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Validated All-in-One™ qPCR Primer for MCL1(NM_021960.4) Search again
Product ID:
HQP102181
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
BCL2L3, EAT, MCL1-ES, MCL1L, MCL1S, Mcl-1, TM, bcl2-L-3, mcl1/EAT
Gene Description:
MCL1 apoptosis regulator, BCL2 family member
Target Gene Accession:
NM_021960.4(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
The protein encoded by this gene belongs to the Bcl-2 family. Alternative splicing occurs at this locus and two transcript variants encoding distinct isoforms have been identified. The longer gene product (isoform 1) enhances cell survival by inhibiting apoptosis while the alternatively spliced shorter gene product (isoform 2) promotes apoptosis and is death-inducing. [provided by RefSeq].
Gene References into function
- expression in normal, hyperplastic and carcinomatous human prostate
- Myeloid cell factor-1 (Mcl-1)is a critical survival factor for multiple myeloma.
- Expression of apoptotic regulators and their significance in cervical cancer
- Mcl-1 is over epxressed in anaplastic large cell lymphoma cell lines and tumors.
- Antisense strategy shows that Mcl-1 rather than Bcl-2 or Bcl-x(L) is an essential survival protein of human myeloma cells.
- follicular dendritic cells protect CLL B cells against apoptosis, at least in part through a CD44-dependent mechanism involving up-regulation of Mcl-1
- inactivation of Mcl-1 by JNK-dependent phosphorylation may be one of the mechanisms through which oxidative stress induces cellular damage in human cells
- related to ratio of p21(WAF)/cyclin A and Jun kinase phosphorylation to apoptosis in human breast carcinomas
- in basal cell carcinoma cells, the upregulation of the anti-apoptotic Mcl-1 protein by interleukin-6 is mainly through the Janus tyrosine kinase/phosphotidyl inositol 3-kinase/Akt, but not the STAT3 pathway.
- interaction of Mcl-1 with tankyrase 1 leads to the modulation of the apoptosis pathway
- The antiapoptotic effect of the in vitro induction of MCL1 expression in Mycobacterium tuberculosis strain H37Rv-infected macrophages promotes the intracellular survival and proliferation of virulent M. tuberculosis.
- activation of STAT3 was dependent on Ser727 phosphorylation, in the absence of detectable Tyr705 phosphorylation; expression of human STAT3 in murine macrophages rescued inhibition of human Mcl-1 promoter gene activation and cell death induced by NaSal
- mechanisms regulating Mcl-1 levels in MM cells are heterogeneous, and are often independent from IL-6 signaling pathways
- the human EAT gene driven by the EF1 alpha promoter induced hyperplasia of Langerhans islet cells and upregulation of Bax and Bag-1 -- possible heterodimeric partners for EAT in the anti-apoptotic process
- Following UV treatment, Mcl-1 protein synthesis is blocked, the existing pool of Mcl-1 protein is rapidly degraded by the proteasome, and cytosolic Bcl-xL translocates to the mitochondria
- Mcl-1 is an important factor contributing to the chemoresistance of human melanoma in vivo.
- protein geranylgeranylation is critical for regulating myeloma tumor cell survival, possibly through regulating Mcl-1 expression
- data suggest a role for Mcl-1 in protecting endothelial cells against Stx-1-induced apoptosis
- Respiratory syncytial virus mediated the strong induction of antiapoptotic factors of the Bcl-2 family, especially Mcl-1, which might account for the delayed induction of apoptosis in RSV-infected cells.
- fMLP-stimulated neutrophils coordinate the regulation of FOXO transcription factors and the survival factor Mcl-1, a mechanism that may allow neutrophils to alter their survival.
- restoration of MCL-1 expression rescued infected cells from E1A-induced apoptosis
- IL-15 does not increase IL-1alpha or IL-1beta production but induces IL-1Ra release, increases myeloid cell differentiation factor-1 stability, decreases the activity of caspase-3 and caspase-8, resulting in an inhibition of vimentin cleavage
- Mcl-1L degradation by either GrB or caspase-3 interferes with Bim sequestration by Mcl-1L
- These results are consistent with a model in which p53 and Mcl1 have opposing effects on mitochondrial apoptosis by interacting with, and modulating the activity of, the death effector Bak.
- Profound changes in the rate of neutrophil apoptosis following Granulocyte macrophage colony-stimulating factor signaling occur via dynamic changes in the rate of Mcl-1 turnover via the proteasome.
- Mcl-1 function is an effective means of inducing apoptosis in Mcl-1-positive B-cell lymphoma.
