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Results report the identification of Spn4A, a previously uncharacterized secretory pathway serine protease inhibitor (serpin) from Drosophila melanogaster that contains a consensus furin (show FURIN Proteins) cleavage site.
Spn4 gene represents a versatile defence tool kit that may provide multiple antiproteolytic functions.
The results of this identify neuroserpin as a modulator of synaptic plasticity, and point to a role for neuroserpin in learning and memory.
the protective effect of neuroserpin maybe independent from its canonical interaction with a tissue-type plasminogen activator (show PLAT Proteins)
Brain metastatic cells from lung cancer and breast cancer express high levels of anti-plasminogen (show PLG Proteins) activator (PA) serpins, including neuroserpin and serpin B2, to prevent plasmin (show PLG Proteins) generation and its metastasis-suppressive effects.
Data indicate that the neuroprotective effect of neuroserpin is due to inhibition of plasmin (show PLG Proteins)-mediated excitotoxin-induced cell death and is independent of neuroserpin's ability to inhibit tissue plasminogen activator (show PLAT Proteins) activity.
Neuroserpin reduces microglial activation and, therefore, plasminogen (show PLG Proteins) activator levels; it has a neuroprotective role after focal ischemic stroke.
Neuroserpin mRNA is widely expressed in neuronal cells in the primary visual cortex during normal development as well as in the adult mouse.
Our results implicate neuroserpin in the regulation of emotional behavior through a mechanism that is at least in part independent of tissue type plasminogen activator (show PLAT Proteins) activity
neuroserpin levels appear to be carefully regulated by LRP (show LRP1 Proteins) and an unidentified cofactor, and this pathway may be critical for maintaining the balance between proteases and inhibitors
Altogether, these data suggest that an overexpression of neuroserpin in the brain parenchyma might limit the deleterious effect of tPA (show PLAT Proteins) on NMDA receptor-mediated neuronal death, which occurs following experimental ischemia.
Transgenic mice overexpressing neuroserpin have decreased plasminogen (show PLG Proteins) activators in sciatic nerve and spinal cord, confirming a role for neuroserpin in the evolution of a neurodegenerative disease.
We present two pediatric cases of progressive myoclonic epilepsy with SERPINI1 pathogenic variants that lead to a severe presentation.
Data indicated that rs9853967 and rs11714980 polymorphisms in CCM3 (show PDCD10 Proteins) and SERPINI1respectively could be associated with a protective role in cerebral cavernous malformations disease.
SERPINI1 is an important regulator of epithelial-mesenchymal transition in an orthotopic implantation model of colorectal cancer
This C-terminal lability is not required for neuroserpin polymerisation in the endoplasmic reticulum, but the additional glycan facilitates degradation of the mutant protein during proteasomal impairment.
Neuroserpin is expressed in naive effector memory and central memory CD4 (show CD4 Proteins) and CD8 (show CD8A Proteins) T cell subsets, and monocytes, B cells, and NK cells. T-cell activation caused its translocation to the immunologic synapse, secretion, and delayed downregulation.
Molecular Dynamics simulations suggest that Neuroserpin conformational stability and flexibility arise from a spatial distribution of intramolecular salt-bridges and hydrogen bonds.
Alzheimer's disease brain tissues with elevated neuroserpin protein also showed increased expression of THRbeta1 and HuD (show ELAVL4 Proteins)
our study did not provide any evidence for an association between genetic variation at the SERPINI1 locus and ischemic stroke
Neuroprotective properties of neuroserpin may be related to the inhibition of excitotoxicity, inflammation, as well as blood brain barrier disruption that occur after acute ischemic stroke.
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.
, serine protease inhibitor 4
, serpin 4
, serpin 42Da
, serpin peptidase inhibitor, clade I (neuroserpin), member 1
, peptidase inhibitor 12
, protease inhibitor 17
, serine protease inhibitor 17
, serpin I1
, serine (or cysteine) proteinase inhibitor, clade I (neuroserpin), member 1
, serine (or cysteine) peptidase inhibitor, clade I, member 1
, serine (or cysteine) proteinase inhibitor clade member 1
, serpin peptidase inhibitor, clade I, member 1