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Mouse SerpinB10 Protein (His Tag)

9830131G07,BB233602,Serpinb10-ps

Catalog Number P50626-M08B
Organism Species Mouse
Host Baculovirus-Insect Cells
Synonyms 9830131G07,BB233602,Serpinb10-ps
Molecular Weight The recombinant mouse SERPINB10 consists of 408 amino acids and has a calculated molecular mass of 46.5 kDa. It migrates as an approximately 44 kDa band in SDS-PAGE under reducing conditions.
predicted N Met
SDS-PAGE
Purity > 94 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the mouse SERPINB10 (Q8K1K6-1) (Met 1-Pro 397) was expressed, with a C-terminal polyhistidine tag.
Bio-activity
Research Area Immunology |Inflammation / Inflammatory Mediator |Plasma Cascade Systems in Inflammation |Fibrinolysis System
Formulation Lyophilized from sterile 50mM Tris, 100mM NaCl, pH 8.0
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background Serpins are the largest and most diverse family of serine protease inhibitors which are involved in a number of fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression and are expressed in a cell-specific manner. Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. The acronym serpin was originally coined because many serpins inhibit chymotrypsin-like serine proteases (serine protease inhibitors). Over 1000 serpins have been identified.
Mouse SerpinB10, also known as Peptidase inhibitor 10, PI-10, Bomapin and SERPINB10, is a nucleus and cytoplasm protein which belongs to the serpin family and Ov-serpin subfamily. SerpinB10 is expressed specifically in the bone marrow. SerpinB10 is a protease inhibitor that may play a role in the regulation of protease activities during hematopoiesis and apoptosis induced by TNF. SerpinB10 is a redox-sensitive nuclear serpin that augments proliferation or apoptosis of leukaemia cells, depending on growth factors availability. SerpinB10 may regulate protease activities in the cytoplasm and in the nucleus.
Reference
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  • Forsyth, S. et al., 2003, Genomics 81: 336-45. 
  • Horvath, AJ. et al., 2004, J. Mol. Evol. 59: 488-97.
  • Steenbakkers PJ. et al., 2008, Mycol. Res. 112 (Pt 8): 999-1006.
  • Przygodzka, P. et al., 2010, BMC Cell Biol. 11: 30.