|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.
|Rat APOH ORF mammalian expression plasmid, C-GFPSpark tag||RG80701-ACG|
|Rat APOH ORF mammalian expression plasmid, C-OFPSpark / RFP tag||RG80701-ACR|
|Rat APOH ORF mammalian expression plasmid, C-Flag tag||RG80701-CF|
|Rat APOH ORF mammalian expression plasmid, C-His tag||RG80701-CH|
|Rat APOH ORF mammalian expression plasmid, C-Myc tag||RG80701-CM|
|Rat APOH ORF mammalian expression plasmid, C-HA tag||RG80701-CY|
|Rat APOH ORF mammalian expression plasmid, N-Flag tag||RG80701-NF|
|Rat APOH ORF mammalian expression plasmid, N-His tag||RG80701-NH|
|Rat APOH ORF mammalian expression plasmid, N-Myc tag||RG80701-NM|
|Rat APOH ORF mammalian expression plasmid, N-HA tag||RG80701-NY|
|Rat APOH Gene cDNA clone plasmid||RG80701-U|
|Rat APOH natural ORF mammalian expression plasmid||RG80701-UT|
|Learn more about expression Vectors|
Apolipoprotein H (APOH), also known as Beta-2-glycoprotein 1, Activated protein C-binding protein, B2GPI, and B2G1, is a glycoprotein synthesized by liver cells and it is present in the blood associated with plasma lipoproteins. It is an essential cofactor for the binding of certain antiphospholipid antibodies (APA) to anionic phospholipid. APOH binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. APOH may prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells. APOH appears to completely inhibit serotonin release by the platelets and prevents subsequent waves of the ADP-induced aggregation. The activity of APOH appears to involve the binding of agglutenating, negatively charged compounds, and inhibits agglutenation by the contact activation of the intrinsic blood coagulation pathway. APOH causes a reduction of the prothrombinase binding sites on platelets and reduces the activation caused by collagen when thrombin is present at physiological serum concentrations of APOH suggesting a regulatory role of APOH in coagulation. APOH plasma concentrations are strongly associated to metabolic syndrome alterations and vascular disease in type 2 diabetic and could be considered as a clinical marker of cardiovascular risk. APOH is found on several classes of lipoproteins, and is involved in the activation of lipoprotein lipase in lipid metabolism. This single-chain glycoprotein also has been implicated in several physiologic pathways including coagulation and the production of hypertension, which are related to the pathogenesis of primary cerebral hemorrhage (PICH).