Sign In to View Organizational & Contract Pricing.
Select a Size
Change View
About This Item
NACRES:
NA.32
UNSPSC Code:
12352200
conjugate
biotin conjugate
form
lyophilized powder
potency
<250 μg per mL agglutination activity (using human blood group A erythrocytes.)
composition
Protein, ~85% E1%/280
extent of labeling
~5 mol biotin per mol protein
storage temp.
2-8°C
Application
Lectin from Bandeiraea simplicifolia (Griffonia simplicifolia) has been used:
- for highlighting murine endothelial cells
- to identify fetal capillaries in endothelial immunohistochemical staining, conjugated with biotin
- to detect tumor total vessels
Biochem/physiol Actions
BS-I has a major affinity for terminal α-D-galactosyl residues with a secondary affinity for terminal N-acetyl-α-D-galactosaminyl residues.
Physical form
Contains sodium citrate
Analysis Note
Agglutination activity is expressed in μg/mL and is determined from serial dilutions of a 1 mg/mL solution using phosphate buffered saline, pH 6.8, containing, for each lectin, calcium, magnesium, and manganese at different concentrations. This activity is the lowest concentration to agglutinate a 2% suspension of appropriate erythrocytes after 1 hr incubation at 25 °C.
Other Notes
BS-I is a tetrameric lectin consisting of two types of subunits designated A and B. There are five BS-I isolectins with different subunit composition: BSI-B4, BSI-AB3, BSI-A2B2, BSI-A3B and BSI-A4. BSI-B4 is blood group B specific and has an exclusive affinity for terminal α-D-galactosyl residues, whereas BSI-A4 has blood group A specificity and has a major affinity for terminal N-acetyl-α-D-galactosaminyl residues.
Still not finding the right product?
Explore all of our products under Lectin from Bandeiraea simplicifolia (Griffonia simplicifolia)
Storage Class
13 - Non Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.