Name : Mouse LRRN1 Protein
Product Source :
Recombinant Mouse LRRN1 Protein is expressed from HEK293 with His tag at the C-Terminus. It contains Ser26-Ala631.[Accession | Q61809]
Molecular Weight :
The protein has a predicted MW of 69.28 kDa. Due to glycosylation, the protein migrates to 80-90 kDa based on Tris-Bis PAGE result.
Endotoxin Level :
Less than 1EU per μg by the LAL method.
Purity :
> 95% as determined by Tris-Bis PAGE> 95% as determined by HPLC
Formulation :
Lyophilized from 0.22μm filtered solution in PBS (pH 7.4). Normally 8% trehalose is added as protectant before lyophilization.
Reconstitution :
Centrifuge the tube before opening. Reconstituting to a concentration more than 100 μg/ml is recommended. Dissolve the lyophilized protein in distilled water.
Storage and Stability :
-20 to -80°C for 12 months as supplied from date of receipt.-80°C for 3-6 months after reconstitution.2-8°C for 2-7 days after reconstitution.Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Product Concentration :
Tris-Bis PAGE Mouse LRRN1 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%. SEC-HPLC The purity of Mouse LRRN1 is greater than 95% as determined by SEC-HPLC.
Background :
Lrrn1 is required for the formation of MHB–loss of function leads to a loss of the morphological constriction and loss of Fgf8. Cells overexpressing Lrrn1 violate the boundary and result in a loss of cell restriction between midbrain and hindbrain compartments. Lrrn1 also regulates the glycosyltransferase Lunatic Fringe, a modulator of Notch signalling, maintaining its expression in midbrain cells which is instrumental in MHB boundary formation.
Synonyms :
Leucine-rich repeat neuronal protein 1; Neuronal leucine-rich repeat protein 1; NLRR-1; NLRR1; FIGLER3; KIAA1497; LRN
References & Citations :
Tossell K, Andreae LC, Cudmore C, Lang E, Muthukrishnan U, Lumsden A, Gilthorpe JD, Irving C. Lrrn1 is required for formation of the midbrain-hindbrain boundary and organiser through regulation of affinity differences between midbrain and hindbrain cells in chick. Dev Biol. 2011 Apr 15;352(2):341-52. doi: 10.1016/j.ydbio.2011.02.002. Epub 2011 Feb 18. PMID: 21315708; PMCID: PMC3084456.
Related category websites: https://www.medchemexpress.com/recombinant-proteins.html
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