Recombinant Human Cathepsin K (CTSK) Protein (His)

Name: Recombinant Human Cathepsin K (CTSK) Protein (His)
Brand: Beta LifeScience
SKU: BLC-10829P
Price: 460.0 USD
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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

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Product Overview

Description	Recombinant Human Cathepsin K (CTSK) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P43235
Target Symbol	CTSK
Synonyms	Cathepsin K; Cathepsin O; Cathepsin O1; Cathepsin O2; Cathepsin X; CATK_HUMAN; CTS02; Ctsk; CTSO; CTSO1; CTSO2; MGC23107; PKND; PYCD
Species	Homo sapiens (Human)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	APDSVDYRKKGYVTPVKNQGQCGSCWAFSSVGALEGQLKKKTGKLLNLSPQNLVDCVSENDGCGGGYMTNAFQYVQKNRGIDSEDAYPYVGQEESCMYNPTGKAAKCRGYREIPEGNEKALKRAVARVGPVSVAIDASLTSFQFYSKGVYYDESCNSDNLNHAVLAVGYGIQKGNKHWIIKNSWGENWGNKGYILMARNKNNACGIANLASFPKM
Expression Range	115-329aa
Protein Length	Full Length of Mature Protein
Mol. Weight	25.5kDa
Research Area	Signal Transduction
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 and may participate partially in the disorder of bone remodeling. 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	HGNC: 2536 OMIM: 265800 KEGG: hsa:1513 STRING: 9606.ENSP00000271651 UniGene: Hs.632466
Associated Diseases	Pycnodysostosis (PKND)
Tissue Specificity	Predominantly expressed in osteoclasts (bones). Expressed in thyroid epithelial cells.

