Glycine max lectin (SBA) (50 mg)
For Research Use Only
Glycine max lectin is isolated from soy bean (Soy bean agglutinin, SBA) by affinity chromatography. The protein has 4 subunits and a molecular weight of 120 kDa. SBA is not blood group specific. It displays carbohydrate binding specifity for N-acetyl-D-galactosamine and galactopyranosyl residues of glycoproteins.
The lectin interacts better with neuramidase-treated cells than with untreated cells. It possesses selective affinity for lymphocytes and human CD34+ hematopoietic stem cells. Immobilized conjugates of SBA are therefore important tools for removing T-cells in bone marrow transplantation.
Glycine max lectin is supplied without preservatives as a white to cream-coloured lyophilized powder from 50 mM NH4HCO3, 10 µM CaCl2.For laboratory use only.
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Binding specificity for N-acetyl-D-galactosamine.
Specificity for blood group: A1 > A2 >> B.
|Appearance: White to cream colored lyophilized powder. |
Source: Soy bean.
Molecular weight: 120 kDa.
Sugar specificity: D-GalNAc.
Activity: Less than 4 µg/ml will agglutinate fresh A1 cells. Older B cells can be stronger than A2 cells. Blood group specificity: A1 > A2 >> B.
Microorganisms: < 100 CFU/g.
Protein content: > 80%, OD280nm (ε 1.28 = 1 mg/ml).
Identity: SDS-PAGE, one band corresponding to the four identical subunits.
Shelf life: Three years when stored at -20°C.
|Studies of SBA-binding normal and tumour cells. |
Blood group agglutination.
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|Glycine Max||Glycine Max||N/A||N/A|