tPA Protein, Mouse, Recombinant (Fc Tag)

1/1
Price:
Size:
Number:

tPA Protein, Mouse, Recombinant (Fc Tag): Product Information

Purity
> 80 % as determined by SDS-PAGE
Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method
Activity
Testing in progress
Protein Construction
A DNA sequence encoding the mouse PLAT (P11214) (Ile309-Gln559) was was expressed with the fused Fc region of human IgG1 at the N-terminus.
Accession#
Expressed Host
HEK293 Cells
Species
Mouse
Predicted N Terminal
Glu
Molecule Mass
The recombinant mouse PLAT/Fc comprises 511 amino acids and has a predicted molecular mass of 56.4 kDa. The apparent molecular mass of the protein is approximately 57 kDa in SDS-PAGE under reducing conditions due to glycosylation.
Formulation
Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
Please refer to the specific buffer information in the hard copy of CoA.
Shipping
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Stability & Storage
Samples are stable for up to twelve months from date of receipt at -70℃
Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

tPA Protein, Mouse, Recombinant (Fc Tag): Images

tPA Protein, Mouse, Recombinant (Fc Tag): Alternative Names

AU020998 Protein, Mouse; AW212668 Protein, Mouse; D8Ertd2e Protein, Mouse; tPA Protein, Mouse

tPA Background Information

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.
Full Name
plasminogen activator, tissue
References
  • Yepes M, et al. (2004) New functions for an old enzyme: nonhemostatic roles for tissue-type plasminogen activator in the central nervous system. Exp Biol Med (Maywood). 229(11): 1097-104.
  • Samson AL, et al. (2006) Tissue-type plasminogen activator: a multifaceted modulator of neurotransmission and synaptic plasticity. Neuron. 50(5): 673-8.
  • Skrzypiec AE, et al. (2008) Tissue plasminogen activator in the amygdala: a new role for an old protease. J Physiol Pharmacol. 59 Suppl 8: 135-46.
  • Hu K, et al. (2008) Novel actions of tissue-type plasminogen activator in chronic kidney disease. Front Biosci. 13: 5174-86.
Add to Cart Successfully Add to Cart Failed Shopping cart is being updated, please wait