Recombinant Mouse Dipeptidyl Peptidase 1 (CTSC) Protein (His&Myc)

Name: Recombinant Mouse Dipeptidyl Peptidase 1 (CTSC) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-00652P
Price: 549.6 USD
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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

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Product Overview

Description	Recombinant Mouse Dipeptidyl Peptidase 1 (CTSC) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P97821
Target Symbol	CTSC
Synonyms	(Cathepsin C)(Cathepsin J)(Dipeptidyl peptidase I)(DPP-I)(DPPI)(Dipeptidyl transferase)(Dipeptidyl peptidase I exclusion domain chain)(Dipeptidyl peptidase I heavy chain)(Dipeptidyl peptidase I light chain)
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	DTPANCTYPDLLGTWVFQVGPRSSRSDINCSVMEATEEKVVVHLKKLDTAYDELGNSGHFTLIYNQGFEIVLNDYKWFAFFKYEVRGHTAISYCHETMTGWVHDVLGRNW
Expression Range	25-134aa
Protein Length	Partial
Mol. Weight	20.1 kDa
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	Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase. Can degrade glucagon. Plays a role in the generation of cytotoxic lymphocyte effector function.
Subcellular Location	Lysosome.
Protein Families	Peptidase C1 family
Database References	KEGG: mmu:13032 STRING: 10090.ENSMUSP00000032779 UniGene: Mm.322945
Tissue Specificity	Broadly distributed, but higher levels found in lung, liver, kidney and spleen. Lower levels found in testis and brain.

Gene Functions References

Neutrophilic Cathepsin C Is Maturated by a Multistep Proteolytic Process and Secreted by Activated Cells during Inflammatory Lung Diseases. PMID: 26884336
A proteolytic cascade, involving cathepsins C and D, controls LLOMe-mediated necrosis. PMID: 25830414
CatC has a role in the selective tuning of innate and adaptive immune responses, relevant to a chronic immune disease, such as atherosclerosis. PMID: 25395616
Data indicate that all-trans retinoic acid (ATRA), which induces miR-23a expression, decreases cathepsin C (CTSC) expression and granzyme B activity leading to impaired NK cell cytotoxicity. PMID: 24440757
These results establish that DPPI is a major determinant of survival following Klebsiella pneumoniae lung infection and suggest that the survival disadvantage in DPPI(+/+) mice is in part due to processing of surfactant protein D by DPPI. PMID: 24955853
found no significant role for CtsC during mammary carcinogenesis but revealed squamous carcinogenesis to be functionally dependent on CtsC PMID: 24065739
Late stage cathepsin C, CXCL13 and Ki-67 overexpression correlate with regional neuropathology in a bovine spongiform encephalopathy transgenic murine model. PMID: 22789860
Proinflammatory cytokines induce expression and release of cathepsin C in microglial cells during neuroinflammatory progression. PMID: 22607609
The production of IL-1beta by macrophages, neutrophils, and mast cells in vitro is dependent on caspase-1 but not on cathepsin C. PMID: 22914048
NADPH oxidase in antimicrobial host defense against A. fumigatus and B. cepacia, whereas the proteases neutrophil elastase, cathepsin G, and lysosomal cysteine protease cathepsin C/ dipeptidyl peptidase I are dispensable PMID: 22163282
CatC is involved in limiting MCMV replication; however, this effect is independent of its role in promoting effector cytolytic activity. PMID: 20975734
Results indicate that mast cell dipeptidyl peptidase I (DPPI) harms the septic host and that DPPI is a novel potential therapeutic target for treatment of sepsis. PMID: 14966572
DPPI regulates a critical step in the development of collagen-induced arthritis that is independent of T cell and B cell functions. PMID: 16059912
Overall, our results indicate that although cathepsin C clearly generates the majority of granzyme B activity, some is still generated in its absence, pointing to alternative mechanisms for granzyme B processing and activation. PMID: 17283185
These findings suggest that DPPI and/or granule-associated serine proteases are necessary for neutrophil recruitment into the diseased aorta and that these proteases act to amplify vascular wall inflammation that leads to abdominal aortic aneurysms. PMID: 17301245
Role of DPPI and TIMP-3 in development of pulmonary fibrosis in early inflammation following bleomycin instillation. PMID: 17673693
DPPI is involved in recruitment of neutrophils following respiratory viral infection; absence of neutrophil-derived DPPI diminishes the acute inflammatory response and mucous cell metaplasia of the chronic asthma that follows Sendai virus infection. PMID: 18292580
Results indicate that DPPI cannot functionally compensate for the loss of TPPI. PMID: 18570628
Examination of mature enamel from DPPI null mice by FTIR showed no significant accumulation of protein; however, microhardness testing revealed that loss of DPPI expression significantly reduced enamel hardness. PMID: 19407151

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.