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Human LRRN3 Protein (His Tag)

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Human LRRN3 Protein Product Information
Synonym:Nbla10363, FIGLER5, FLJ11129, NLRR-3, NLRR3
Protein Construction:A DNA sequence encoding the human LRRN3 (AAH35133.1) extracellular domain (Met 1-Thr 628) was fused with a polyhistidine tag at the C-terminus.
Expressed Host:Baculovirus-Insect Cells
Shipping:In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Human LRRN3 Protein QC Testing
Purity:> 90 % as determined by SDS-PAGE
Endotoxin:< 1.0 EU per μg of the protein as determined by the LAL method
Stability:Samples are stable for up to twelve months from date of receipt at -70℃
Predicted N Terminal:Met 1
Molecule Mass:The recombinant human LRRN3 consists of 616 amino acids and predicts a molecular mass of 70 kDa as estimated in SDS-PAGE under reducing conditions.
Formulation:Lyophilized from sterile 20mM Tris, 500mM NaCl, pH 7.0, 10% gly
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
Human LRRN3 Protein Usage Guide
Storage:Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution:A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
Human LRRN3 Protein SDS-PAGE
Human LRRN3 Protein (His Tag) SDS-PAGE
Other LRRN3 Recombinant Protein Products
LRRN3 Background

Leucine-rich repeat neuronal protein 3, also known as neuronal leucine-rich repeat protein 3 (NLRR-3), is a member of leucine-rich (LRR) family whose members have significant functions in neural development. Leucine-rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. All proteins containing these repeats are thought to be involved in protein-protein interactions. The crystal structure of ribonuclease inhibitor protein has revealed that leucine-rich repeats correspond to β-α structural units. These units are arranged so that they form a parallel β-sheet with one surface exposed to solvent, so that the protein acquires an unusual, non-globular shape. These two features may be responsible for the protein-binding functions of proteins containing leucine-rich repeats. LRRN3 plays an important role in cerebellum postnatal development. In a unilateral cortical injury cerebral cortex, NLRR-3 mRNA increased in layers 2-3 which suggests that NLRR-3 may be an important component of the pathophysiological response to brain injury. 

Human LRRN3 References
  • Yang J, et al. (2011) Role of LRRN3 in the cerebellum postnatal development in rats. Zhong Nan Da Xue Xue Bao Yi Xue Ban. 36 (5): 424-9.
  • Hutcheson HB, et al. (2004) Examination of NRCAM, LRRN3, KIAA0716, and LAMB1 as autism candidate genes. BMC Med Genet. 5: 12.
  • Ishii N, et al. (1996) Increased expression of NLRR-3 mRNA after cortical brain injury in mouse. Brain Res Mol Brain Res. 40 (1): 148-52.
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    Catalog: 11610-H08B-50
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