Recombinant Mouse Cathepsin K (CTSK) Protein (His)

Beta LifeScience SKU/CAT #: BLC-04411P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Mouse Cathepsin K (CTSK) Protein (His)

Beta LifeScience SKU/CAT #: BLC-04411P
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Product Overview

Description Recombinant Mouse Cathepsin K (CTSK) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P55097
Target Symbol CTSK
Synonyms Ctsk; Cathepsin K; EC 3.4.22.38
Species Mus musculus (Mouse)
Expression System E.coli
Tag N-6His
Target Protein Sequence VPDSIDYRKKGYVTPVKNQGQCGSCWAFSSAGALEGQLKKKTGKLLALSPQNLVDCVTENYGCGGGYMTTAFQYVQQNGGIDSEDAYPYVGQDESCMYNATAKAAKCRGYREIPVGNEKALKRAVARVGPISVSIDASLASFQFYSRGVYYDENCDRDNVNHAVLVVGYGTQKGSKHWIIKNSWGESWGNKGYALLARNKNNACGITNMASFPKM
Expression Range 115-329aa
Protein Length Full Length of Mature Protein
Mol. Weight 27.4kDa
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 involved in osteoclastic bone resorption. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation. Involved in the release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen.
Subcellular Location Lysosome. Secreted. Apical cell membrane; Peripheral membrane protein; Extracellular side.
Protein Families Peptidase C1 family
Database References
Tissue Specificity Predominantly expressed in bones. Expressed in thyroid epithelial cells.

