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L7634

Sigma-Aldrich

α-Lactose-Agarose

saline suspension

Sinónimos:

alpha-lactose resin

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About This Item

MDL number:
UNSPSC Code:
41106500
NACRES:
NA.56
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biological source

bovine milk

Quality Level

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

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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B Beaumelle et al.
The Journal of biological chemistry, 268(31), 23661-23669 (1993-11-05)
Ricin translocation was demonstrated (using both fluorescence- and radiolabel-based assays) across the membrane of endosomes purified from mouse lymphocytes. Selectivity of the process was shown by the absence of translocation activity of transferrin and horseradish peroxidase used as membrane-bound and
C V Hughes et al.
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
Jing Wang et al.
Veterinary parasitology, 148(3-4), 247-255 (2007-07-24)
The effects of the second glutamic acid (E) in the C-terminal CRDs on the hemagglutination and lactose-binding characteristics of the recombinant galectins of nematode Haemonchus contortus were observed using two isoforms of recombinant galectins as models, and the sugar-binding abilities
E V Lourenço et al.
Glycobiology, 11(7), 541-547 (2001-07-12)
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.
Nadine Keller et al.
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

Questions

  1. Can this resin be cleaned and re-used?

    1 answer
    1. This product is assayed for the ability to bind lectin from Arachis hypogaea. The lectin is loaded in a 0.5 M sodium chloride, 0.01 M sodium phosphate buffer, pH 6.8. The column is washed with the same buffer. The lectin is eluted in the same buffer containing 0.1 M alpha-lactose.

      The resin can be regenerated by washing with 3-5 column volumes of 50 mM acetic acid, pH 3.0 containing 0.5 M sodium chloride, followed by 50 mM borate buffer at pH 7.0. The resin can also be washed with 6 M guanidine hydrochloride solution, adjust to pH 3 with acetic acid. The ligand on the resin is susceptible to hydrolysis at pH above 10.

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