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Merck

L2140

Sigma-Aldrich

Lectin from Bandeiraea simplicifolia (Griffonia simplicifolia)

Isolectin B4 (BSI-B4), biotin conjugate, lyophilized powder

Synonim(y):

Bandeirea simplicifolia agglutinin, BS-I

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About This Item

Kod UNSPSC:
12352202
NACRES:
NA.32

pochodzenie biologiczne

Bandieraea simplicifolia

Poziom jakości

białko sprzężone

biotin conjugate

Formularz

lyophilized powder

siła działania

<50 μg per mL agglutination activity (using human blood group B erythrocytes)

skład

Protein, ~95% E1%/280

zakres etykietowania

3-6 mol biotin per mol protein

temp. przechowywania

−20°C

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Opis ogólny

Lectin from Bandeiraea simplicifolia (Griffonia simplicifolia) has A and B subunits, which recognizes αGalNAc and αGal-end groups respectively. Lectins are extracted from the seeds of the legume shrub Griffonia simplicifolia, which are carbohydrate binding proteins.

Zastosowanie

Lectin from Bandeiraea simplicifolia (Griffonia simplicifolia) has been used for immunohistochemistry and immunofluorescence staining.

Działania biochem./fizjol.

BS-I has a major affinity for terminal α-D-galactosyl residues with a secondary affinity for terminal N-acetyl-α-D-galactosaminyl residues.
Lectin from Bandeiraea simplicifolia (Griffonia simplicifolia) agglutinates human blood group A and B cells. It is specific for αGalNAc- and αGal. It acts as a reagent for the detection of this αGal epitope in biological materials. Lectin from Bandeiraea simplicifolia is used as a marker for xenoreactive antigen (αGal1−3Gal) and cancer. Lectin plays an important role in fertilization, embryogenesis, inflammation, metastasis and host-parasite recognition.

Inne uwagi

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.

Postać fizyczna

Contains citrate buffer salts and calcium chloride

Komentarz do analizy

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.
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Kod klasy składowania

11 - Combustible Solids

Klasa zagrożenia wodnego (WGK)

WGK 3

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable

Środki ochrony indywidualnej

Eyeshields, Gloves, type N95 (US)


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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

Sensory processing of deep tissue nociception in the rat spinal cord and thalamic ventrobasal complex
Sikandar S, et al.
Physiological Reports, 5(14), e13323-e13323 (2017)
Isolectins IA and IB of Griffonia (Bandeiraea) simplicifolia crystal structure of metal-free gs i-b4 and molecular basis for metal binding and monosaccharide specificity
Lescar J, et al.
The Journal of Biological Chemistry, 277(8), 6608-6614 (2002)
Quan Yuan et al.
Tissue engineering. Part A, 24(9-10), 719-728 (2017-10-06)
The aim of this study was to analyze the three-dimensional distribution of hypoxia in the arteriovenous (AV) loop model in rats, by examining the distribution of hypoxia-inducible factor-1 alpha (HIF-1α). AV loops were created from the femoral artery and vein
Ludovic Wrobel et al.
Neuroscience letters, 495(1), 49-54 (2011-03-23)
Oxytocin can influence various spinal functions. However, little is known about the spinal neuronal networks responsible for oxytocin effects. The aim of this study was to localize and characterize spinal neurons expressing oxytocin receptors. We used an oxytocin receptor-reporter mouse
The Lectins: Properties, Functions, and Applications in Biology and Medicine (2012)

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