Recombinant Human Neuroserpin Protein (SERPINI1), Active

Name: Recombinant Human Neuroserpin Protein (SERPINI1), Active
Brand: Beta LifeScience
SKU: BLC-05557P
Availability: InStock

Collections: All products, Featured enzyme molecules, High-quality recombinant proteins

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Product Overview

Description	Recombinant Human Neuroserpin Protein (SERPINI1), Active is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 95% as determined by SDS-PAGE and HPLC.
Endotoxin	Less than 1.0 EU/μg as determined by LAL method.
Activity	Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using rat C6 cells is less than 0.5 μg/ml, corresponding to a specific activity of >2000 IU/mg.
Uniprotkb	Q99574
Target Symbol	SERPINI1
Synonyms	DKFZp781N13156; Neuroserpin; NEUS_HUMAN; Peptidase inhibitor 12; PI-12; PI12; Protease inhibitor 12 ; Serine or cysteine proteinase inhibitor clade I (neuroserpin) member 1; Serine or cysteine proteinase inhibitor clade I member 1; Serpin I1; Serpin peptidase inhibitor clade I (neuroserpin) member 1; SERPINI1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	Tag-Free
Complete Sequence	TGATFPEEAIADLSVNMYNRLRATGEDENILFSPLSIALAMGMMELGAQGSTQKEIRHSMGYDSLKNGEEFSFLKEFSNMVTAKESQYVMKIANSLFVQNGFHVNEEFLQMMKKYFNAAVNHVDFSQNVAVANYINKWVENNTNNLVKDLVSPRDFDAATYLALINAVYFKGNWKSQFRPENTRTFSFTKDDESEVQIPMMYQQGEFYYGEFSDGSNEAGGIYQVLEIPYEGDEISMMLVLSRQEVPLATLEPLVKAQLVEEWANSVKKQKVEVYLPRFTVEQEIDLKDVLKALGITEIFIKDANLTGLSDNKEIFLSKAIHKSFLEVNEEGSEAAAVSGMIAISRMAVLYPQVIVDHPFFFLIRNRRTGTILFMGRVMHPETMNTSGHDFEEL
Expression Range	17-410aa
Protein Length	Full Length of Mature Protein
Mol. Weight	44.7 kDa
Research Area	Neuroscience
Form	Lyophilized powder
Buffer	Lyophilized from a 0.2 µm filtered PBS, pH 7.5
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Serine protease inhibitor that inhibits plasminogen activators and plasmin but not thrombin. May be involved in the formation or reorganization of synaptic connections as well as for synaptic plasticity in the adult nervous system. May protect neurons from cell damage by tissue-type plasminogen activator (Probable).
Subcellular Location	Secreted. Cytoplasmic vesicle, secretory vesicle lumen. Perikaryon.
Protein Families	Serpin family
Database References	HGNC: 8943 OMIM: 602445 KEGG: hsa:5274 STRING: 9606.ENSP00000295777 UniGene: PMID: 28631894 Data indicated that rs9853967 and rs11714980 polymorphisms in CCM3 and SERPINI1respectively could be associated with a protective role in cerebral cavernous malformations disease. PMID: 27737651 SERPINI1 is an important regulator of epithelial-mesenchymal transition in an orthotopic implantation model of colorectal cancer PMID: 26892864 The thermal and chemical stability along with the polymerisation propensity of both Wild Type and Glu289Ala NS were characterized. PMID: 26329378 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. PMID: 26367528 the protective effect of neuroserpin maybe independent from its canonical interaction with a tissue-type plasminogen activator PMID: 26176694 Neuroserpin is expressed in naive effector memory and central memory CD4 and CD8 T cell subsets, and monocytes, B cells, and NK cells. T-cell activation caused its translocation to the immunologic synapse, secretion, and delayed downregulation. PMID: 25670787 Molecular Dynamics simulations suggest that Neuroserpin conformational stability and flexibility arise from a spatial distribution of intramolecular salt-bridges and hydrogen bonds. PMID: 25450507 Alzheimer's disease brain tissues with elevated neuroserpin protein also showed increased expression of THRbeta1 and HuD PMID: 24036060 our study did not provide any evidence for an association between genetic variation at the SERPINI1 locus and ischemic stroke PMID: 21487809 the origins of conformational lability PMID: 21961602 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. PMID: 21569344 Hrd1 and gp78 mediate mutant neuroserpin turnover through the ERAD pathway. PMID: 21507957 high serum neuroserpin levels before intravenous tPA and neuroserpin levels decrease at 24 h after ischaemic stroke, independently of tPA treatment, may have a role in good functional outcome PMID: 21174006 The latent and polymer hNS forms obtained at 45 degrees C and 85 degrees C differ in their chemical and thermal stabilities; furthermore, the human neuroserpin polymers also differ in size and morphology PMID: 21081089 investigated the refolding and polymerization pathways of wild-type neuroserpin and of the pathogenic mutants S49P and H338R PMID: 20691191 Mutant Neuroserpin (S49P) that causes familial encephalopathy with neuroserpin inclusion bodies is a poor proteinase inhibitor and readily forms polymers in vitro PMID: 11880376 The interactions between NSP and t-PA were distinct from those between plasmin and NSP, suggesting that the physiologic effect of t-PA-NSP interactions may be more complex than previously thought. PMID: 12228252 Neuroserpin has a role as a selective inhibitor of tissue-type plasminogen activator in the central nervous system [review] PMID: 14983220 neuroserpin mutants that cause dementia accumulate as polymers within the endoplasmic reticulum PMID: 15090543 tissue plasminogen activator and neuroserpin are widely expressed in the human central nervous system PMID: 15269833 reactive centre loop of neuroserpin Portland being partially inserted into beta-sheet A to adopt a conformation similar to an intermediate on the polymerization pathway PMID: 15291813 Data show that the S49P mutant of neuroserpin that causes the dementia familial encephalopathy with neuroserpin inclusion bodies (FENIB) forms a latent species in vitro and in vivo in addition to the formation of polymers. PMID: 15664988 neuroserpin interacts with Abeta(1-42) to form off-pathway non-toxic oligomers and so protects neurons in Alzheimer disease PMID: 16849336 intergenic region of the head-to-head PDCD10-SERPINI1 gene pair provides an interesting and informative example of a complex regulatory system PMID: 17212813 in a French family with the S52R mutation of the neuroserpin gene, progressive myoclonic epilepsy was associated with a frontal syndrome PMID: 17606885 This study provides the first evidence that neuroserpin is associated with early-onset ischemic stroke among Caucasian women. PMID: 17961231 conformational modification in the protein under oxidative stress PMID: 18051703 We report a neuroserpin mutation that causes electrical status epilepticus of slow-wave sleep. PMID: 18591508 Neuroserpin and tissue plasminogen activator are associated with amyloid-beta plaques in Alzheimer brain tissue. PMID: 19222708 Human neuroserpin: structure and time-dependent inhibition PMID: 19265707 Analyses restricted to glioblastoma (n = 254) yielded significant associations for the SELP, DEFB126/127, SERPINI1, and LY96 genetic regions. PMID: 19423540 intracellular neuroserpin polymers activate NF-kappaB by a pathway that is independent of the IRE1, ATF6, and PERK limbs of the canonical unfolded protein response but is dependent on intracellular calcium PMID: 19423713

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.