Background
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 44.6 kDa non-glycosylated protein containing 394 amino-acid residues.
Specifications
Additional Names
Serpin I1, Protease inhibitor 12
Preparation
Determined by the dose - dependent stimulation of the proliferation of rat C6 cells using a concentration range of 0.3 - 0.6 μg/ml.
Location
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
Source
E. coli
Reactivity
n/a
Tested Application
n/a
Storage
The lyophilized Neuroserpin recombinant protein is stable for at least 2 years from date of receipt at -20ËšC. Reconstituted Neuroserpin is stable for at least 3 months when stored in working aliquots with a carrier protein at -20ËšC. As with any protein, exposing Neuroserpin recombinant protein to repeated freeze / thaw cycles is not recommended. When working with proteins care should be taken to keep recombinant protein at a cool and stable temperature.
Species Reactivity
n/a
Purity
Greater than 96% by SDS-PAGE gel and HPLC analyses.
Endotoxin level is less than 0.1 ng per μg (1EU/μg).
