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Validated All-in-One™ qPCR Primer for CTSD(NM_001909.4) Search again
Product ID:
HQP093868
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
CLN10, CPSD, HEL-S-130P
Gene Description:
cathepsin D
Target Gene Accession:
NM_001909.4(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
This gene encodes a lysosomal aspartyl protease composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. This proteinase, which is a member of the peptidase C1 family, has a specificity similar to but narrower than that of pepsin A. Transcription of this gene is initiated from several sites, including one which is a start site for an estrogen-regulated transcript. Mutations in this gene are involved in the pathogenesis of several diseases, including breast cancer and possibly Alzheimer disease. [provided by RefSeq].
Gene References into function
- Evaluation of Cath-D can act as a predictor of distant metastasis of salivary adenoid cystic carcinoma (SACC) and direct the clinical treatment.
- polymorphism unrelated to Alzheimer disease in a Spanish population.
- Molecular dynamics and free energy analyses of cathepsin D-inhibitor interactions.
- expression of cathepsin D in cholesteatoma
- procathepsin D interacts with prosaposin in human breast and ovarian cancer cells. (procathepsin D)
- Down-regulation of cathepsin-D expression by antisense gene transfer inhibits tumor growth and experimental lung metastasis of human breast cancer cells.
- Cathepsin D polymorphism in Italian sporadic and familial Alzheimer's disease. patients and controls. our data do not support a role for the catD gene as a genetic risk factor in the development of AD.
- Cerebrospinal fluid levels of beta-amyloid(42) in patients with Alzheimer's disease are related to the exon 2 polymorphism of the cathepsin D gene.
- cathepsin-D stimulates tumor growth by acting as a mitogenic factor on cancer and endothelial cells independently of its catalytic activity. Our results give the first evidence on the role of cathepsin-D at tumor progression steps, affecting angiogenesis
- QTL associated with general intelligence is located within exon 2 of the cathepsin D (CTSD) gene.
- Expressed in breast cancer and specifically cleaves the chemokines macrophage inflammatory protein-1 alpha, macrophage inflammatory protein-1 beta, and SLC protein that are also expressed in breast cancer.
- Cat D triggers Bax activation, Bax induces the selective release of mitochondrial AIF, and the latter is responsible for the early apoptotic phenotype in T-cells
- COX-2 exerts a negative feedback on the expression of cathepsin D to reduce the generation of the antiangiogenic factor angiostatin, hence promoting a proangiogenic environment.
- cathepsin D has a role in promoting cancer cell proliferation and invasion
- intracellular accumulation of poorly degradable, oxidized lipid-protein cross-links, may alter the turnover of cathepsin D, causing its mistargeting into the extracellular space
- Review. Cathepsin D seems to facilitate early phases of tumor progression such as cell proliferation and local dissemination.
- Cleaves prolactin whose fragments are potentially physiological antiangiogenic inhibitors of tumor growth.
- defective acidification results in the aberrant secretion of proCD in certain cancer cells and interferes mainly with the normal disassembly of the receptor-enzyme complexes and efficient receptor reutilization in the Golgi
- The inhibition of cathepsin D activity by pepstatin A decreased the number of apoptotic cells in catL-deficient A549 cells after anti-Fas treatment.
- cathepsin D is crucial for fibroblast invasive outgrowth and could act as a key paracrine communicator between cancer and stromal cells, independently of its catalytic activity.
- Plasma cathepsin D isoforms and their active metabolites increase after myocardial infarction and contribute to plasma renin activity.
- Our results showed that lowering cathepsin D activity in antisense cell conditioned media abolished their inhibitory effect on osteoblast cell calcification.
- review of cath-D action in cancer progression and metastasis, as well as its dual function in apoptosis [review]
- The minimal lysosomal enzyme recognition domain has been identified in CPSD.
- CTSD*T allele frequency showed a statistically significant increasing trend from Northern to Southern regions of Europe in AD patients and controls
- CatD induces apoptosis via degradation of Trx protein, which is an essential anti-apoptotic and reactive oxygen species scavenging protein in endothelial cells
- results imply that cytosolic cath-D stimulates apoptotic pathways by interacting with a member of the apoptotic machinery rather than by cleaving specific substrate(s)
- Functional analysis indicated that proteolytic processing of DCD-1L by Cathepsin D in human sweat modulates the innate immune defense of human skin.
