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. Mouse Serpin A11, also known as SERPINA11, is a member of the serpin family.
Pack Size | Availability | Price/USD | Quantity |
---|---|---|---|
100 μg | 5 days | $ 600.00 |
Description | 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. Mouse Serpin A11, also known as SERPINA11, is a member of the serpin family. |
Species | Mouse |
Expression System | HEK293 |
Tag | His |
Accession Number | E9QLL8 |
Synonyms | serpin peptidase inhibitor, clade A (α-1 antiproteinase, antitrypsin), member 11, serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 11, Gm895 |
Construction | A DNA sequence encoding the mouse SERPINA11 isoform 1 (NP_955018.2) (Met 1-Gly 424) was expressed, fused with a polyhistidine tag at the C-terminus. |
Protein Purity | > 94 % as determined by SDS-PAGE |
Molecular Weight | Approxiamtely 46.2 kDa |
Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method |
Formulation | Lyophilized from sterile PBS, pH 7.4. Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0. 01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA. |
Reconstitution | A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information. |
Stability & Storage |
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles. |
Shipping |
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise. |
Research 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 1 serpins have been identified. Mouse Serpin A11, also known as SERPINA11, is a member of the serpin family. |
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Please read the User Guide of Recombinant Proteins for more specific information.
Serpin A11 Protein, Mouse, Recombinant (His) serpin peptidase inhibitor, clade A (α-1 antiproteinase, antitrypsin), member 11 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 11 Gm895 recombinant recombinant-proteins proteins protein