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SRP6313

Sigma-Aldrich

Alpha 2 Antiplasmin from human plasma

≥95% (SDS-PAGE)

Synonym(s):

AAP, Alpha-2-plasmin inhibitor, PLI, SERPINF2

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About This Item

UNSPSC Code:
12352202
NACRES:
NA.32

biological source

human

Assay

≥95% (SDS-PAGE)

form

lyophilized

potency

≥5.0 I.U. per mg

mol wt

70 kDa

packaging

pkg of 100 μg

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... SERPINF2(5345)

General description

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.

Biochem/physiol Actions

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.

Physical form

Lyophilized from 20 mM Bis-Tris, pH 6.4, with 200 mM NaCl.

Reconstitution

In water or aqueous buffer

Disclaimer

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.

Pictograms

Exclamation mark

Signal Word

Warning

Hazard Statements

Hazard Classifications

Eye Irrit. 2

WGK

WGK 3

Regulatory Information

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Certificates of Analysis (COA)

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Noncovalent interaction of ?2-antiplasmin with fibrin (ogen): localization of ?2-antiplasmin-binding sites.
Tsurupa G, et al.
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.
Hu N
BMC Genomics, 7, 299-299 (2006)
Ekaterina Mindel et al.
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.
Shahian DM and Levine JD
Chest, 97(6), 1488-1490 (1990)
The kidney is a major site of alpha(2)-antiplasmin production.
Menoud PA
The Journal of Clinical Investigation, 97(11), 2478-2484 (1996)

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