Fagus Antibody Services

Recombinant Human tPA/PLAT Protein

£489.60£612.00 excluding VAT

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.

Size

20µg

Active Protein
Activity
Protein Construction

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.

Sequence

Ile 311-Pro 562

Fusion Tag
Accession

NP_000921.1

Species

Human

Expressed Host

HEK293 Cells

Shipping

This product is provided as lyophilized powder which is shipped with ice packs.

Purity

> 95 % as determined by reducing SDS-PAGE.

Endotoxin

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

Stability and Storage

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

Mol Mass

28 kDa

AP Mol Mass

38 kDa

Formulation

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

Research Areas

Cell biology, Cardiovascular, Cancer, metabolism

Reconstitution

Please refer to the printed manual for detailed information.

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