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Literature summary for 3.4.21.68 extracted from

  • Majidzadeh-A, K.; Khalaj, V.; Fatemeh, D.; Mahdi, H.; Farzaneh, B.; Ahmad, A.; Mahboudi, F.
    Cloning and expression of functional full-length human tissue plasminogen activator in Pichia pastoris (2010), Appl. Biochem. Biotechnol., 162, 2037-2048.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
the gene encoding full-length human t-PA is cloned into pPICZalphaA expression vector downstream of alcohol oxidase promoter and alpha-mating signal sequence from Saccharomyces cerevisiae and flush with the kex2 cleavage site to express the protein with a native N-terminus. Pichia pastoris strain GS115 is transformed with this cassette, and methanol utilizing (mut+) transformants are selected for production and secretion of functional human t-PA into culture media. Subcloning in Escherichia coli strain Top10 F' Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
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Source Tissue

Source Tissue Comment Organism Textmining

Subunits

Subunits Comment Organism
More t-PA is a serine-protease enzyme containing 527 amino acid residues in five structural domains. The correct folding of t-PA requires the correct pairing of 17 disulfide bridges in the molecule Homo sapiens

Synonyms

Synonyms Comment Organism
Tissue plasminogen activator
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Homo sapiens
tPA
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Homo sapiens

General Information

General Information Comment Organism
additional information t-PA is a serine-protease enzyme containing 527 amino acid residues in five structural domains Homo sapiens
physiological function tissue plasminogen activator, t-PA, plays a pivotal role in the treatment of acute myocardial infarction, ischemic stroke, and deep vein thrombosis Homo sapiens