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Recombinant Human LRRN3 Protein (His Tag)
SKU: PKSH031067-100
Recombinant Human LRRN3 Protein (His Tag)
| SKU # | PKSH031067 |
| Expression Host | Baculovirus-Insect Cells |
Description
| Synonyms | FIGLER5, NLRR-3, NLRR3 |
| Species | Human |
| Expression Host | Baculovirus-Insect Cells |
| Sequence | Met 1-Thr 628 |
| Accession | AAH35133.1 |
| Calculated Molecular Weight | 70.0 kDa |
| Observed Molecular Weight | 70 kDa |
| Tag | C-His |
| Bio-activity | Not validated for activity |
Properties
| Purity | > 90 % as determined by reducing SDS-PAGE. |
| Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method. |
| Storage | Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months. |
| Shipping | This product is provided as lyophilized powder which is shipped with ice packs. |
| Formulation | Lyophilized from sterile 20mM Tris, 500mM NaCl,，10% glycerol, 3Mm DTT, 0.5mM PMSF, pH8.5, 5% trehalose, 5%mannitol, 0.01% Tween 80 Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual. |
| Reconstitution | Please refer to the printed manual for detailed information. |
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.