|Datasheet||Specific References||Reviews||Related Products||Protocols|
|Vector Type||Mammalian Expression Vector|
|Expression Method||Constiutive ,Stable / Transient|
|Selection In Mammalian Cells||Hygromycin|
A myc tag is a polypeptide protein tag derived from the c-myc gene product that can be added to a protein using recombinant DNA technology. It can be used for affinity chromatography, then used to separate recombinant, overexpressed protein from wild type protein expressed by the host organism. It can also be used in the isolation of protein complexes with multiple subunits.
A myc tag can be used in many different assays that require recognition by an antibody. If there is no antibody against the studied protein, adding a myc-tag allows one to follow the protein with an antibody against the Myc epitope. Examples are cellular localization studies by immunofluorescence or detection by Western blotting.
The peptide sequence of the myc-tag is: N-EQKLISEEDL-C (1202 Da). It can be fused to the C-terminus and the N-terminus of a protein. It is advisable not to fuse the tag directly behind the signal peptide of a secretory protein, since it can interfere with translocation into the secretory pathway.
|Human APP / PN2 transcript variant 2 ORF mammalian expression plasmid, C-GFPSpark tag||HG10703-ACG|
|Human APP / PN2 transcript variant 2 ORF mammalian expression plasmid, C-OFPSpark / RFP tag||HG10703-ACR|
|Human APP / PN2 transcript variant 2 ORF mammalian expression plasmid, C-Flag tag||HG10703-CF|
|Human APP / PN2 transcript variant 2 ORF mammalian expression plasmid, C-His tag||HG10703-CH|
|Human APP / PN2 transcript variant 2 ORF mammalian expression plasmid, C-Myc tag||HG10703-CM|
|Human APP / PN2 transcript variant 2 ORF mammalian expression plasmid, C-HA tag||HG10703-CY|
|Human APP / PN2 transcript variant 2 Gene cDNA clone plasmid||HG10703-M|
|Human APP / PN2 transcript variant 2 ORF mammalian expression plasmid, N-Flag tag||HG10703-NF|
|Human APP / PN2 transcript variant 2 ORF mammalian expression plasmid, N-His tag||HG10703-NH|
|Human APP / PN2 transcript variant 2 ORF mammalian expression plasmid, N-Myc tag||HG10703-NM|
|Human APP / PN2 transcript variant 2 ORF mammalian expression plasmid, N-HA tag||HG10703-NY|
|Human APP / PN2 transcript variant 2 natural ORF mammalian expression plasmid||HG10703-UT|
|Learn more about expression Vectors|
Amyloid precursor protein (APP) is a type I transmembrane protein expressed in many tissues and concentrated in the synapses of neurons, and is suggested as a regulator of synapse formation and neural plasticity. APP can be processed by two different proteolytic pathways. In one pathway, APP is cleaved by β- and γ-secretase to produce the amyloid-β-protein (Aβ, Abeta, beta-amyloid) which is the principal component of the amyloid plaques, the major pathological hallmark of Alzheimer’s disease (AD), while in the other pathway, α-secretase is involved in the cleavage of APP whose product exerts antiamyloidogenic effect and prevention of the Aβ peptide formation. The aberrant accumulation of aggregated beta-amyloid peptides (Abeta) as plaques is a hallmark of AD neuropathology and reduction of Abeta has become a leading direction of emerging experimental therapies for the disease. Besides this pathological function of Abeta, recently published data reveal that Abeta also has an essential physiological role in lipid homeostasis. Cholesterol increases Abeta production, and conversely A beta production causes a decrease in cholesterol synthesis. Abeta may be part of a mechanism controlling synaptic activity, acting as a positive regulator presynaptically and a negative regulator postsynaptically. The pathological accumulation of oligomeric Abeta assemblies depresses excitatory transmission at the synaptic level, but also triggers aberrant patterns of neuronal circuit activity and epileptiform discharges at the network level. Abeta-induced dysfunction of inhibitory interneurons likely increases synchrony among excitatory principal cells and contributes to the destabilization of neuronal networks. There is evidence that beta-amyloid can impair blood vessel function. Vascular beta-amyloid deposition, also known as cerebral amyloid angiopathy, is associated with vascular dysfunction in animal and human studies. Alzheimer disease is associated with morphological changes in capillary networks, and soluble beta-amyloid produces abnormal vascular responses to physiological and pharmacological stimuli.