Mouse SERPINI1 Protein (His Tag)

Serine (or cysteine) peptidase inhibitor, clade I, member 1 Protein Datasheet

SERPINI1 Protein Product Information

• Synonym: AI837402, Ns, PI-12, PI12, Spi17
• Protein Construction: A DNA sequence encoding the mouse SERPINI1 (O35684) (Met 1-Leu 410) was expressed, with a C-terminal polyhistidine tag.
• Source: Mouse
• Expression Host: Human Cells

SERPINI1 Protein QC Testing

• Purity: > 95 % as determined by SDS-PAGE.
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: Thr 17
• Molecular Mass: The secreted recombinant mouse SERPINI1 comprises 405 amino acids and has a calculated molecular mass of 46 kDa. The apparent molecular mass of rmSERPINI1 is approximately 45-50 kDa in SDS-PAGE under reducing conditions as a result of glycosylation.
• Formulation: Lyophilized from sterile PBS , pH 7.4
  1. Normally 5 % - 8 % trehalose and mannitol 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.
• SDS-PAGE: SERPINI1 protein

SERPINI1 Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. 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.

SERPINI1 Protein Description

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).

References

1. Schrimpf SP. et al., 1997, Genomics. 40 (1): 55-62.
2. Hill RM. et al., 2002, Ann N Y Acad Sci. 971: 406-15.
3. Yepes M. et al., 2004, Thromb. Haemost. 91 (3): 457-64.
4. Galliciotti G. et al., 2006, Front Biosci. 11: 33-45.