|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.
|人 HSP90AA1 基因全长ORF克隆 (表达载体), C端GFPSpark标签||HG11445-ACG|
|人 HSP90AA1 基因全长ORF克隆 (表达载体), C端OFPSpark标签||HG11445-ACR|
|人 HSP90AA1 基因全长ORF克隆 (表达载体), N端GFPSpark标签||HG11445-ANG|
|人 HSP90AA1 基因全长ORF克隆 (表达载体), N端OFPSpark标签||HG11445-ANR|
|人 HSP90AA1 基因全长ORF克隆 (表达载体), C端FLAG标签||HG11445-CF|
|人 HSP90AA1 基因全长ORF克隆 (表达载体), C端His标签||HG11445-CH|
|人 HSP90AA1 基因全长ORF克隆 (表达载体), C端Myc标签||HG11445-CM|
|人 HSP90AA1 基因全长ORF克隆 (表达载体), C端HA标签||HG11445-CY|
|人 HSP90AA1 基因全长ORF克隆||HG11445-G|
|人 HSP90AA1 基因全长ORF克隆 (表达载体), N端FLAG标签||HG11445-NF|
|人 HSP90AA1 基因全长ORF克隆 (表达载体), N端His标签||HG11445-NH|
|人 HSP90AA1 基因全长ORF克隆 (表达载体), N端Myc标签||HG11445-NM|
|人 HSP90AA1 基因全长ORF克隆 (表达载体), N端HA标签||HG11445-NY|
|人 HSP90AA1 基因全长ORF克隆 (表达载体), 无标签||HG11445-UT|
Heat shock protein 90 (90 kDa heat-shock protein, HSP90) is a molecular chaperone involved in the trafficking of proteins in the cell. It is a remarkably versatile protein involved in the stress response and in normal homoeostatic control mechanisms. HSP90 interacts with 'client proteins', including protein kinases, transcription factors and others, and either facilitates their stabilization and activation or directs them for proteasomal degradation. By this means, HSP90 displays a multifaceted ability to influence signal transduction, chromatin remodelling and epigenetic regulation, development and morphological evolution. HSP90 operates as a dimer in a conformational cycle driven by ATP binding and hydrolysis at the N-terminus. Disruption of HSP90 leads to client protein degradation and often cell death. Under stressful conditions, HSP90 stabilizes its client proteins and provides protection to the cell against cellular stressors such as in cancer cells. Especially, several oncoproteins act as HSP90 client proteins and tumor cells require higher HSP90 activity than normal cells to maintain their malignancy. For this reason, Hsp90 has emerged as a promising target for anti-cancer drug development.