|Calculated MW||44.8 kDa|
|Other Names||Serpin I1, Protease inhibitor 12|
|Sequence||MTGATFPEEA IADLSVNMYN RLRATGEDEN ILFSPLSIAL AMGMMELGAQ GSTQKEIRHS MGYDSLKNGE EFSFLKEFSN MVTAKESQYV MKIANSLFVQ NGFHVNEEFL QMMKKYFNAA VNHVDFSQNV AVANYINKWV ENNTNNLVKD LVSPRDFDAA TYLALINAVY FKGNWKSQFR PENTRTFSFT KDDESEVQIP MMYQQGEFYY GEFSDGSNEA GGIYQVLEIP YEGDEISMML VLSRQEVPLA TLEPLVKAQL VEEWANSVKK QKVEVYLPRF TVEQEIDLKD VLKALGITEI FIKDANLTGL SDNKEIFLSK AIHKSFLEVN EEGSEAAAVS GMIAISRMAV LYPQVIVDHP FFFLIRNRRT GTILFMGRVM HPETMNTSGH DFEEL|
|Application Notes||Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 week. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at -20°C to -80°C.|
|Storage||-20°C; Sterile filtered through a 0.2 micron filter. Lyophilized from 20 mM Sodium Phosphate pH 7.8 and 50 mM NaCl|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Neuroserpin is an inhibitory serpin that is expressed predominantly in central nervous system. Although the physiological target of neuroserpin is still unclear, cumulative evidence suggest that it plays an important role in controlling proteolytic degradation of extracellular matrix (ECM) during synaptogenesis and the subsequent development of neuronal plasticity. In the adult brain, neuroserpin is secreted from the growth cones of neurons in areas where synaptic changes are associated with learning and memory, i.e. cerebral cortex, hippocampus, and amygdala. The neuroprotective role of neuroserpin has been demonstrated in transgenic mice lacking neuroserpin expression. The deficiency of neuroserpin in these mice was associated with motor neuron disease characterized by axonal degradation. In humans, defects in neuroserpin, caused by point mutations in the neuroserpin gene, underlie a hereditary disorder called the familial encephalopathy with neuroserpin inclusion bodies (FENIB). Recombinant human neuroserpin is a 44.8 kDa non-glycosylated protein containing 395 amino-acid residues.
Schrimpf S.P.,et al.Genomics 40:55-62(1997).
Kinter J.,et al.Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Bechtel S.,et al.BMC Genomics 8:399-399(2007).
Mural R.J.,et al.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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