|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 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 TPSB2 ORF mammalian expression plasmid, C-GFPSpark tag||HG10505-ACG|
|Human TPSB2 ORF mammalian expression plasmid, C-OFPSpark / RFP tag||HG10505-ACR|
|Human TPSB2 ORF mammalian expression plasmid, C-Flag tag||HG10505-CF|
|Human TPSB2 ORF mammalian expression plasmid, C-His tag||HG10505-CH|
|Human TPSB2 ORF mammalian expression plasmid, C-Myc tag||HG10505-CM|
|Human TPSB2 ORF mammalian expression plasmid, C-HA tag||HG10505-CY|
|Human TPSB2 Gene cDNA clone plasmid||HG10505-M|
|Human TPSB2 ORF mammalian expression plasmid, N-Flag tag||HG10505-NF|
|Human TPSB2 ORF mammalian expression plasmid, N-His tag||HG10505-NH|
|Human TPSB2 ORF mammalian expression plasmid, N-Myc tag||HG10505-NM|
|Human TPSB2 ORF mammalian expression plasmid, N-HA tag||HG10505-NY|
|Human TPSB2 natural ORF mammalian expression plasmid||HG10505-UT|
|Learn more about expression Vectors|
Tryptases comprise a family of trypsin-like serine proteases, the peptidase family S1, and fall into two groups, α and β. β-tryptases appear to be the main isoenzymes expressed in mast cells, whereas α-tryptases predominate in basophils. Tryptase is unique in two respects: it is enzymatically active only as a heparin-stabilized tetramer, and it is resistant to all known endogenous proteinase inhibitors because of the unique arrangement of the active sites. Additionally, tryptase family genes have an intron immediately upstream of the initiator codon which separates the transcription initiation site from protein coding sequence, and this feature is characteristic of tryptases. β-tryptases existing in three isoforms (β1,β2,β3) are released in secretory granules, and have been implicated as mediators in the pathogenesis of asthma and other allergic and inflammatory disorders. It has been reported that β-tryptase selectively cleaves ASM-derived eotaxin and RANTES and abrogates their chemotactic activities.