Recombinant Mouse Serpin G1 Protein (C-6His)

Name: Recombinant Mouse Serpin G1 Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-0943NP
Availability: InStock

BL-0943NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Mouse Serine Protease Inhibitor-clade G1 is produced by our Mammalian expression system and the target gene encoding Ala20-Gly504 is expressed with a 6His tag at the C-terminus.
Accession	P97290
Synonym	SERPIN G1;Plasma protease C1 inhibitor;C1 Inh;C1 esterase inhibitor;C1-inhibiting factor;Serping1;C1nh
Gene Background	SERPIN G1 is a member of the serpin family, The C-terminal serpin domain is similar to other serpins, and this part of C1-INH provides the inhibitory activity. SERPIN G1 is involved in the inhibition of the complement system to prevent spontaneous activation. SERPIN G1 may play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. SERPIN G1 prevents the proteolytic cleavage of later complement components C4 and C2 by C1 and MBL. SERPIN G1 is a very efficient physiological inhibitor of FXIIa, plasma kallikrein and fXIa, and could inhibit chymotrypsin and kallikrein. It forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases in the C1 complex of classical pathway of complement. Activation of the C1 complex is under control of the C1-inhibitor.
Molecular Mass	54.6 KDa
Apmol Mass	90 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, pH 8.0.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Activation of the C1 complex is under control of the C1-inhibitor. It forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases. May play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. Very efficient inhibitor of FXIIa. May inhibit chymotrypsin and kallikrein.
Subcellular Location	Secreted.
Protein Families	Serpin family
Database References	KEGG: mmu:12258 STRING: 10090.ENSMUSP00000023994 UniGene: Mm.38888

Gene Functions References

C1INH prevented myocardial ischemia reperfusion injury in mice. PMID: 22705194
Transgenic mice have been generated that express human C1 inhibitor mRNA and protein under the control of the human promoter and regulatory elements; C1nh production is demonstrated in mouse brain, spleen, liver, heart, kidney, and lung. PMID: 12421980
In vivo, C1 inhibitor (C1INH) reduces the number of viable bacteria in the blood and peritoneal fluid and accelerates killing of bacteria by blood neutrophils and peritoneal macrophages. PMID: 17785834
C1-inhibitor limits neointimal plaque formation and inflammation. This may involve blockade of complement activation, inhibition of leukocyte recruitment, and reduced triglyceride levels PMID: 18071075
In addition to the protective activities mediated via inhibition of the complement system, these studies indicate that C1INH also plays a direct role in suppression of leukocyte transmigration into reperfused tissue. PMID: 18787060

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.