Arachis hypogaea)
suitability
suitable for chromatography
storage temp.
2-8°C
Application
α-Lactose-agarose has been used:
- in protein chromatography to purify galectins from lysed bacteria cells
- to capture ricin based on lectin-carbohydrate affinity
- to study microneme proteins and host-parasite cell surface receptors
α-lLactose-agarose is used in protein chromatography, affinity chromatography and carbohydrate matrices. α--Lactose-agarose has been used to study microneme proteins and host-parasite cell surface receptors.
Physical form
Suspension in 0.15 M NaCl, 0.01 M sodium phosphate, pH 6.8, containing 0.02% sodium azide
Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Proceedings of the National Academy of Sciences of the United States of America, 101(21), 7982-7987 (2004-05-19)
Secretions of the uterus support survival and growth of the conceptus (embryo/fetus and associated membranes) during pregnancy. Galectin-15, also known as OVGAL11 and a previously uncharacterized member of the galectin family of secreted beta-galactoside lectins containing a conserved carbohydrate recognition
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Host cell invasion by Toxoplasma gondii is a multistep process with one of the first steps being the apical release of micronemal proteins that interact with host receptors. We demonstrate here that micronemal protein 1 (MIC1) is a lactose-binding lectin.
Infection and immunity, 72(8), 4791-4800 (2004-07-24)
Microneme proteins have been shown to play an important role in the early phase of host cell adhesion, by mediating the contact between the parasite and host cell surface receptors. In this study we have identified and characterized a lectin-like
Infection and immunity, 60(3), 1178-1186 (1992-03-01)
The gram-negative human oral bacterium Veillonella atypica PK1910 exhibits both lactose-inhibitable and lactose-noninhibitable coaggregations with certain human oral streptococci. A mild sonication procedure was used to obtain a veillonella surface protein preparation against which antisera were prepared. To characterize the
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