Skip to Content
MilliporeSigma
All Photos(1)

Key Documents

SRP3122

Sigma-Aldrich

Neuritin human

recombinant, expressed in E. coli, ≥98% (SDS-PAGE), ≥98% (HPLC), suitable for cell culture

Synonym(s):

CPG15, NRN1

Sign Into View Organizational & Contract Pricing


About This Item

UNSPSC Code:
12352202
NACRES:
NA.32

biological source

human

recombinant

expressed in E. coli

assay

≥98% (HPLC)
≥98% (SDS-PAGE)

form

lyophilized

potency

20.0-30.0 ng/mL ED50

mol wt

9.7 kDa

packaging

pkg of 20 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 ... NRN1(51299)

General description

NRN1 (neuritin 1) is a highly conserved extracellular GPI (glycosylphosphatidylinositol)-anchored protein that was initially identified in rat hippocampal dentate gyrus in a screening of candidate kainic acid-induced plasticity related genes. This protein is also secreted in a soluble form.
Recombinant human Neuritin is a covalently disulfide-linked homodimer, consisting of two 9.8kDa polypeptide monomers, each containing 89 amino acid residues.

Biochem/physiol Actions

NRN1 (neuritin 1) is implicated in synaptic plasticity during brain development, and is an activity-dependent protein. Synaptic plasticity is dependent upon neuronal migration, and a study shows that NRN1 protein facilitates neuronal cell migration, and its levels influence microtubule stability. This protein also promotes dendritic arborization and synapse maturation in the central nervous system (CNS). It facilitates the survival of neural progenitors and differentiated neurons during early embryonic development, and during late development it is responsible for the maturation and formation of synapses by promoting the growth and stabilization of axons and dendrites. Study in human microendothelial cells (HMEC-1) shows that the expression of this protein is hypoxia-induced, and it is a hypoxic perinecrotic marker.
Recombinant human Neuritin is a covalently disulfide-linked homodimer, consisting of two 9.8kDa polypeptide monomers, each containing 89 amino acid residues.

Sequence

MAGKCDAVFK GFSDCLLKLG DSMANYPQGL DDKTNIKTVC TYWEDFHSCT VTALTDCQEG AKDMWDKLRK ESKNLNIQGS LFELCGSGN

Physical form

Lyophilized with no additives.

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


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Neuritin 1 promotes retinal ganglion cell survival and axonal regeneration following optic nerve crush.
Sharma TP et al
Cell Death & Disease, 6, e1661-e1661 (2015)
Characterization of the expression of the hypoxia-induced genes neuritin, TXNIP and IGFBP3 in cancer.
Le Jan S et al
Febs Letters, 580(14), 3395-3400 (2006)
Neuritin 1 promotes neuronal migration.
Zito A et al
Brain Structure &Amp; Function, 219(1), 105-118 (2014)
G S Naeve et al.
Proceedings of the National Academy of Sciences of the United States of America, 94(6), 2648-2653 (1997-03-18)
Neural activity and neurotrophins induce synaptic remodeling in part by altering gene expression. A cDNA encoding a glycosylphoshatidylinositol-anchored protein was identified by screening for hippocampal genes that are induced by neural activity. This molecule, named neuritin, is expressed in postmitotic-differentiating

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service