|Datasheet||Specific References||Reviews||Related Products||Protocols|
|Vector Type||Mammalian Expression Vector|
|Expression Method||Constiutive, Stable / Transient|
|Selection In Mammalian Cells||Hygromycin|
Human influenza hemagglutinin (HA) is a surface glycoprotein required for the infectivity of the human virus. The HA tag is derived from the HA-molecule corresponding to amino acids 98-106 has been extensively used as a general epitope tag in expression vectors. Many recombinant proteins have been engineered to express the HA tag, which does not appear to interfere with the bioactivity or the biodistribution of the recombinant protein. This tag facilitates the detection, isolation, and purification of the proteins.
The actual HA tag is as follows: 5' TAC CCA TAC GAT GTT CCA GAT TAC GCT 3' or 5' TAT CCA TAT GAT GTT CCA GAT TAT GCT 3' The amino acid sequence is: YPYDVPDYA.
|Human LRRN3 ORF mammalian expression plasmid, C-GFPSpark tag||HG11610-ACG|
|Human LRRN3 ORF mammalian expression plasmid, C-OFPSpark / RFP tag||HG11610-ACR|
|Human LRRN3 ORF mammalian expression plasmid, C-Flag tag||HG11610-CF|
|Human LRRN3 ORF mammalian expression plasmid, C-His tag||HG11610-CH|
|Human LRRN3 ORF mammalian expression plasmid, C-Myc tag||HG11610-CM|
|Human LRRN3 ORF mammalian expression plasmid, C-HA tag||HG11610-CY|
|Human LRRN3 Gene cDNA clone plasmid||HG11610-M|
|Human LRRN3 ORF mammalian expression plasmid, N-Flag tag||HG11610-NF|
|Human LRRN3 ORF mammalian expression plasmid, N-His tag||HG11610-NH|
|Human LRRN3 ORF mammalian expression plasmid, N-Myc tag||HG11610-NM|
|Human LRRN3 ORF mammalian expression plasmid, N-HA tag||HG11610-NY|
|Human LRRN3 natural ORF mammalian expression plasmid||HG11610-UT|
|Learn more about expression Vectors|
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.