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> Antibody > Rabbit PAb Antibody > SERPINA3C / Serpina3c Antibody (Antigen Affinity Purified) SERPINA3C / Serpina3c Antibody (Antigen Affinity Purified)
| Catalog | Size (Price) | Quantity | In Stock | Operation | Other Information |
| 50375-RP02 |
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YES |
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Mouse Serine Protease Inhibitor A3C Antibody (Antigen Affinity Purified)
| Order or Inquire for Serpina3c Antibody product | ![]() |
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| Detection limit is 0.5 ng/lane in WB | |||
| Detection limit is 0.00245 ng/well in ELISA |
SERPINA3C / Serpina3c Antibody Product Information
| Immunogen : |
Recombinant mouse Serpina3c protein ( Catalog#50375-M08H ) |
| Antibody Type : | Rabbit Polyclonal Antibody ( Antibody Purification Platform ) |
| Ig Type : |
Rabbit IgG |
| Formulation : | 0.2 μm filtered solution in PBS with 5% trehalose |
| Preparation : |
Produced in rabbits immunized with purified, human cell-derived, recombinant mouse SERPINA3C extracellular domain ( rM Serpina3c ; Catalog#50375-M08H ; NP_032484.1 ; Met 1 - Ala 417 ). Total IgG was purified by Protein A affinity chromatography. |
SERPINA3C / Serpina3c Antibody Usage Guide
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Specificity : |
Mouse SERPINA3C / Serpina3c |
| Western blot : | This antibody can be used at 0.1 - 0.2 μg/mL with the appropriate secondary reagents to detect mouse SERPINA3C in WB. Using a DAB detection system, the detection limit for mouse SERPINA3C is approximately 0.5 ng/lane under non-reducing conditions and reducing conditions |
| Direct ELISA : | This antibody can be used at 0.5 - 1 μg/mL with the appropriate secondary reagents to detect mouse SERPINA3C. The detection limit for mouse SERPINA3C is approximately 0.00245 ng/well |
| Storage : | This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -70℃. Preservative-Free. Sodium azide is recommended to avoid contamination (final concentration 0.05%-0.1%). It is toxic to cells and should be disposed of properly. Avoid repeated freeze-thaw cycles. |
SERPINA3C / Serpina3c Antibody Related Products & Topics
Related Areas:
Enzyme>>Protease & Regulator>>Serine Protease & Regulator>>Serpin Superfamily>>Serpina3c
Proteins:
| Molecule | Species | Description //For Detailed Info. and Price------CLICK! | Cat. No |
| Serpina3c | Mouse | Serpina3c Protein, Recombinant | 50375-M08H |
Antibodies:
| Molecule | Application | Description //For Detailed Info. and Price------CLICK! | Cat. No |
| Mouse Serpina3c |
WB, ELISA | Rabbit Polyclonal Antibody | 50375-RP01 |
| Mouse Serpina3c |
WB, ELISA | Rabbit Polyclonal Antibody (Antigen Affinity Purified) | 50375-RP02 |
SERPINA3C / Serpina3c Antibody 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. Serine protease inhibitor A3C, also known as Kallikrein-binding protein, KBP, and Serpina3c, is a secreted protein which belongs to the serpin family. The reactive center loop (RCL) extends out from the body of the Serpina3c protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the serpin reactive site and the protease. The resulting inactive serpin-protease complex is highly stable. Variability within the reactive center loop (RCL) sequences of Serpina3 paralogs may determine target protease specificity.
References
- Irving JA. et al., 2000, Genome Res. 10: 1845-64.
- Irving J. et al., 2002, Mol Biol Evol 19 (11): 1881-90.
- Forsyth, S. et al., 2003, Genomics 81: 336-345.
- Horvath, AJ. et al., 2004, J. Mol. Evol. 59: 488-497.
- Steenbakkers PJ. et al., 2008, Mycol. Res. 112 (Pt 8): 999-1006.
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