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Validated All-in-One™ qPCR Primer for CTSK(NM_000396.3) Search again
Product ID:
HQP003626
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
CTS02, CTSO, CTSO1, CTSO2, PKND, PYCD
Gene Description:
cathepsin K
Target Gene Accession:
NM_000396.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
The protein encoded by this gene is a lysosomal cysteine proteinase involved in bone remodeling and resorption. This protein, which is a member of the peptidase C1 protein family, is predominantly expressed in osteoclasts. However, the encoded protein is also expressed in a significant fraction of human breast cancers, where it could contribute to tumor invasiveness. Mutations in this gene are the cause of pycnodysostosis, an autosomal recessive disease characterized by osteosclerosis and short stature. This gene may be subject to RNA editing. [provided by RefSeq].
Gene References into function
- This study demonstrates for the first time a critical role of Cathepsin K in cartilage degradation by synovial fibroblasts (SFs) in rheumatoid arthritis (RA) that is comparable to its well-known activity in osteoclasts.
- cathepsin K binds with chondroitin sulfate for collagenase activity
- Selective inhibition of the collagenolytic activity by altering its S2 subsite specificity
- review discusses the human disease pycnodysostosis caused by cathepsin K deficiency and cathepsin K activity and regulation
- data suggest that extracellular cysteine proteases may participate in the regulation of kinin levels at inflammatory sites, and clearly support that cathepsin K may act as a potent kininase
- cathepsin K may have a role in contributing to the invasive potential of prostate cancer
- In db/db mice, cathepsin k(ctsk) increased, as did Mitf and TFE3, two transcription factors involved in ctsk induction in osteoclasts. Ctsk was increased in other obese models including A(y), fat, and tubby.
- cathepsin K is capable to degrade aggrecan complexes at specific cleavage sites
- cathepsin K has a role in lysosomal collagenolytic activity
- Cathepsin K plays a pivotal role in lung matrix homeostasis under physiological and pathological conditions.
- RANKL-induced cathepsin K gene expression is cooperatively regulated by the combination of the transcription factors and p38 MAP kinase in a gradual manner.
- These findings suggest that a specific function of human cathepsin X is unlikely to result from sequence specificity, but rather from a combination of its unique positional specificity and the co-localization of enzyme and substrate.
- heparan sulfate proteoglycans can regulate the cellular trafficking and the enzymatic activity of cathepsin X
- results support the role of cathepsin K as a major proteinase in osteoclastic bone resorption
- Several novel ketoamide-based inhibitors of cathepsin K have been identified.
- Cathepsin X is not involved in degradation of extracellular matrix, a proteolytic event leading to tumor cell invasion and metastasis, and its expression, restricted to immune cells suggests a role in phagocytosis and the regulation of immune response.
- Cathepsin K co-localized with TRAP in osteoclast-resorptive compartments, supporting a role for cathepsin K in the extracellular processing of monomeric TRAP in the resorption lacuna.
- Osteoblastic cathepsin K may thus contribute to collagenous matrix maintenance and recycling of improperly processed collagen I
- The presence of active cathepsins L, K and S suggests that they contribute to the extracellular breakdown of the extracellular matrix.
- Active cathepsin X mediates the function of beta(2) integrin receptors during cell adhesion and that it could also be involved in other processes associated with beta(2) integrin receptors such as phagocytosis and T cell activation.
- Cathepsin K is essential for normal bone resorption (review)
- CTSK may be involved in the pathogenesis of obesity by promoting adipocyte differentiation.
- Possiable role in homeostasis of dermal extracellular matrix and dynamic equilibrium between matrix synthesis and proteolytic degradation, by counteracting deposition of matrix proteins during scar formation with its matrix-degrading activity.
- analysis of human cathepsins K, L, and S iunteractions with elastins
- Cathepsin K is constitutively expressed in normal human brain, and is alterated in its expression inscizophrenia.
- molecular characterization of 12 unrelated patients with Pycnodysostosis; mutational profile consisted of 12 different mutations, including nine previously unreported ones
- Cathepsin K expression is of predictive prognostic value for patients with high-grade osteosaromas and metastasis at diagnosis.
- In breast cancer patients, cathepsin K serum levels were significantly lower than in sex matched control group or in patients with primary osteoporosis
- in peri-and postmenopausal women, moderate negative correlation of serum cathepsin K levels with change in femoral neck BMD, but none with change in spinal BMD was found
- Induction of cathepsin K is associated with the activation of protein p38 MAP kinase.
- Myeloma-osteoclast interactions stimulated the production of TRAP, cathepsin K, MMP-1, -9, and uPA
- did not detect any plasminogen degradation by cathepsins B, K and L.
- catK may play an important role in melanoma invasion and metastasis by mediating intracellular degradation of matrix proteins after phagocytosis
- cathepsin K is involved in the cleavage of type II collagen in human articular cartilage in certain OA patients and that it may play a role in both OA pathophysiology and the aging process.
- Cathepsin X causes cytoskeletal rearrangements and stimulates migration of T lymphocytes.
- Comparison of the S2 site between rat and human cathepsin K sequences indicated that two S2 residues at Ser134 and Val160 in rat are varied to Ala and Leu, respectively, in the human enzyme.
- crystal structure of a 1:n complex of cathepsin K:chondroitin 4-sulfate
- CTSK may function as a paracrine factor in breast tumorigenesis.
- cathepsin B, cathepsin H, cathepsin X and cystatin C may have roles in inflammatory breast cancer
- incomplete inactivation may partially explain why active cysteine cathepsins are still found during acute lung inflammation