|Datasheet||Specific References||Reviews||Related Products||Protocols|
|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.
|Human SPARC ORF mammalian expression plasmid, C-GFPSpark tag||HG10929-ACG|
|Human SPARC ORF mammalian expression plasmid, C-OFPSpark / RFP tag||HG10929-ACR|
|Human SPARC ORF mammalian expression plasmid, C-Flag tag||HG10929-CF|
|Human SPARC ORF mammalian expression plasmid, C-His tag||HG10929-CH|
|Human SPARC ORF mammalian expression plasmid, C-Myc tag||HG10929-CM|
|Human SPARC ORF mammalian expression plasmid, C-HA tag||HG10929-CY|
|Human SPARC Gene cDNA clone plasmid||HG10929-M|
|Human SPARC ORF mammalian expression plasmid, N-Flag tag||HG10929-NF|
|Human SPARC ORF mammalian expression plasmid, N-His tag||HG10929-NH|
|Human SPARC ORF mammalian expression plasmid, N-Myc tag||HG10929-NM|
|Human SPARC ORF mammalian expression plasmid, N-HA tag||HG10929-NY|
|Human SPARC natural ORF mammalian expression plasmid||HG10929-UT|
|Learn more about expression Vectors|
Secreted protein acidic and rich in cysteine (SPARC), also known as Osteonectin (ON), is a member of the SPARC family. SPARC consists of three domains: a EF-hand domain, a follistatin-like domain and a Kazal-like domain, and each of which has independent activity and unique properties. The activity of SPARC is context- and cell-type-dependent, which is highlighted by the fact that SPARC has shown seemingly contradictory effects on tumor progression in both clinical correlative studies and in animal models. The location of SPARC in the nuclear matrix of certain proliferating cells, but only in the cytosol of postmitotic neurons, indicates potential functions of SPARC as a nuclear protein, which might be involved in the regulation of cell cycle progression and mitosis. It functions not only to modulate cell-cell and cell-matrix interactions, but its de-adhesive and growth inhibitory properties in non-transformed cells have led to studies to assess its role in cancer. Its divergent actions reflect the complexity of this protein, because in certain types of cancers, such as melanomas and gliomas, SPARC is associated with a highly aggressive tumor phenotype, while in others, mainly ovarian, neuroblastomas and colorectal cancers, SPARC may function as a tumor suppressor. Recent studies have also demonstrated a role for SPARC in sensitizing therapy-resistant cancers. Notably, SPARC is linked to human obesity.