( We provide with HSP90AA1 qPCR primers for gene expression analysis, MP201868 )
|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.
|小鼠 HSP90/HSP90AA1 基因ORF全长cDNA克隆(表达载体), C-GFPSpark 标签||MG51995-ACG|
|小鼠 HSP90/HSP90AA1 基因ORF全长cDNA克隆(表达载体), C-OFPSpark 标签||MG51995-ACR|
|小鼠 HSP90/HSP90AA1 基因ORF全长cDNA克隆(表达载体), N-GFPSpark 标签||MG51995-ANG|
|小鼠 HSP90/HSP90AA1 基因ORF全长cDNA克隆(表达载体), N-OFPSpark 标签||MG51995-ANR|
|小鼠 HSP90/HSP90AA1 基因ORF全长cDNA克隆(表达载体), C-Flag 标签||MG51995-CF|
|小鼠 HSP90/HSP90AA1 基因ORF全长cDNA克隆(表达载体), C-His 标签||MG51995-CH|
|小鼠 HSP90/HSP90AA1 基因ORF全长cDNA克隆(表达载体), C-Myc 标签||MG51995-CM|
|小鼠 HSP90/HSP90AA1 基因ORF全长cDNA克隆(表达载体), C-HA 标签||MG51995-CY|
|小鼠 HSP90/HSP90AA1 基因ORF全长cDNA(克隆载体)||MG51995-G|
|小鼠 HSP90/HSP90AA1 基因ORF全长cDNA克隆(表达载体), N-Flag 标签||MG51995-NF|
|小鼠 HSP90/HSP90AA1 基因ORF全长cDNA克隆(表达载体), N-His 标签||MG51995-NH|
|小鼠 HSP90/HSP90AA1 基因ORF全长cDNA克隆(表达载体), N-Myc 标签||MG51995-NM|
|小鼠 HSP90/HSP90AA1 基因ORF全长cDNA克隆(表达载体), N-HA 标签||MG51995-NY|
|小鼠 HSP90/HSP90AA1 基因ORF全长cDNA克隆(表达载体)||MG51995-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.