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product name
Alpha 2 Antiplasmin from human plasma, ≥95% (SDS-PAGE)
由来生物
human
アッセイ
≥95% (SDS-PAGE)
形状
lyophilized
有効性
≥5.0 I.U. per mg
分子量
70 kDa
包装
pkg of 100 μg
UniProtアクセッション番号
輸送温度
wet ice
保管温度
−20°C
遺伝子情報
human ... SERPINF2(5345)
詳細
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.
生物化学的/生理学的作用
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.
物理的形状
Lyophilized from 20 mM Bis-Tris, pH 6.4, with 200 mM NaCl.
再構成
In water or aqueous buffer
免責事項
RESEARCH USE ONLY. This product is regulated in France when intended to be used for scientific purposes, including for import and export activities (Article L 1211-1 paragraph 2 of the Public Health Code). The purchaser (i.e. enduser) is required to obtain an import authorization from the France Ministry of Research referred in the Article L1245-5-1 II. of Public Health Code. By ordering this product, you are confirming that you have obtained the proper import authorization.
シグナルワード
Warning
危険有害性情報
危険有害性の分類
Eye Irrit. 2
保管分類コード
11 - Combustible Solids
WGK
WGK 3
適用法令
試験研究用途を考慮した関連法令を主に挙げております。化学物質以外については、一部の情報のみ提供しています。 製品を安全かつ合法的に使用することは、使用者の義務です。最新情報により修正される場合があります。WEBの反映には時間を要することがあるため、適宜SDSをご参照ください。
Jan Code
SRP6313-100UG:
試験成績書(COA)
製品のロット番号・バッチ番号を入力して、試験成績書(COA) を検索できます。ロット番号・バッチ番号は、製品ラベルに「Lot」または「Batch」に続いて記載されています。
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Noncovalent interaction of ?2-antiplasmin with fibrin (ogen): localization of ?2-antiplasmin-binding sites.
Biochemistry, 49(35), 7643-7651 (2010)
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
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)
The kidney is a major site of alpha(2)-antiplasmin production.
The Journal of Clinical Investigation, 97(11), 2478-2484 (1996)
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