Maackia amurensis (MAA) (AP)

Referência M1062-50B-1mg

Tamanho : 1mg

Marca : US Biological

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M1062-50B Maackia amurensis (MAA) (AP)

Clone Type
Polyclonal
Grade
Purified
Shipping Temp
Blue Ice
Storage Temp
4°C Do Not Freeze

Pure Maackia amurensis lectin (MAA), Alkaline Phosphatase conjugated.||Lectins are derived from the extracts of plants, animals, viruses and microorganisms and are known to agglutinate red blood cells. These agglutinins can select cell types according to blood group activities utilizing sugar-binding mechanisms. ||Lectins form precipitates with glycoconjugates and are useful for identifying or separating oligosaccharides with identical sugar compositions such as galactose, mannose or glucose.||Carbohydrate Specificity:|Sialic acid alpha(2,3) Galactose.||Inhibitory Carbohydrate: |Not inhibited by simple sugars at < 50mM. Lactose and Sialic acid will exhibit some inhibitory potency at concentrations greater than 75mM. Sialyllactose alpha (2, 6) is the most potent inhibitor of leukoagglutination.||Activity: |Less than 0.5ug/ml will agglutinate type O human erythrocytes.||Storage and Stability: |Store product at 4°C. DO NOT FREEZE! Stable at 4°C for 6 months after receipt as an undiluted liquid. Dilute required amount only prior to immediate use. Further dilutions can be made in assay buffer. For maximum recovery of product, centrifuge the original vial prior to removing the cap.

Applications
Purity: Purified|Concentration: As reported|Form: Supplied as a liquid in 0.01M PBS, 0.15M sodium chloride, pH 7.2-7.4, 20-50% glycerol, 0.05% sodium azide. Labeled with Alkaline Phosphatase (AP).||Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.
Form
Supplied as a liquid in 0.01M PBS, 0.15M sodium chloride, pH 7.2-7.4, 20-50% glycerol, 0.05% sodium azide. Labeled with Alkaline Phosphatase (AP).
Purity
Purified
References
1. Kawaguchi, T., et al. (1974) J. Biol. Chem.254 : 2786-2792, 2. Wang, W. -C. and Cummings, R. D. (1988) J. Biol. Chem. 263 :4576-4585.