Griffonia Simplicifolia Lectin I (GSL I) Isolectin B4 Protein

Name: Griffonia Simplicifolia Lectin I (GSL I) Isolectin B4 Protein
Brand: Novus Biologicals
SKU: B-1205-NB
Price: 299 USD
Availability: InStock

Novus Biologicals | Catalog # B-1205-NB

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Product Specifications
Scientific Data
Preparation & Storage
Background
Product Documents
Specific Notices

Key Product Details

Conjugate

Biotin

Applications

Immunohistochemistry, Western Blot, ELISA, Immunocytochemistry/ Immunofluorescence, Bioactivity, Dot Blot

View all Griffonia Simplicifolia Lectin I (GSL I) Isolectin B4 Proteins and Enzymes »

Product Specifications

Description

A biologically active protein corresponding to Griffonia Simplicifolia Lectin I (GSL I) Isolectin B4.

Source: Griffonia (Bandeiraea) simplicifolia seeds

GSL I-B4 isolectin contains only the B subunits. It is a useful marker for endothelial cells from nonprimates such as mouse, rat, rabbit, and goat as well as a marker for non-peptidergic unmyelinated primary afferent neurons. This “B”-rich lectin preferentially agglutinates blood group B cells and is specific for a-galactose residues.

Biotinylated GSL I-B4 has an appropriate number of biotins bound to provide the optimum staining characteristics for this lectin. This conjugate is supplied essentially free of unconjugated biotins and is preserved with sodium azide.
Specific for galactose.

Purity

Affinity purified

Predicted Molecular Mass

114 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Activity

This "B"-rich lectin preferentially agglutinates blood group B cells and is specific for alpha-galactose residues.

Application Notes

For most applications, a freshly prepared working solution of 5 - 20 ug/mL in the buffer mentioned below is recommended..

Protein / Peptide Type

Protein

Scientific Data Images for Griffonia Simplicifolia Lectin I (GSL I) Isolectin B4 Protein

Griffonia Simplicifolia Lectin I (GSL I) Isolectin B4 Native Protein [B-1205-NB] - Griffonia Simplicifolia Lectin I (GSL I) Isolectin B4, Biotinylated

Formulation, Preparation, and Storage

B-1205-NB

Formulation	10 mM HEPES (pH 7.5), 0.15 M NaCl, 0.1 mM CaCl2
Preservative	0.08% Sodium Azide
Concentration	Please see the vial label for concentration. If unlisted please contact technical services.
Shipping	The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage	Store at 4C in the dark.

Background: Griffonia Simplicifolia Lectin I (GSL I) Isolectin B4

GSL I is a family of glycoproteins with molecular weights of approximately 114 kDa. There are two types of subunits, termed A and B, with slightly different molecular weights. These subunits combine to form tetrameric structures, resulting in five isolectins. The A -rich lectin preferentially agglutinates blood group A erythrocytes and thus appears to be specific for alpha-N-acetylgalactosamine residues, while the B -rich lectin preferentially agglutinates blood group B cells and is specific for alpha-galactose residues. Our GSL I is a mixture of the five isolectins. GSL I has been reported to bind several glycoproteins including laminin.

This biotinylated lectin is an ideal intermediate for examining glycoconjugates using the Biotin-Avidin/Streptavidin System. First the biotinylated lectin is added, followed by the VECTASTAIN ABC Reagent, Avidin D conjugate, or streptavidin derivative.

Inhibiting Sugar: 500 mM galactose or 100 mM raffinose

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Product Specific Notices for Griffonia Simplicifolia Lectin I (GSL I) Isolectin B4 Protein

This product is manufactured by Vector Laboratories and distributed by Novus Biologicals.

This product is for research use only and is not approved for use in humans or in clinical diagnosis. This product is guaranteed for 1 year from date of receipt.

Citations for Griffonia Simplicifolia Lectin I (GSL I) Isolectin B4 Protein

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