Recombinant Mouse tPA/PLAT Protein (Fc Tag)

Recombinant Mouse tPA/PLAT Protein (Fc Tag)

SKU #	PKSM040444
Expression Host	HEK293 Cells

Description

Synonyms	AU020998,AW212668,D8Ertd2e,tPA
Species	Mouse
Expression Host	HEK293 Cells
Sequence	Ile309-Gln559
Accession	P11214
Calculated Molecular Weight	56.4 kDa
Observed Molecular Weight	57 kDa
Tag	N-hFc
Bio-activity	Not validated for activity

Properties

Purity	> 80 % as determined by reducing SDS-PAGE.
Endotoxin	< 1.0 EU per g of the protein as determined by the LAL method.
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.
Shipping	This product is provided as lyophilized powder which is shipped with ice packs.
Formulation	Lyophilized from sterile PBS, pH 7.4 Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual.
Reconstitution	Please refer to the printed manual for detailed information.

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 and 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.