Galanthus nivalis (Snowdrop bulb) (GNA) (HRP)

Referencia G1044-25-500ug

embalaje : 500ug

Marca : US Biological

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G1044-25 Galanthus nivalis (Snowdrop bulb) (GNA) (HRP)

Clone Type
Polyclonal
Grade
Purified
Shipping Temp
Blue Ice
Storage Temp
-20°C

Galanthus nivalis agglutinin (GNA) is a small molecular weight tetramer consisting of subunits of about 13,000D. This lectin contains little or no carbohydrate. Unlike most mannose-specific lectins, it is not a metalloprotein and does not require Ca++ or Mn++ for binding. Binding seems to be preferentially directed toward structures containing (a-1,3) mannose residues. In contrast to most mannose-binding lectins, GNA will not bind alpha linked glucose. Reports indicate that this lectin binds IgM, but not bind IgG immunoglobulin classes of rat and mouse. The only protein from human serum reported to bind to this lectin is a2-macroglobulin.||Activity (unconjugated): |≤15ug/ml will agglutinate human type O erythrocytes.||Carbohydrate Specificity: |Mannose||Inhibitory Carbohydrate:|Mannose alpha(1,3) >Mannose||Storage and Stability: |May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 6 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Labeled with horseradish peroxidase (HRP). Sodium azide is a potent inhibitor of peroxidase and should not be added to HRP conjugates. HRP conjugates are sensitive to light.

Applications
Source: Galanthus nivalis (snowdrop bulb)|Purity: Purified|Concentration: ~1mg/ml|Form: Supplied as a liquid in PBS, pH 7.3. Labeled with Horseradish peroxidase (HRP).||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 PBS, pH 7.3. Labeled with Horseradish peroxidase (HRP).
Purity
Purified
References
1. Chapman, A., Kornfeld, R., J. Biol. Chem. 254: 816-82 (1979). 2. Van Damme, E.J.M., et al., FEBS Lett. 215: 140-144 (1987). 3. Shibuya, N., et al., Arch. Biochem. Biophys. 267: 676-680 (1988).