L6512
Lectin from Helix pomatia
biotin conjugate, lyophilized powder
Synonym(s):
Helix pomatia agglutinin, HPA
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About This Item
Recommended Products
conjugate
biotin conjugate
form
lyophilized powder
extent of labeling
2-4 mol biotin per mol protein
impurities
salt, free
storage temp.
−20°C
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General description
Lectins are carbohydrate-binding proteins, omnipresent, found in fungi, plants and animals. These oligomeric proteins are characterized by the presence of a carbohydrate recognition domain.
Application
Lectin from Helix pomatia has been used to study its binding activities in Gyrodactylus derjavini parasitizing fins of Oncorhynchus mykiss.
Biochem/physiol Actions
Lectin is useful in glycoconjugate characterizing, imaging and targeting. Lectin participates in host recognition and tissue adhesion. Lectins shows resistance to proteolytic degradation in vivo.
HPA has anti-A human blood group specificity and has an affinity for terminal N-acetyl-α-D-galactosaminyl residues. Conjugates are prepared from affinity purified lectin.
Analysis Note
Where reported, agglutination activity is expressed in μg/ml and is determined from serial dilutions in phosphate buffered saline, pH 6.8, of a 1 mg/ml solution. This activity is the lowest concentration to agglutinate a 2% suspension of human blood group A erythrocytes after 1 hour incubation at 25 °C.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Histochemical characteristics of Gyrodactylus derjavini parasitizing the fins of rainbow trout (Oncorhynchus mykiss)
Folia Parasitol (Praha), 45(4), 312-318 (1998)
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Mucosal Health in Aquaculture, 3-54 (2015)
PEAS AND LENTILS
Encyclopedia of food sciences and nutrition, 4433-4440 (2003)
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Diseases of aquatic organisms, 32(3), 195-200 (1998-07-24)
A lethal effect of rainbow trout Oncorhynchus mykiss plasma containing intact complement factors on Gyrodactylus derjavini was demonstrated. It was associated with binding of complement factor C3 to certain carbohydrate-rich parasite structures. Parasites were exposed in vitro to plasma from
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