|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.
|Rat CTSS ORF mammalian expression plasmid, C-GFPSpark tag||RG80443-ACG|
|Rat CTSS ORF mammalian expression plasmid, C-OFPSpark / RFP tag||RG80443-ACR|
|Rat CTSS ORF mammalian expression plasmid, C-Flag tag||RG80443-CF|
|Rat CTSS ORF mammalian expression plasmid, C-His tag||RG80443-CH|
|Rat CTSS ORF mammalian expression plasmid, C-Myc tag||RG80443-CM|
|Rat CTSS ORF mammalian expression plasmid, C-HA tag||RG80443-CY|
|Rat CTSS Gene cDNA clone plasmid||RG80443-G|
|Rat CTSS ORF mammalian expression plasmid, N-Flag tag||RG80443-NF|
|Rat CTSS ORF mammalian expression plasmid, N-His tag||RG80443-NH|
|Rat CTSS ORF mammalian expression plasmid, N-Myc tag||RG80443-NM|
|Rat CTSS ORF mammalian expression plasmid, N-HA tag||RG80443-NY|
|Rat CTSS natural ORF mammalian expression plasmid||RG80443-UT|
|Learn more about expression Vectors|
Cathepsin S (CTSS), one of the lysosomal proteinases, has many important physiological functions in the nervous system, especially in process of extracellular matrix degradation and endocellular antigen presentation. CTSS is synthesized as inactive precursor of 331 amino acids consisting of a 15-aa signal peptide, a propeptide of 99 aa, and a mature polypeptide of 217 aa. It is activated in the lysosomes by a proteolytic cleavage of the propeptide. Cathepsin S is expressed in the lysosome of antigen presenting cells, primarily dendritic cells, B-cells and macrophages. Compared with other lysosomal cysteine proteases, cathepsin S has displayed some unique characteristics. Cathepsin S is most well known for its critical function in the proteolytic digestion of the invariant chain chaperone molecules, thus controlling antigen presentation to CD4+ T-cells by major histocompatibility complex (MHC) class II molecules or to NK1.1+ T-cells via CD1 molecules. Cathepsin S also appears to participate in direct processing of exogenous antigens for presentation by MHC class II to CD4+ T-cells, or in cross-presentation by MHC class I molecules to CD8+ T-cells. In addition, although direct evidence is still lacking, in its secreted form cathepsin S is implicated in degradation of the extracellular matrix, which may contribute to the pathology of a number of diseases, including arthritis, atherosclerosis, neurological diseases and chronic obstructive pulmonary disease.