추천 제품
일반 설명
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.
애플리케이션
Lectin from Helix pomatia has been used to study its binding activities in Gyrodactylus derjavini parasitizing fins of Oncorhynchus mykiss.
생화학적/생리학적 작용
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.
분석 메모
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
개인 보호 장비
Eyeshields, Gloves, type N95 (US)
Overview of fish immunity
Mucosal Health in Aquaculture, 3-54 (2015)
Histochemical characteristics of Gyrodactylus derjavini parasitizing the fins of rainbow trout (Oncorhynchus mykiss)
Buchmann K, et al.
Folia Parasitol (Praha), 45(4), 312-318 (1998)
PEAS AND LENTILS
Encyclopedia of food sciences and nutrition, 4433-4440 (2003)
Cédric Jäger et al.
BMC nephrology, 23(1), 178-178 (2022-05-11)
Recurrence of IgA nephropathy (IgAN) after kidney transplantation occurs in about 30% of patients. The relevance of recurrence for the long-term graft survival is expected to increase, since graft survival continues to improve. In a nested study within the Swiss
Yoko Nabeshima et al.
Scientific reports, 10(1), 19122-19122 (2020-11-07)
Human group-specific component protein (Gc protein) is a multifunctional serum protein which has three common allelic variants, Gc1F, Gc1S and Gc2 in humans. Gc1 contains an O-linked trisaccharide [sialic acid-galactose-N-acetylgalactosamine (GalNAc)] on the threonine420 (Thr420) residue and can be converted
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