- Possession of the CTSD T allele has a modulating effect on the pathogenesis of Alzheimer disease by increasing the amount of Abeta deposited as senile plaques in the brain.
- A model is proposed in which cathepsin D inactivates CCL20 and possibly prevents the establishment of an effective antitumoral immune response in melanomas.
- Our data suggest that the CTSD-T allele of the CTSD-C/T polymorphism is associated with an increased relative risk for late-onset AD and, more interestingly, the combination of CTSD-T with the A2M-G allele seems to increase this risk.
- Glucosamine sulfate-induced K562 cell apoptosis involves the translocation of cathepsin D from the lysosome to the cytosol.
- Cathepsin D regulates intracellular transport of phospholipid and cholesterol and ABCA1-mediated lipid efflux.
- The influence of aluminum (Al) on the Abeta peptide degradation by cathepsin D, was demonstrated.
- Functional mapping of the N-terminal sequence of procathepsin D is reported; peptides derived from this sequence were used to localize and characterize the structural determinants involved in activity regulation of the enzyme's catalytic core.
- mutagenized the region of aminoacids (comprising the beta-hairpin loop) involved in the latter proteolytic maturation step and generated a mutant CD that cannot be converted into the mature double-chain form
- cathepsin D was a typical secretory protein that exhibited the increased abundance inM-BE, a SV40T-transformed human bronchial epithelial cell line with the phenotypic features of early tumorigenesis at high passage
- Myocardial STAT3 protein levels are reduced and serum levels of activated cathepsin D and 16 kDa prolactin are elevated in postpartum cardiomyopathy patients.
- Results confirm that the proapoptotic effect of cathepsin D in the cytosol is independent of its catalytic activity and suggest that the interaction of cathepsin D with the downstream effector does not involve the active site of the enzyme.
- Lysosome is the primary target and the axis cathepsin D-Bax as the effective pathway of hydrogen peroxide lethal activity in neuroblastoma cells.
- Secretion of procathepsin D is not only linked to cancer cells but also plays a role in normal physiological conditions like wound healing and tissue remodeling.
- Overexpression of S100P leads to increased expression of another early pancreatic cancer marker, S100A6, as well as the aspartic protease cathepsin D, both of which are involved in cellular invasion.
- The kinetic constants (kcat, Km, kcat/Km) for cleaving peptides with beta-sites of the WT or the mutated Swedish families (SW) APP by human BACE 1 and cathepsin D were determined and found to be similar.
- the entire 27-44 amino acid region of activation peptide is necessary for the stimulatory actions of procathepsin D on breast cancer cells
- This data do not support a role of two gene polymorphisms of the CTSD rs17571 as a possible susceptibility factors for sporadic AD.
- [review]
- Missorting of cathepsin D in GARP-depleted cells results from accumulation of recycling MPRs in a population of light, small vesicles downstream of endosomes.
- treatment with human interferon-gamma and/or human tumor necrosis factor-alpha had little effect on intracellular levels of Cath D, whereas cytokine stimulation increased the extracellular presence of ProCath D in endothelial cell cultures
- Results describe cathepsin D and aldo-keto reductase 1C2 and 1B10 dysregulation in Barrett's esophagus and esophageal adenocarcinoma.
- alterations in the amyloid processing activity of cathepsin D may affect the neuropathogenesis of variant Creutzfeldt-Jakob disease
- GGA2 is recruited to the trans-Golgi network independently of the other Golgi-localized, gamma-ear-containing, ARF-binding proteins and is required for the efficient sorting of lysosomal enzymes
- breast cancer cells, which are devoid of Maspin, are refractory to IFN-gamma with respect to changes in vacuolar pH and CatD
- up-regulation of cathepsin D enhances angiogenesis, growth, and metastasis
- role of cathepsin D in antiapoptotic signaling in neuroblastoma cells and suggest a novel mechanism for the development of chemotherapy resistance in neuroblastoma.
- Activities of cathepsins B and D in the lysate of necrotic rho0 cells were inhibited by the addition of apoptotic parental Jurkat cell lysate
- cathepsin D is the main lysosomal enzyme involved in alpha-synuclein degradation
- Data show that cathepsin D is decreased in the CSF of temporal lobe epilepsy patients.