Gene Functions References

  1. these data indicate that CatK not only plays a major role in bone remodeling but also modulates modeling-based cortical bone formation by degrading periostin and thereby moderating Wnt-beta-catenin signaling. PMID: 28322464
  2. This study established a possible role of CatK in TLR7 proteolytic activation, Treg immunosuppressive activity, and lupus autoimmunity and pathology. PMID: 28093526
  3. catK deficiency almost completely blunted the increased vascular remodeling response of apoE-/- mice to flow cessation, possibly by correcting hyperlipidemia-associated pro-inflammatory effects on the peripheral immune response PMID: 27636705
  4. Cathepsin K expression is increased in the bone of a diabetic mouse model. PMID: 26892148
  5. Data suggest Ctsk gene, key gene upregulated during osteoclast differentiation, is transcriptionally activated during cell hypoxia-induced mitochondrial dysfunction/disruption; hnRNPA2 (heterogeneous ribonucleoprotein A2) is coactivator in this process. PMID: 25800988
  6. cathepsin K knockout attenuates age-related decline in cardiac function via suppressing caspase-dependent and caspase-independent apoptosis PMID: 25692548
  7. Data (including data from studies in knockout/transgenic mice) suggest that Ctsk is involved in inflammatory response and bone resorption in both rheumatoid arthritis and periodontitis; thus, Ctsk appears to play a role in osteoimmune responses. PMID: 25896020
  8. In a mouse model of post-traumatic osteoarthritis, cathepsin K activity was significantly increased in injured knees relative to uninjured knees. PMID: 25278057
  9. Gene deletion of cathepsin K in mice accelerated callus size resolution, significantly increased callus mineralized mass, and improved mechanical strength as compared to wild type mice. PMID: 24928497
  10. synergism between HIV proteins and pro-atherogenic shear stress to increase endothelial cell expression of the powerful protease cathepsin K PMID: 24719048
  11. in addition to its other effects, the absence of CatK in OCP limits their ability to engraft in a repairing fracture callus compared to WT OCP. PMID: 24590570
  12. Cardiac mammalian target of rapamycin and extracellular signal-regulated kinases (ERK) signaling cascades were upregulated by pressure overload, the effects of which were attenuated by cathepsin K knockout. PMID: 23529168
  13. The localization pattern of the intercellular junction proteins E-cadherin and occludin was altered in the colon of Ctsk-/- mice, suggesting potential impairment of the barrier function. PMID: 23152408
  14. Targeted ablation of Ctsk in hematopoietic cells, or specifically in osteoclasts and cells of the monocyte-osteoclast lineage, resulted in increased bone volume and bone formation rate as well as osteoclast and osteoblast numbers. PMID: 23321671
  15. cathepsin K contributes to the development of obesity-associated cardiac hypertrophy and may represent a potential target for the treatment to obesity-associated cardiac anomalies. PMID: 23069627
  16. cathepsin K exocytosis is controlled by PKCdelta through modulation of the actin bundling protein myristoylated alanine-rich C-kinase substrate. PMID: 22806935
  17. results raise significant concerns regarding in vivo bone phenotypes created using Ctsk(Cre/+) mice and warrant further investigation into the role of Cathepsin K in gametes as well as alternative tools for studying osteoclast-specific gene loss in vivo PMID: 22860046
  18. CTK plays crucial direct roles in the early to intermediate stage of osteoarthritis development. CTK-positive chondrocytes and synovial cells may be a possible target to prevent disease progression in osteoarthritis. PMID: 21968827
  19. This study demonstrates that curcumin increases the expression of cathepsins K and L in lung which an effect on lung fibroblast cell behavior. PMID: 22126332
  20. We propose that cathepsin K activity has an important impact on the development and maintenance of the CNS in mice PMID: 21794126
  21. variants of ENaC subunits may contribute to the variation of BP response to dietary sodium intake PMID: 21721952
  22. CatK plays an essential role in abdominal aortic aneurysm formation by promoting T-cell proliferation, vascular SMC apoptosis, and elastin degradation and by affecting vascular cell protease expression and activities. PMID: 21817099
  23. BK channel controls resorptive osteoclast activity by regulating Cathepsin K release PMID: 21695131
  24. Airway development is partly regulated by cathepsin K expression contributes to lung development the maintenance of the airway structural integrity via an interaction with TGF-beta1. PMID: 21627832
  25. Cathepsin K deficiency affected mostly the occurrence and composition of lung granulomas in a murine model of sarcoidosis. PMID: 21251246
  26. the levels of cathepsin K and MMP-9 increase in the conditioned medium from IL-17A-treated cells PMID: 20937352
  27. while catK deficiency has major impact on various vasculopathies, it did not affect murine aneurysm formation. PMID: 19775691
  28. Data indicate that cathepsin K ablation in mice results in reduced body fat content under conditions requiring a rapid accumulation of fat stores. PMID: 17668061
  29. Results suggest that the accumulation of glycosaminoglycans in murine mucopolysaccharidosis I bone has an inhibitory effect on cathepsin K activity, resulting in impaired osteoclast activity and decreased cartilage resorption. PMID: 19834056
  30. Cathepsin K-deficient osteoclasts are fully differentiated and are capable of degrading the organic phase of alveolar bone during tooth formation and eruption in CK-/- knockout mice. PMID: 12719657
  31. cathepsin K has a role in utilization of luminal thyroglobulin for thyroxine liberation PMID: 12782676
  32. Cathepsin K plays a pivotal role in lung matrix homeostasis under physiological and pathological conditions. PMID: 15161653
  33. Altogether, these data suggest that while Cat K may contribute to control lung fibrosis, TGF-beta appears to limit its overexpression in response to silica particles PMID: 16045809
  34. overexpression of the cathepsin K gene under its own promoter in transgenic mice makes them susceptible to progressive synovitis PMID: 16329095
  35. Scavenger receptor-mediated uptake (particularly by CD36) of modified LDL increased in the absence of catK, resulting in an increased macrophage size because of increased cellular storage of cholesterol esters, thereby enlarging the lysosomes PMID: 16365196
  36. CatK-deficient mice were generated by targeted disruption of the Ctsk gene and compared their bone structural and mechanical properties with wildtype (WT) controls. PMID: 16753017
  37. Cathepsin K is a mechanosensitive, extracellular matrix protease that may be involved in arterial wall remodeling and atherosclerosis. PMID: 17098827
  38. cathepsin K plays a key role in osteoclasts apoptosis and senescence, revealing the importance of osteoclasts senescence in bone homeostasis. PMID: 17210673
  39. AP-1 stimulates the cathepsin K promoter in RAW 264.7 cells. PMID: 17897792
  40. results suggest cathepsin K plays an important role in the immune system; pharmacological inhibition or targeted disruption of cathepsin K resulted in defective Toll-like receptor 9 signaling in dendritic cells in response to unmethylated CpG DNA PMID: 18239127
  41. experiments raise doubts about a crucial role of cathepsin K in arthritic bone destruction PMID: 18240253
  42. cathepsin K deficiency appears to increase lesion stability in brachiocephalic arteries by maintaining the integrity of the tunica media and by decreasing plaque vulnerability to rupture PMID: 18291403
  43. essential role of CatK in adipogenesis and body weight gain, possibly via degradation of fibronectin PMID: 18818416
  44. CTSK may play a role in adipogenesis in early differentiation phases and produce an effect at least partly by degrading type I collagen. PMID: 18840928
  45. The purpose of this paper is to describe bone mass, strength, resorption, and formation in young adult CatK null mice. PMID: 18845279
  46. Leucocyte CatK is an important determinant of atherosclerotic plaque composition, vulnerability, and bone remodelling. PMID: 19015136
  47. cathepsin K interaction with type I collagen is required for 1) the release of cryptic Arg-Gly-Asp motifs during the initial attachment of osteoclasts and 2) termination of resorption PMID: 19028686
  48. increased biosynthesis of cathepsin K was sufficient to accelerate the osteoclastic bone resorption cycle. PMID: 19118660
  49. Free cholesterol accumulation in macrophage membranes activates Toll-like receptors and p38 mitogen-activated protein kinase and induces cathepsin K. PMID: 19122179
  50. the hypercalcification of the cathepsin K-deficient growth plate is due to persistence of calcified cartilage and point to a role of cathepsin K in bone tissue development as well as skeletal remodeling. PMID: 19172215

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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.

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