LRRN3 Protein (His Tag)

Leucine rich repeat neuronal 3 Protein Datasheet

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.
• Source: Human
• Expression Host: Baculovirus-Insect cells

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
• Molecular 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, pH7.0, 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.
• SDS-PAGE: LRRN3 protein

LRRN3 Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. 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.

LRRN3 Protein Description

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.

References

1. Yang J. et al., 2011, Zhong Nan Da Xue Xue Bao Yi Xue Ban. 36 (5): 424-9.
2. Hutcheson HB. et al., 2004, BMC Med Genet. 5 (5): 12.
3. Ishii N. et al., 1996, Brain Res Mol Brain Res. 40 (1):148-52.