LRRN3 Protein (His tag)
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- Target See all LRRN3 products
- LRRN3 (Leucine Rich Repeat Neuronal 3 (LRRN3))
- Protein Type
- Recombinant
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Origin
- Human
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Source
- Baculovirus infected Insect Cells
- Purification tag / Conjugate
- This LRRN3 protein is labelled with His tag.
- Purpose
- Recombinant Human LRRN3 Protein (His Tag)
- Sequence
- Met 1-Thr 628
- Characteristics
- 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.
- Purity
- > 90 % as determined by reducing SDS-PAGE.
- Endotoxin Level
- < 1.0 EU per μg as determined by the LAL method.
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- Restrictions
- For Research Use only
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- Format
- Lyophilized
- Reconstitution
- Please refer to the printed manual for detailed information.
- Buffer
- Lyophilized from sterile 20 mM Tris, 500 mM NaCl, pH 7.0, 10 % glycerol
- Storage
- 4 °C,-20 °C,-80 °C
- Storage Comment
- Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
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- Target
- LRRN3 (Leucine Rich Repeat Neuronal 3 (LRRN3))
- Alternative Name
- LRRN3 (LRRN3 Products)
- Synonyms
- nlrr3 Protein, nlrr-3 Protein, MGC146637 Protein, FIGLER5 Protein, NLRR-3 Protein, NLRR3 Protein, Nlrr3 Protein, leucine rich repeat neuronal 3 Protein, leucine rich repeat protein 3, neuronal Protein, LRRN3 Protein, lrrn3 Protein, Lrrn3 Protein
- Background
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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.
Synonym: FIGLER5;NLRR-3;NLRR3
- Molecular Weight
- 70 kDa
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