Product Catalog


SERPING1 Protein (His Tag)
| Catalog | Size (Price) | Quantity | In Stock | Operation | Other Information |
| 10995-H08H |
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YES |
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Plasma Protease C1 Inhibitor ( SERPING1 / C1IN ) Protein
SERPING1 / C1IN Protein Price Inquiry ( Available Sizes )
SERPING1 / C1IN Protein Product Information
| Synonym: |
C1IN, C1INH, C1NH, HAE1, HAE2, SERPING1 |
| Protein Construction: |
A DNA sequence encoding the human SERPING1 (NP_000053.2) precursor (Met 1-Ala 500) was expressed with a polyhistidine tag at the C-terminus. |
| Source: | Human |
| Expression Host: | Human Cells |
SERPING1 / C1IN Protein QC Testing
| Purity: |
> 95 % as determined by SDS-PAGE. |
SDS-PAGE:![]() SERPING1 protein |
| Endotoxin: | < 1.0 EU per μg of the protein as determined by the LAL method. | |
| Stability: | Samples are stable for up to twelve months from date of receipt at -70℃ | |
| Predicted N terminal: | Asn 23 | |
| Molecular Mass: |
The secreted recombinant human SERPING1 consists of 489 amino acids and predictes a molecular mass of 54.3 kDa. In SDS-PAGE under reducing conditions, it migrates with the apparent molecular mass of 110 kDa due to glycosylation. |
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| Formulation: |
Lyophilized from sterile PBS, pH 7.4 |
SERPING1 / C1IN Protein Usage Guide
| Storage: |
Store it under sterile conditions at -70℃ upon receiving. Recommend to aliquot the protein into smaller quantities for optimal storage. Avoid repeated freeze-thaw cycles. |
| Reconstitution: | A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information. |
SERPING1 / C1IN Protein Related Products & Topics
Related Areas:
Enzyme>>Protease & Regulator>>Serine Protease & Regulator>>Serpin Superfamily>>C1 inhibitor/SerpinG1
Immunology>>Innate Immunity>>Complement System>>C1 inhibitor/SerpinG1
Proteins:
| Molecule | Species | Description //For Detailed Info. and Price------CLICK! | Cat. No |
| C1 inhibitor/SerpinG1 | Human | C1 inhibitor/SerpinG1 Protein, Recombinant | 10995-H08H |
Antibodies:
| Molecule | Application | Description //For Detailed Info. and Price------CLICK! | Cat. No |
| Human C1 inhibitor/SerpinG1 |
WB, ELISA | Mouse Monoclonal Antibody | 10995-MM03 |
| Human C1 inhibitor/SerpinG1 |
WB, ELISA | C1 inhibitor/SerpinG1 Antibody, Rabbit MAb | 10995-R018 |
| Human C1 inhibitor/SerpinG1 |
WB, ELISA | Rabbit Polyclonal Antibody | 10995-RP01 |
| Human C1 inhibitor/SerpinG1 |
WB, ELISA | Rabbit Polyclonal Antibody (Antigen Affinity Purified) | 10995-RP02 |
SERPING1 / C1IN Protein Description
Plasma protease C1 inhibitor, also known as C1-inhibiting factor, C1-INH, C1 esterase inhibitor, SERPING1 and C1IN, is a serine protease inhibitor protein. C1-INH is the largest member among the serpin class of proteins. Remarkably, C1-INH has a 2-domain structure, unlike most family members. The C-terminal serpin domain is similar to other serpins, and this part of C1-INH provides the inhibitory activity. The N-terminal domain is not essential for C1-INH to inhibit proteinases and has no similarity to other proteins. The main function of C1-INH is the inhibition of the complement system to prevent spontaneous activation. C1-INH is an acute phase protein and circulates in blood at levels of around 0.25 g/L, whose levels rise 2-fold during inflammation. C1-INH irreversibly binds to and inactivates C1r and C1s proteinases in the C1 complex of classical pathway of complement. C1-INH prevents the proteolytic cleavage of later complement components C4 and C2 by C1 and MBL. Although named after its complement inhibitory activity, C1-INH also inhibits proteinases of the fibrinolytic, clotting, and kinin pathways. Most notably, C1-INH is the most important physiological inhibitor of plasma kallikrein, fXIa and fXIIa.
References
- Theriault, A. et al., 1990, Hum. Genet. 84 (5): 477-9.
- Davis, AE. et al., 2004, Drug News Perspect. 17 (7): 439-46.
- Koles, K. et al., 2004, Glycobiology. 14 (1): 51-64.
- Cicardi, M. et al., 2005, Springer Semin. Immunopathol. 27(3): 286-98.
- Bernstein, JA. et al., 2008, Ann. Allergy Asthma Immunol.100: S41-6.
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