The secreted recombinant human SERPINI1 consists of 405 amino acids after removal of the signal peptide and has a calculated molecular mass of 46 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rh SERPINI1 is approximately 50-55 kDa due to glycosylation.
Lyophilized from sterile PBS, pH 7.4 Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the hard copy of CoA.
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 -20℃ to -80℃ 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.
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
neuroserpin Protein, Human; PI12 Protein, Human; Serpin I1 Protein, Human
Neuroserpin Background Information
Neuroserpin, also known as Protease inhibitor 12 and SERPINI1, is a secreted protein which belongs to the serpin family. Neuroserpin is a serine protease inhibitor that inhibits plasminogen activators and plasmin but not thrombin. Serine protease inhibitors of the serpin superfamily are involved in many cellular processes. Neuroserpin was first identified as a protein secreted from the axons of dorsal root ganglion neurons. Neuroserpin is predominantly expressed in the brain, and is expressed in the late stages of neurogenesis during the process of synapse formation. Overexpression of neuroserpin in an anterior pituitary corticotroph cell line results in the extension of neurite-like processes, suggesting that neuroserpin may play a role in cell communication, cell adhesion, and/or cell migration. Neuroserpin may be involved in the formation or reorganization of synaptic connections, as well as synaptic plasticity in the adult nervous system. Neuroserpin may also protect neurons from cell damage by tissue-type plasminogen activator. Defects of neuroserpin are the cause of familial encephalopathy with neuroserpin inclusion bodies (FEN1B).
serpin peptidase inhibitor, clade I (neuroserpin), member 1
Schrimpf SP. et al., 1997, Genomics. 40 (1): 55-62.
Hill RM. et al., 2002, Ann N Y Acad Sci. 971: 406-15.
Yepes M. et al., 2004, Thromb. Haemost. 91 (3): 457-64.
Galliciotti G. et al., 2006, Front Biosci. 11: 33-45.
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