- The MCL-1 promoter insertion may identify a high-risk group of CD38-negative CLL patients
- VEGF-induced MM cell proliferation and survival are mediated via Mcl-1; VEGF up-regulates Mcl-1 expression in a time- and dose-dependent manner in 3 human MM cell lines and MM patient cells
- MCL1 is subject to multiple, separate, post-translational phosphorylation events, produced in living versus dying cells at ERK-inducible versus ERK-independent sites
- the fortilin-MCL1 interaction increases cellular resistance to apoptosis by allowing MCL1, an independently antiapoptotic protein, to stabilize another independently antiapoptotic protein, fortilin
- drug sensitivities of CLL leukemic cells correlated inversely with Mcl-1 levels; results suggest that Mcl-1 may contribute to cell survival in CLL; an inverse correlation was found between Mcl-1 expression and Rai stage
- Cleavage of Mcl-1 by caspases modifies its subcellular localization, increases its association with Bim and inhibits its antiapoptotic function.
- Mcl-1 solution structure and analysis of binding by proapoptotic BH3-only ligands
- SDF-1/CXCL12 enhanced cell survival in synergy with other cytokines involves activation of CREB and induction of Mcl-1 and c-Fos
- Overexpression of Mcl-1 protected hepatoma cells against apoptosis induced by tert-butyl hydroperoxide.
- Mcl-1 accumulation is an unwanted molecular consequence of exposure to proteasome inhibitors, which slows down their proapoptotic effects
- MCL-1 is a BCR/ABL-dependent survival factor and interesting target in chronic myeloid leukemia.
- removal of N-terminal domains of Bid by caspase-8 and Mcl-1 by caspase-3 enables the maximal mitochondrial perturbation that potentiates TRAIL-induced apoptosis
- Knockdown results in a significant level of apoptosis in the absence of external apoptotic stimulation
- Mcl-1 is induced by signaling through the B-cell receptor, which promotes survival of chronic lymphocytic leukemia B cells
- Mcl-1 protein is overexpressed in a subset of human NSCLC and enhanced levels of Mcl-1 may protect lung cancer cells from death induced by a variety of pro-apoptotic stimuli.
- Overexpression of anti-apoptotic Mcl-1 may function to enhance the viability of testicular germ cells, thereby leading to tumorigenesis.
- role in sequestering proapoptotic Bak
- The Mcl-1, which has been shown to be essential for the survival of human myeloma cells in vitro, is overexpressed in vivo in MM in relation with relapse and shorter survival. Mcl-1 represents a potential therapeutical target in multiple myeloma.
- autocrine IL-6/Akt signaling pathway enhances Mcl-1 expression in cholangiocarcinoma
- Mule (Mcl-1 ubiquitin ligase E3)is both required and sufficient for the polyubiquitination of Mcl-1
- The interaction of PUMA with MCL1 is not sufficient to prevent the rapid degradation of MCL1.
- The anti-apoptotic poein MCL1 inhibits mitochondrial Ca2+ signals.
- Melphalan-induced apoptosis in multiple myeloma is associated with a cleavage of MCL1 and BIM and a decrease in the MCL1/BIM complex.
- Mcl-1 is downregulated via inhibition of translation after administration of BAY 43-9006 in human leukemia cells
- The unliganded form of Mcl-1 is sensitive to LASU1-mediated degradation of Mcl-1.
- Knockdown of HIF-1alpha induced parallel knockdown of Mcl-1 mRNA and protein expression, whereas Mcl-1 knockdown had no noticeable effect on HIF-1alpha expression. Both of these proteins were shown to be anti-apoptotic.
- Mcl-1 is overexpressed in half of HCC-tissues. ASO targeting Mcl-1 revealed a prominent single agent and chemosensitizing activity against HCC in vitro.
- Mcl-1 is an important factor for the apoptosis resistance of human HCC, and constitutes an interesting target for HCC therapy
- Mcl-1 was critical for the survival of RA synovial fibroblasts, because the forced reduction of Mcl-1 using a Mcl-1 antisense-expressing adenoviral vector induced apoptotic cell death, which was mediated through Bax, Bak, and Bim
- Data demonstrate a novel regulation of tBid by Mcl-1 through protein-protein interaction in apoptotic signaling from death receptors to mitochondria.
- REVIEW: Mcl-1 plays an apical role in many cell death and survival regulatory programs.
- Mcl-1 may serve as a direct substrate for TRAIL-activated caspases implying the existence of a novel TRAIL/caspase-8/Mcl-1/Bim communication mechanism between the extrinsic and the intrinsic apoptotic pathways
- Analysis of B-cell chronic leukemia cells for ZAP 70 expression and the expression of cyclin E, bcl-2, bax, and mcl-1.
- The results demonstrate that the control of MCL-1 stability by GSK-3 is an important mechanism for the regulation of apoptosis by growth factors, PI3K, and AKT.
