SRP3123
Neuroserpin human
recombinant, expressed in E. coli, ≥96% (SDS-PAGE), ≥96% (HPLC), suitable for cell culture
Synonym(s):
Protease inhibitor 12, Serpin I1
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About This Item
UNSPSC Code:
12352202
NACRES:
NA.32
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biological source
human
recombinant
expressed in E. coli
assay
≥96% (HPLC)
≥96% (SDS-PAGE)
form
lyophilized
mol wt
44.6 kDa
packaging
pkg of 25 μg
technique(s)
cell culture | mammalian: suitable
impurities
<0.1 EU/μg endotoxin, tested
color
white to off-white
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
Gene Information
human ... SERPINI1(5274)
General description
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.
Biochem/physiol Actions
SERPINI1, also known as neuroserpin, is a serine proteinase inhibitor that belongs to the serpin superfamily. It inhibits plasminogen activators and plasmin but not thrombin and is predominantly secreted by axons in the brain. Neuroserpin may be involved in the regulation of axonal growth and the development of synaptic plasticity. Defects in this gene cause familial encephalopathy with neuroserpin inclusion bodies (FENIB), which is characterized by the accumulation of mutant neuroserpin polymers. The protein may have a role in colorectal cancer.
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
Physical form
Lyophilized from 20 mM Sodium Phosphate pH 7.8 + 50 mM NaCl.
Reconstitution
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 Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Find documentation for the products that you have recently purchased in the Document Library.
An overview of the serpin superfamily
Ruby H P Law
Genome Biology, 7 (2006)
SERPINI1 regulates epithelial-mesenchymal transition in an orthotopic implantation model of colorectal cancer
Yasufumi Matsuda
Cancer Science, 107 (2016)
E Miranda et al.
Cellular and molecular life sciences : CMLS, 63(6), 709-722 (2006-02-09)
Proteinases and their inhibitors play important roles in neural development, homeostasis and disease. Neuroserpin is a member of the serine proteinase inhibitor (serpin) superfamily that is secreted from the growth cones of neurons and inhibits the enzyme tissue-type plasminogen activator
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