①Heparinases
Heparinases can clave glycosidic bonds of heparin and/or heparan sulfate by a β-elimination mechanism, generating unsaturated products (mostly
disaccharides) with a double bond be-tween C4 and C5 of the uronate residue.
Features:
● Natural heparinase, from Flavobacterium heparinum.
● It has the highest specific activity compare with other products on the market.
● Pure enzyme, free of BSA or other protein impurities.
● Good stability, consistent batch reproducibility and degradation characteristics.
②TOSOH TSKgel SWXL Columns
Tosoh SWxl series columns feature high porous volume/unit volume ratio, low sample absorption, and high column efficiency. Could be used for MW
determinations of heparin and LMWHs.
③BioCore™ SEC columns
Asnail co-developed the BioCore SEC-HP columns, tailored for molecular weight (MW) and MW distribution. The column is durable and can provide
better volume exclusion separation.
④Dionex™ IonPac™ AS11 IC Columns
The Column specifically designed to resolve a large number of inorganic anions and organicacid anions from a single sample injection in one gradient run using hydroxide eluent systems.USP officially specifies the method for the identification of heparin sodium chromatography.
Heparinase I can degrade heparin and heparan sulfate, making it a powerful tool for heparin structural research, clinical diagnosis, and industrial quality control.
Heparinase I selectively cleaves the linkages between glucosamine and O-sulfated iduronic acid in heparin and heparan sulfate (relative activity approximately 3:1), with the main products being disaccharides. This enzyme can also cleave the pentasaccharide binding site of antithrombin III within heparin molecules.
Human Antithrombin is derived from human plasma, purified through affinity chromatography and gel filtration chromatography methods, and subjected to S/D virus inactivation steps.
Human Antithrombin is a serine protease inhibitor that forms a complex with heparin, leading to the inactivation of factor IIa (thrombin) and factor Xa. The biochemical potency of heparin can be determined based on the catalytic dissociation rate of residual coagulation factors on the corresponding chromogenic substrates.
Heparinase I, derived from Bacteroides fragilis, is widely utilized in heparinase I applications, including as a raw material for diagnostic reagents in thromboelastography heparin cups.
Factor XIIIa, a raw material for platelet cup diagnostic reagents used in thromboelastography.
The Asnail™ Heparin Anti-Factor 10 Assay is a two-step chromogenic substrate assay for the detection of heparin activity (including unfractionated heparin and low molecular weight heparin) in manual or automated experiments. This method is only suitable for the detection of heparin in human citric acid plasma or purified solution.
The kit is intended for scientific research only and is prohibited for clinical diagnosis and treatment.
Activated Factor X (FXa) is the product of calf plasma Factor X activation by Factor X activator of Luceri viper, purified by ion exchange and gel filtration chromatography, and added to the S/D virus inactivation step. FXa works with other blood factors in the body to activate prothrombin to produce thrombin, triggering a coagulation waterfall reaction.
S-2765 is a chemically synthesized activated Factor Xa (FXa)-specific substrate.
S-2238 is a chemically synthesized thrombin (Factor IIa, FXa)-specific substrate.
The AsnailTM Heparin Anti-Binary Assay is a two-step chromogenic substrate assay for the detection of heparin activity (including unfractionated heparin and low molecular weight heparin) by manual or automated experiments. This method is only suitable for the detection of heparin in human citric acid plasma or purified solution. The kit is intended for scientific research only and is prohibited for clinical diagnosis and treatment.
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