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SRP3123

Sigma-Aldrich

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

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 Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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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
SERPINI1 regulates epithelial-mesenchymal transition in an orthotopic implantation model of colorectal cancer
Yasufumi Matsuda
Cancer Science, 107 (2016)
An overview of the serpin superfamily
Ruby H P Law
Genome Biology, 7 (2006)
Jianping Guo et al.
Advanced science (Weinheim, Baden-Wurttemberg, Germany), 8(18), e2004303-e2004303 (2021-07-20)
Copper plays pivotal roles in metabolic homoeostasis, but its potential role in human tumorigenesis is not well defined. Here, it is revealed that copper activates the phosphoinositide 3-kinase (PI3K)-protein kinase B (PKB, also termed AKT) oncogenic signaling pathway to facilitate

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