|Application ||WB, FC, IF, IHC-P, E|
|Calculated MW||46427 Da|
|Antigen Region||19-45 aa|
|Other Names||Neuroserpin, Peptidase inhibitor 12, PI-12, Serpin I1, SERPINI1, PI12|
|Target/Specificity||This SERPINI1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 19-45 amino acids from the N-terminal region of human SERPINI1.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||SERPINI1 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Serine protease inhibitor that inhibits plasminogen activators and plasmin but not thrombin (PubMed:9442076, PubMed:26329378, PubMed:19265707, PubMed:19285087, PubMed:11880376). May be involved in the formation or reorganization of synaptic connections as well as for synaptic plasticity in the adult nervous system. May protect neurons from cell damage by tissue-type plasminogen activator (Probable).|
|Cellular Location||Secreted. Cytoplasmic vesicle, secretory vesicle lumen. Perikaryon|
|Tissue Location||Detected in brain cortex and hippocampus pyramidal neurons (at protein level) (PubMed:17040209) Predominantly expressed in the brain (PubMed:9070919)|
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Provided below are standard protocols that you may find useful for product applications.
This gene encodes a member of the serpin superfamily of serine proteinase inhibitors. The protein is primarily secreted by axons in the brain, and preferentially reacts with and inhibits tissue-type plasminogen activator. It is thought to play a role in the regulation of axonal growth and the development of synaptic plasticity. Mutations in this gene result in familial encephalopathy with neuroserpin inclusion bodies (FENIB), which is a dominantly inherited form of familial encephalopathy and epilepsy characterized by the accumulation of mutant neuroserpin polymers. Multiple alternatively spliced variants, encoding the same protein, have been identified.
Takehara, S., et al. J. Mol. Biol. 403(5):751-762(2010)
Han, S., et al. Hum. Immunol. 71(7):727-730(2010)
Rajaraman, P., et al. Cancer Epidemiol. Biomarkers Prev. 19(5):1356-1361(2010)
Davies, M.J., et al. J. Biol. Chem. 284(27):18202-18209(2009)
Rajaraman, P., et al. Cancer Epidemiol. Biomarkers Prev. 18(5):1651-1658(2009)
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