ECHICETIN from Echis carinatus sochureki
Main features: Snaclec Echicetin
Echicetin is a C-type lectin purified from Echis carinatus sochureki snake venom, the Indian Saw-scaled Viper.
Primary structure: A dimer of 2 subunits: subunit α with 133 AA (16 kDa) and subunit β with 123 AA (14 kDa). ECHICETIN from Echis carinatus sochureki
Alpha subunit: DQDCLSGWSF YEGHCYQLFR LKTWDEAEKY CNQWDGGHLV SIESNAKAEF VAQLISRKLP KSAIEDRVWI GLRDRSKREQ CGHLWTDNSF VHYEHVVPPT KCFVLERQTE FRKWIAVNCE FKFPFVCKAK IPR – 4 Disulfide bonds: 4 – 15; 31 – 127; 81 – Interchain (with C-75 in subunit beta); 102 – 119.
Beta subunit: NCLPDWSVYE GYCYKVFKER MNWADAEKFC MKQVKDGHLV SFRNSKEVDF MISLAFPMLK MELVWIGLSD YWRDCYWEWS DGAQLDYKAW DNERHCFAAK TTDNQWMRRK CSGEFYFVCK CPA – 4 Disulfide bonds: 2 – 13; 30 – 119; 75 – Interchain (with C-81 in subunit alpha); 96 – 111.
Molecular weight: 30 kDa
Purity: ≥ 99%
Biological activity: ECHICETIN from Echis carinatus sochureki
Snaclec Echicetin is a C-type lectin that binds to platelet glycoprotein Iba and blocks von Willebrand factor (vWF) and Thrombin binding.
Echicetin inhibits aggregation of washed platelets induced by vWF, thrombin, or alboaggregin-A. However, when complexed with the pentameric plasma immunoglobulin Mkappa (IgMκ), echicetin binds specifically to GPIb and activates platelets. This is caused by P-selectin expression and activation of alpha-/Ib/beta-3 as well as tyrosine phosphorylation of several signal transduction molecules, including p53/56(LYN), p64, p72(SYK), p70 to p90, and p120. In vivo, it induces thrombocytopenia when injected into mice, probably accounting for activation of platelets rather than inhibition.
Uses: Echicetin can be used either to block GPlba functions or, if labeled with 125I or biotin or FITC, to measure GPlba expression levels. In the presence of plasma, echicetin agglutinates platelets via GPlba and LGM and can be used to assess GPlba expression levels directly, independently of vWF levels or function.
Packaging: Lyophilised powder in 50 µg glass vial.