Gene Functions References

Sclerostin is degraded by cathepsin K in vitro. Cathepsin K degradation of sclerostin is affected by hypoxia. PMID: 29859187
Upregulation of CTSK seems to be associated with high incidence of lymphatic spread and poor survival in OSCC. CTSK could therefore serve as a predictive biomarker for OSCC. PMID: 29618339
our data showed that elevated Cathepsin K in epithelial ovarian cancer can potentiate the metastasis of epithelial ovarian cancer cells PMID: 29303207
results highlight the possibility that the interaction between GAGs and collagen under acidic conditions has a regulatory impact on cathepsin K-mediated bone degradation. PMID: 29029096
measurement of a periostin fragment resulting from in vivo cathepsin K digestion may help to identify subjects at high risk of fracture. PMID: 28766739
cathepsin K in the development of chronic subdural hematoma PMID: 28887075
Cathepsin K expression within the subchondral bone of the medial tibia plateau was not associated with osteoclast density or symptomatic knee osteoarthritis. PMID: 28087412
The enhanced invasion of carcinomas resulting from cathepsin K overexpression is probably due to the increased cell migration and adhesion. Thus, cathepsin K is implicated not only in protein degradation but also in invasion, migration and adhesion of oral squamous cell carcinomas. PMID: 28117540
positive expression of cathepsin K in melanoma of the skin is associated with other unfavorable prognostic factors PMID: 27709599
Patients affected by castration-resistant prostate carcinoma may be tested for cathepsin K, and a positive strong expression (2+) could be a useful predictive biomarker of response to targeted agents, aiding in the selection of patients eligible for these treatments. PMID: 28085175
Of 160 top compounds tested in enzymatic assays, 28 compounds showed blocking of the collagenase activity of Cathepsin K (CatK) at 100 muM. PMID: 29088253
Cathepsin K cleavage of SDF-1alpha inhibits its chemotactic activity towards glioblastoma stem-like cells. PMID: 28040478
Increased cathepsin K expression in skull base chordoma was associated with tumor invasion and reduced progression free survival. PMID: 28216213
Immunohistochemistry confirmed cathepsin K protein was expressed in lymphangioleiomyomatosis but not control lungs. Cathepsin K gene expression and protein and protease activity were detected in lymphangioleiomyomatosis -associated fibroblasts but not the LAM cell line 621-101. PMID: 28623674
The allosteric site of cathepsin K has been modified by site-directed mutagenesis, and it was shown that it is involved in specific regulation of the collagenolytic activity of cathepsin K. PMID: 27859061
Cathepsin K and osteocalcin plasma levels may be suggested as the significant markers of osteopoenia/osteoporosis. In addition, cathepsin K plasma level can be also a valuable marker of severe Coronary Atherosclerosis and Coronary Artery Calcification . PMID: 26988144
Six mutations in CTSK were identified in 33 families with pycnodysostosis. The high frequency of pycnodysostosis in Ceara State is the consequence of the high inbreeding in that region. PMID: 27558267
The above studies not only demonstrated that CTSK was widely expressed in tooth-related cells (including odonto- clasts, periodontal ligament cells, pulp cells and odonto- blasts), but also indicated that CTSK was closely related to the development of tissues in oral and maxillofacial region as well as occurrence and development of many oral diseases. PMID: 26458004
This mutation (c.480_481insT), (p.L160fsX173) is a novel frameshift mutation. The index case extends the phenotypic spectrum and the list of previously reported mutations in the CTSK gene. PMID: 25304337
There is an increase in levels of CATK in type 1 Gaucher patients compared to the control group. In the patient group, CATK showed higher levels in patients with bone damage compared to those without it. PMID: 25662720
increased expression and activation in osteoarthritis cartilage PMID: 26241216
elevated levels of CatK are closely associated with the presence of chronic heart failure and that the measurement of circulating CatK provides a noninvasive method of documenting and monitoring the extent of chronic heart failure PMID: 26302400
Cathepsins in Rotator Cuff Tendinopathy: Identification in Human Chronic Tears and Temporal Induction in a Rat Model. PMID: 25558848
The study determined almost identical substrate specificities for cysteine cathepsins K, L and S. PMID: 25626674
Matrix-metalloproteinase-9 is cleaved and activated by cathepsin K. PMID: 26219353
Sequence analysis of the patient's CTSK gene revealed homozygosity for a missense mutation (c.746T>C) in exon 6, which leads to amino change (p.Ile249Thr) in the mature CTSK protein PMID: 25725806
The presence of high levels of inactive proforms of cathepsin K in GBM tissues and cells indicate that in GBM the proteolytic/collagenolytic role is not its primary function but it plays rather a different yet unknown role. PMID: 25356585
Two compounds have sizable effects on enzyme activity using interstitial collagen as a natural substrate of cathepsin K and four compounds show a significantly stabilizing effect on cathepsin K. PMID: 25184245
Studies indicate cathepsin X as a target for improving diagnosis and treating cancer patients. PMID: 24835450
SDF-1alpha is involved in homing of CXCR4+ GSLCs and leukocytes and that cathepsin K and osteopontin are involved in the migration of GSLCs out of the niches PMID: 25809793
one cathepsin K molecule binds to collagen-bound glycosaminoglycans at the gap region and recruits a second protease molecule that provides an unfolding and cleavage mechanism for triple helical collagen PMID: 25422423
The identification of CatK exosites opens up the prospect of designing highly potent inhibitors that selectively inhibit the degradation of therapeutically relevant substrates by this multifunctional protease. PMID: 25279554
The data indicated that elevated levels of cathepsin K are closely associated with the presence of CAD and that circulating cathepsin K serves a useful biomarker for CAD. PMID: 24954318
synergism between HIV proteins and pro-atherogenic shear stress to increase endothelial cell expression of the powerful protease cathepsin K PMID: 24719048
Cathepsin K appears to be consistently and strongly expressed in melanocytic lesions and valuable in distinguishing malignant melanomas from the majority of human cancers. PMID: 24696729
results demonstrate that CS plays an important role in contributing to the enhanced efficiency of CatK collagenase activity in vivo PMID: 24958728
identified five CTSK missense mutations (M1I, I249T, L7P, D80Y and D169N), one nonsense mutation (R312X) and one 301 bp insertion in intron 7, which is revealed as Alu sequence; among them, only L7P and I249 were described previously PMID: 24767306
Expression of cathepsins K, S and V within keratinocytes is reduced in photoprotected skin of aged women. PMID: 23871919
The use of exome sequencing in the molecular diagnosis of 2 siblings initially thought to be affected by "intermediate osteopetrosis", which identified a homozygous mutation in the CTSK gene, is described. PMID: 24269275
Data indicate that cathepsin K is expressed in oral tongue squamous cell carcinoma (OTSCC) tissue in both carcinoma and tumor microenvironment (TME) cells. PMID: 23951042
Increased plasma CatK levels are linked with the presence of atrial fibrillation. PMID: 24342995
Skipping of the 121-bp exon 2 results in elimination of the normal start codon and an expected absence of the wild-type CTSK protein. PMID: 24134756
catalase expression (or activity) was higher, while intracellular and extracellular Cat S, Cat L, and Cat K activities were lower in the non-invasive CL1-0 cells compared to the highly invasive CL1-5 cells. PMID: 24583396
Identification of a novel insertional frameshift mutation in exon 4 of the CTSK gene in two families with pycnodysostosis. PMID: 23689398
The basic amino acid clusters in cathepsin K play roles in the formation of collagenolytically active protease complexes. PMID: 24088021
These data indicated that high levels of CatK are closely linked with the presence of coronary artery disease. PMID: 23369704
Our results demonstrate that increased adhesion, migration and invasiveness of tumor cells depend on the inactivation of the tumor suppressive function of profilin 1 by cathepsin X. PMID: 23326535
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
Cathepsin X deficiency leads to a reduced phosphorylation of the IGF-I receptor in response to IGF-I stimulation. PMID: 23152410
show for the first time that bone marrow macrophage-supplied CTSK may be involved in CCL2- and COX-2-driven pathways that contribute to tumor progression in bone PMID: 22614014

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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.