SRP6313
Alpha 2 Antiplasmin from human plasma
≥95% (SDS-PAGE)
Synonyme(s) :
AAP, Alpha-2-plasmin inhibitor, PLI, SERPINF2
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About This Item
Produits recommandés
Source biologique
human
Pureté
≥95% (SDS-PAGE)
Forme
lyophilized
Puissance
≥5.0 I.U. per mg
Poids mol.
70 kDa
Conditionnement
pkg of 100 μg
Numéro d'accès UniProt
Conditions d'expédition
wet ice
Température de stockage
−20°C
Informations sur le gène
human ... SERPINF2(5345)
Description générale
α-2 antiplasmin (AAP) is a member of the Serpin superfamily. Liver and kidney are major sites of its production and other tissues such as muscle, intestine, central nervous system, and placenta also express its mRNA at a moderate level. The tissue expression pattern indicates that it is a key regulator of plasmin mediated proteolysis in these tissues. The gene encoding this protein is localized on human chromosome 17.
α-2 antiplasmin (AAP) is a member of the Serpin superfamily. Liver and kidney are major sites of its production and other tissues such as muscle, intestine, central nervous system, and placenta also express its mRNA at a moderate level. The tissue expression pattern indicates that it is a key regulator of plasmin mediated proteolysis in these tissues. The AAP gene is mapped to human chromosome 17p13 and codes for a glycoprotein of single chain containing 464 amino acid residues.
Actions biochimiques/physiologiques
α-2 antiplasmin (AAP) is the primary physiological inhibitor of the serine protease plasmin, which is responsible for the dissolution of fibrin clots. In addition to plasmin, it is also an efficient inhibitor of trypsin and chymotrypsin. α-antiplasmin-deficiency is a rare coagulation disorder which allows unrestrained fibrinolytic activity. Individuals with this condition may receive therapeutic A2AP prior to surgery to prevent postoperative hemorrhaging.
α-2 antiplasmin (AAP) is the primary physiological inhibitor of the serine protease plasmin, which is responsible for the dissolution of fibrin clots. It inhibits the action of protease by the formation In addition to plasmin, it is also an efficient inhibitor of trypsin and chymotrypsin. α-antiplasmin-deficiency is a rare coagulation disorder which allows unrestrained fibrinolytic activity. AAP is known to inhibit fibrinogenolysis by preventing free plasmin circulation.
Forme physique
Lyophilized from 20 mM Bis-Tris, pH 6.4, with 200 mM NaCl.
Reconstitution
In water or aqueous buffer
Clause de non-responsabilité
Ce produit, destiné à la recherche scientifique, est soumis à une réglementation spécifique en France, y compris pour les activités d′importation et d′exportation (Article L 1211-1 alinéa 2 du Code de la Santé Publique). L′acheteur (c′est-à-dire l′utilisateur FINAL) est tenu d′obtenir une autorisation d′importation auprès du ministère français de la recherche, mentionné à l′article L1245-5-1 II du Code de la Santé Publique. En commandant ce produit, vous confirmez détenir l′autorisation d′importation requise.
Mention d'avertissement
Warning
Mentions de danger
Conseils de prudence
Classification des risques
Eye Irrit. 2
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
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Les clients ont également consulté
Noncovalent interaction of ?2-antiplasmin with fibrin (ogen): localization of ?2-antiplasmin-binding sites.
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Genome-wide loss of heterozygosity and copy number alteration in esophageal squamous cell carcinoma using the Affymetrix GeneChip Mapping 10 K array.
BMC Genomics, 7, 299-299 (2006)
Journal of neuroscience research, 99(3), 966-976 (2020-12-10)
Many coagulation factor proteases are increased in the brain during ischemic stroke. One of these proteases is plasmin. In this study we established a novel method for direct quantitative measurement of plasmin activity in male mouse brain slices using a
The kidney is a major site of alpha(2)-antiplasmin production.
The Journal of Clinical Investigation, 97(11), 2478-2484 (1996)
Open-heart surgery in a patient with heterozygous alpha 2-antiplasmin deficiency. Perioperative strategies in the first reported case.
Chest, 97(6), 1488-1490 (1990)
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