Recombinant Mouse Cathepsin G (CTSG) Protein (His-SUMO)

Name: Recombinant Mouse Cathepsin G (CTSG) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09790P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) Ctsg.

Collections: Enzymes, Featured enzyme molecules, Protease, Recombinant proteins

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Product Overview

Description	Recombinant Mouse Cathepsin G (CTSG) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P28293
Target Symbol	CTSG
Synonyms	Ctsg; Cathepsin G; EC 3.4.21.20; Vimentin-specific protease; VSP
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	IIGGREARPHSYPYMAFLLIQSPEGLSACGGFLVREDFVLTAAHCLGSSINVTLGAHNIQMRERTQQLITVLRAIRHPDYNPQNIRNDIMLLQLRRRARRSGSVKPVALPQASKKLQPGDLCTVAGWGRVSQSRGTNVLQEVQLRVQMDQMCANRFQFYNSQTQICVGNPRERKSAFRGDSGGPLVCSNVAQGIVSYGSNNGNPPAVFTKIQSFMPWIKRTMRRFAPRYQRPANSLSQAQT
Expression Range	21-261aa
Protein Length	Full Length of Mature Protein
Mol. Weight	42.9kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Serine protease with trypsin- and chymotrypsin-like specificity. Cleaves complement C3. Cleaves vimentin. Has antibacterial activity against the Gram-negative bacterium P.aeruginosa.
Subcellular Location	Cell surface. Membrane; Peripheral membrane protein.
Protein Families	Peptidase S1 family
Database References	KEGG: mmu:13035 STRING: 10090.ENSMUSP00000015583 UniGene: Mm.4858
Tissue Specificity	In adult, detected only in bone marrow where expression is restricted to a small population of early myeloid cells.

Gene Functions References

these findings present evidence of an arterial-specific recruitment pattern centered on CatG-instructed adhesion strengthening. The inhibition of this process could provide a novel strategy for treatment of arterial inflammation with limited side effects. PMID: 27660294
Cathepsin G activity may impair efferocytosis, which could lead to an accumulation of lesion-associated apoptotic cells and the accelerated progression of early atherosclerotic lesions to more complex lesions in Apoe(-/-) mice. PMID: 23934850
SerpinB1 is critical for maintaining polymorphonuclear neutrophils survival by antagonizing intracellular cathepsin G activity. PMID: 23532733
Cathepsin G-regulated release of formyl peptide receptor agonists modulate neutrophil effector functions. PMID: 22879591
Cathepsin G and neutrophil elastase contribute to lung-protective immunity against mycobacterial infections in mice. PMID: 22461690
This is the first study showing a contribution of neutrophil-derived neutral serine proteases CG and NE to lung-protective immunity against focal pneumonia-inducing serotype 19 S. pneumoniae in mice. PMID: 21911460
In the absence of a pathogen challenge, neutrophil-derived proteases and nucleosomes contribute to large vessels thrombosis, the main trigger of myocardial infarction and stroke. PMID: 20676107
Inhibition of TGF-beta significantly reduces microvessel density in mammary tumor-induced bone lesions, mediated by decreased expression of both vascular endothelial growth factor (VEGF) and monocyte chemotactic protein (MCP)-1. PMID: 19646811
neutrophil elastase and cathepsin G are inhibited by PAI-1 mutants PMID: 15131125
cathepsin G activity at the tumor-bone interface plays an important role in mammary tumor-induced osteolysis through RANKL PMID: 18632634
both Cat-G and PAR(4) play key roles in generating and/or amplifying relapses in ulcerative colitis PMID: 19528350
Cathepsin G and MMP9 were identified as proteases involved in enhanced TGF-beta signaling at the tumor-bone interface of mammary tumor-induced osteolytic lesions. PMID: 19671689
Serine protease required for resistance to microbial infection; contributes to pathogenessis in endotoxic shock PMID: 10714686

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.