| 説明 |
Serpins are the largest and most diverse family of serine protease inhibitors which are involved in some fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression and are expressed in a cell-specific manner.SerpinB2, also known as Plasminogen activator inhibitor 2, Placental plasminogen activator inhibitor, Monocyte Arg-serpin, Urokinase inhibitor and PAI2, is a cytoplasm protein that belongs to the serpin family and Ov-serpin subfamily. SerpinB2 is a major product of activated monocytes and macrophages and is substantially induced during most inflammatory processes. Distinct from its widely described extracellular role as an inhibitor of urokinase plasminogen activator. SerpinB2 has been shown to have an intracellular role as a retinoblastoma protein (Rb)-binding protein that inhibits Rb degradation. SerpinB2 is widely described as an inhibitor of urokinase plasminogen activator. SerpinB2 inhibits urokinase-type plasminogen activator. The monocyte derived SerpinB2 is distinct from the endothelial cell-derived PAI-1. SerpinB2 is a potentially important inducible host factor that significantly promotes HIV-1 replication. |
| Species |
Human
|
| Expression Host |
Baculovirus Insect Cells
|
| Tag |
GST
|
| Accession Number |
P05120
|
| 別名 |
PAI, serpin peptidase inhibitor, clade B (ovalbumin), member 2, Serpin B2, PLANH2, PAI-2, HsT1201, PAI2
|
| Construction |
The full length of Human SERPINB2 (NP_002566.1) (Met 1-Pro 415) was fused with the GST tag at the N-terminus.
|
| Protein Purity |
≥ 90 % as determined by SDS-PAGE
|
| 分子量 |
73 kDa (predicted)
|
| Endotoxin |
< 1.0 EU/μg of the protein as determined by the LAL method.
|
| Formulation |
Lyophilized from a solution filtered through a 0.22 μm filter, containing 50 mM Tris, 100 mM NaCl, pH 8.0, 0.5 mM Reduced Glutathione, 10% glycerol, 0.5 mM PMSF. Typically, a mixture containing 5% to 8% trehalose, mannitol, and 0.01% Tween 80 is incorporated as a protective agent before lyophilization.
|
| Reconstitution |
A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information.
|
| Stability & Storage |
It is recommended to store recombinant proteins at -20°C to -80°C for future use. Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at-80℃. For reconstituted proteinsolutions, the solution can be stored at -20°c to -80'c for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
|
| Shipping |
In general, Lyophilized powders are shipping with blue ice.
|
| Research Background |
Serpins are the largest and most diverse family of serine protease inhibitors which are involved in some fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression and are expressed in a cell-specific manner.SerpinB2, also known as Plasminogen activator inhibitor 2, Placental plasminogen activator inhibitor, Monocyte Arg-serpin, Urokinase inhibitor and PAI2, is a cytoplasm protein that belongs to the serpin family and Ov-serpin subfamily. SerpinB2 is a major product of activated monocytes and macrophages and is substantially induced during most inflammatory processes. Distinct from its widely described extracellular role as an inhibitor of urokinase plasminogen activator. SerpinB2 has been shown to have an intracellular role as a retinoblastoma protein (Rb)-binding protein that inhibits Rb degradation. SerpinB2 is widely described as an inhibitor of urokinase plasminogen activator. SerpinB2 inhibits urokinase-type plasminogen activator. The monocyte derived SerpinB2 is distinct from the endothelial cell-derived PAI-1. SerpinB2 is a potentially important inducible host factor that significantly promotes HIV-1 replication.
|
参考文献
1.
Sumi, Y. et al., 1989, J. Biochem. 106: 703-7.
2.
Rawlings, N.D. et al., 2004, Biochem J. 378: 705-16.
3.
Gillard, A. et al., 2006, Am J Nephrol. 26 (1): 34-42.
4.
Schroder,WA. et al., 2010, J Immunol. 184 (5): 2663-70.
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