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PLAT Protein

Recombinant PLAT protein expressed in HEK-293 Cells.
Catalog No. ABIN7197374

Quick Overview for PLAT Protein (ABIN7197374)

Target

See all PLAT Proteins
PLAT (Plasminogen Activator, Tissue (PLAT))

Protein Type

Recombinant

Origin

  • 16
  • 6
  • 2
  • 1
Human

Source

  • 9
  • 8
  • 3
  • 1
  • 1
  • 1
  • 1
HEK-293 Cells

Purity

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

    Recombinant Human tPA/PLAT Protein

    Sequence

    Ile 311-Pro 562

    Characteristics

    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 Level

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

    For Research Use only
  • Format

    Lyophilized

    Reconstitution

    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

    Storage

    4 °C,-20 °C,-80 °C

    Storage Comment

    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))

    Alternative Name

    tPA/PLAT

    Background

    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;

    Molecular Weight

    28 kDa

    NCBI Accession

    NP_000921

    Pathways

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