Human SerpinI2 HEK293 Overexpression Lysate: Product Information
This Human SerpinI2 overexpression lysate was created in HEK293 Cells and intented for use as a Western blot (WB) positive control. Purification of SerpinI2 protein (Cat: 11008-H08H) from the overexpression lysate was verified.
A DNA sequence encoding the human SERPINI2 (NP_006208.1) (Met 1-Leu 405) was expressed, with a polyhistidine tag at the C-terminus.
The recombinant human SERPINI2 consists of 398 amino acids and predictes a molecular mass of 45.5 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rhSERPINI2 is approximately 45-55 kDa due to glycosylation.
Human SerpinI2 HEK293 Overexpression Lysate: Usage Guide
Cell lysate was prepared by homogenization of the over-expressed cells in ice-cold modified RIPA Lysis Buffer with cocktail of protease inhibitors (Sigma). Cell debris was removed by centrifugation. Protein concentration was determined by Bradford assay (Bio-Rad protein assay, Microplate Standard assay). The cell lysate was boiled for 5 min in 1 x SDS loading buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 5% b-mercaptoethanol, and lyophilized.
1. Centrifuge the tube for a few seconds and ensure the pellet at the bottom of the tube.
2. Re-dissolve the pellet using 200μL pure water and boil for 2-5 min.
1 X Sample Buffer (1 X modified RIPA buffer+1 X SDS loading buffer).
Stability & Storage
Store at 4℃ for up to twelve months from date of receipt. After re-dissolution, aliquot and store at -80℃ for up to twelve months. Avoid repeated freeze-thaw cycles.
Western Blot (WB) Optimal dilutions/concentrations should be determined by the end user.
Human SerpinI2 HEK293 Overexpression Lysate: Alternative Names
Human MEPI Overexpression Lysate; Human PANCPIN Overexpression Lysate; Human PI14 Overexpression Lysate; Human Serpin I2 Overexpression Lysate; Human TSA2004 Overexpression Lysate
SerpinI2 Background Information
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 1 serpins have been identified. Serpin-I2, also known as myoepithelium-derived serine protease inhibitor, Pancreas-specific protein TSA24, Peptidase inhibitor 14, PI14, SERPINI2 and MEPI, is a secreted protein which belongs to theserpin family. It is expressed in pancreas and adipose tissues. SERPINI2 deficiency directly results in the acinar cell apoptosis and malabsorption.
serpin peptidase inhibitor, clade I (pancpin), member 2
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Forsyth, S. et al., 2003, Genomics 81: 336-45.
Horvath, AJ. et al., 2004, J. Mol. Evol. 59: 488-97.
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