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PLAT Protein

Recombinant PLAT-Protein exprimiert in HEK-293 Cells.
Produktnummer ABIN7197374

Kurzübersicht für PLAT Protein (ABIN7197374)

Target

Alle PLAT Proteine anzeigen
PLAT (Plasminogen Activator, Tissue (PLAT))

Protein-Typ

Recombinant

Spezies

  • 15
  • 5
  • 2
  • 1
Human

Quelle

  • 10
  • 6
  • 2
  • 1
  • 1
  • 1
  • 1
HEK-293 Cells

Reinheit

> 95 % as determined by reducing SDS-PAGE.
  • Verwendungszweck

    Recombinant Human tPA/PLAT Protein

    Sequenz

    Ile 311-Pro 562

    Produktmerkmale

    The β chain (Ile 311-Pro 562) of mature human tPA (NP_000921.1) was obtained after cleavage of the N-terminal human IgG1 Fc region from the purified chimera.

    Endotoxin-Niveau

    < 1.0 EU per μg as determined by the LAL method.
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  • Beschränkungen

    Nur für Forschungszwecke einsetzbar
  • Format

    Lyophilized

    Rekonstitution

    Please refer to the printed manual for detailed information.

    Buffer

    Lyophilized from sterile 100 mM Glycine, 10 mM NaCl, 50 mM Tris, pH 7.5

    Lagerung

    4 °C,-20 °C,-80 °C

    Informationen zur Lagerung

    Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
  • Target

    PLAT (Plasminogen Activator, Tissue (PLAT))

    Andere Bezeichnung

    tPA/PLAT

    Hintergrund

    Background: Tissue plasminogen activator (abbreviated tPA or PLAT), is traditionally viewed as a simple serine protease whose main function is to convert plasminogen into biologically active plasmin. As a protease, tPA plays a crucial role in regulating blood fibrinolysis, in maintaining the homeostasis of extracellular matrix and in modulating the post-translational activation of growth factors. tPA is synthesized and secreted as a single chain polypeptide precursor which is cleaved in turn by plasmin. Proteolytic cleavage at the C-terminal side of Arg275 generates the enzyme composed of two subunits, designated as α and β chains which are held together by a single disulfide bond. Unlike the other members of the chymotrypsin family, tPA has one particular distinction in that the catalytic efficiency of the single-chain enzyme is only slightly lower than that of the proteolytically cleaved form and is therefore not a true zymogen. tPA is found not only in the blood, where its primary function is as a thrombolytic enzyme, but also in the central nervous system (CNS). It participats in a number of physiological and pathological events in the CNS, as well as the role of neuroserpin as the natural regulator of tPA's activity in these processes. Increased or decreased activity of tPA leads to hyperfibrinolysis or hypofibrinolysis, respectively. In addition, as a cytokine, tPA plays a pivotal role in the pathogenesis of renal interstitial fibrosis through diverse mechanisms. Thus, as a fibrogenic cytokine, it promotes the progression of kidney diseases.

    Synonym: T-PA; TPA; t-plasminogen activator; Tissue plasminogen activator;

    Molekulargewicht

    28 kDa

    NCBI Accession

    NP_000921

    Pathways

    Autophagie, Smooth Muscle Cell Migration, Platelet-derived growth Factor Receptor Signaling, SARS-CoV-2 Protein Interaktom
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