|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.
|人 S100A16 基因全長cDNA ORF克隆 (表達載體), C-GFPSpark 標籤||HG11137-ACG|
|人 S100A16 基因全長cDNA ORF克隆 (表達載體), C-OFPSpark 標籤||HG11137-ACR|
|人 S100A16 基因全長cDNA ORF克隆 (表達載體), N-GFPSpark 標籤||HG11137-ANG|
|人 S100A16 基因全長cDNA ORF克隆 (表達載體), N-OFPSpark 標籤||HG11137-ANR|
|人 S100A16 基因全長cDNA ORF克隆 (表達載體), C-Flag 標籤||HG11137-CF|
|人 S100A16 基因全長cDNA ORF克隆 (表達載體), C-His 標籤||HG11137-CH|
|人 S100A16 基因全長cDNA ORF克隆 (表達載體), C-Myc 標籤||HG11137-CM|
|人 S100A16 基因全長cDNA ORF克隆 (表達載體), C-HA 標籤||HG11137-CY|
|人 S100A16 基因全長cDNA ORF(克隆載體)||HG11137-M|
|人 S100A16 基因全長cDNA ORF克隆 (表達載體), C-Flag 標籤||HG11137-M-F|
|人 S100A16 基因全長cDNA ORF克隆 (表達載體), N-Flag 標籤||HG11137-NF|
|人 S100A16 基因全長cDNA ORF克隆 (表達載體), N-His 標籤||HG11137-NH|
|人 S100A16 基因全長cDNA ORF克隆 (表達載體), N-Myc 標籤||HG11137-NM|
|人 S100A16 基因全長cDNA ORF克隆 (表達載體), N-HA 標籤||HG11137-NY|
|人 S100A16 基因全長cDNA ORF克隆 (表達載體)||HG11137-UT|
S100A16 is a member of S100 protein super family that carries calcium-binding EF-hand motifs. S100 proteins are cell- and tissue-specific and are involved in many intra- and extracellular processes through interacting with specific target proteins. S100A16 expression was found to be astrocyte-specific. The S100A16 protein was found to accumulate within nucleoli and to translocate to the cytoplasm in response to Ca(2+) stimulation. The homodimeric structure of human S100A16 in the apo state has been obtained both in the solid state and in solution, resulting in good agreement between the structures with the exception of two loop regions. The homodimeric solution structure of human S100A16 was also calculated in the calcium(II)-bound form. Differently from most S100 proteins, the conformational rearrangement upon calcium binding is minor. Immunoprecipitation analysis revealed that S100A16 could physically interact with tumor suppressor protein p53, also a known inhibitor of adipogenesis. Overexpression or RNA interference-initiated reduction of S100A16 led to the inhibition or activation of the expression of p53-responsive genes, respectively. S100A16 protein is a novel adipogenesis-promoting factor.