- This signalling cascade results in viability in a group of patients in which observe an increase of Mcl-1 expression levels after CD5 stimulation in B-CLL patients.
- MCL1 was upregulated by PMA in THP-1 & U937 myeloid leukemia cells, but by microtubule disrupting agents only in THP-1 cells.
- Noxa/Mcl-1 axis is an apoptosis rheostat in dividing cells, in a selective pathway that functions to restrain lymphocyte expansion and can be triggered by glucose deprivation
- The internal EELD domain facilitates mitochondrial targeting of Mcl-1 via a Tom70-dependent pathway.
- Overexpression of Mcl-1 protects HaCaT cells from both ultraviolet and protein kinase C delta-catalytic fragment-induced apoptosis and blocks release of cytochrome c from the mitochondria.
- Mcl-1 is a promising molecular target for antisense oligonucleotide-based treatment strategies for gastric cancer in the future.
- Mycobacterium leprae inhibits apoptosis in THP-1 cells by upregulation of Mcl-1 gene expression and downregulation of Bad and Bak .
- The expression of Mcl-1 was suppressed with small interfering RNA (siRNA) or chemical inhibitors of the phosphatidylinositol 3-kinase (PI 3-kinase)/Akt-1 and signal transducer and activator of transcription 3 (STAT-3) pathways.
- Specific knockdown of Mcl-1 gene expression by small interfering RNA yielded an increase in apoptosis of LNCaP-IL-6+ cells.
- These results demonstrate that anoxia-induced cell death requires the loss of Mcl-1 protein and inhibition of the electron transport chain to negate Bcl-X(L)/Bcl-2 proteins.
- Because of its rapid turnover, Mcl-1 may serve as a convergence point for signals that affect global translation, coupling translation to cell survival and the apoptotic machinery
- GX15-070 induced apoptosis in vitro in MCL cell lines and primary cells from patients with MCL by releasing Bak from Mcl-1 and Bcl-X(L).
- This study is the first to show a clear dissociation between changes in Bcl-2 expression (downregulation) and Bcl-XL, Mcl-1 expression (upregulation) during progression of melanoma.
- Results indicate that the turnover of Mcl-1 by beta-TrCP is an essential mechanism for GSK-3beta-induced apoptosis and contributes to GSK-3beta-mediated tumor suppression and chemosensitization.
- the antiapoptotic function of Mcl-1 is enhanced by serine 64 phosphorylation
- EXEL-0862 induced apoptotic death in EOL-1 cells and imatinib-resistant T674I FIP1L1-PDGFR-alpha-expressing cells, and resulted in significant downregulation of the antiapoptotic protein Mcl-1 through a caspase-3 dependent mechanism.
- Both ionizing radiation and daunorubicin treatment resulted in concerted protein modulations of Mcl-1, Hdm2 and Flt3.
- preformed Bim(EL)/Mcl-1 and Bim(EL)/Bcl-x(L) complexes can be rapidly dissociated following activation of ERK1/2 by survival factors
- tribbles homolog 2-Mcl-1 axis plays an important role in survival factor withdrawal-induced apoptosis of TF-1 erythroleukemia cells.
- stress-induced phosphorylation of eIF2 alpha is directly coupled to mitochondrial apoptosis regulation via translational repression of MCL-1
- The degradation versus stabilized expression of antiapoptotic MCL1 is thus controlled by N-terminal truncation as well as by ERK- and GSK3 (but not G2/M)-induced phosphorylation
- BCR/ABL induces SPK1 expression and increases its cellular activity, leading to upregulation of Mcl-1 in CML cells.
- Treatment with vorinostat and sorafenib synergistically induces apoptosis in chronic myelogenous leukemia cells through a process that involves Mcl1 down-regulation and inhibition of p21(CIP1) induction.
- Mcl-1 confers TRAIL resistance by serving as a buffer for Bak, Bim, and Puma, and sorafenib is a potential modulator of TRAIL sensitivity
- Mcl-1(139) is an HLA-A2-restricted epitope from Mcl-1 recognized spontaneously by cytotoxic T cells in cancer patients.
- These results suggest that the N terminus of MCL-1 plays a major regulatory role, regulating coordinately the mitochondrial (anti-apoptotic) and nuclear (anti-proliferative) functions of MCL-1.
- a caspase-9 signaling cascade induces feedback disruption of the mitochondrion through cleavage of anti-apoptotic Bcl-2, Bcl-xL, and Mcl-1
- Akt and Mcl-1 are major components of a survival pathway that can be activated in CLL B cells by antigen stimulation.
- While TNFalpha had no effect on MCL-1 transcription, it induced expression of another antiapoptotic molecule, BFL-1.
- Mcl-1 degradation primes the cell for Bim and Bax activation and anoikis, which can be blocked by oncogenic signaling in metastatic cells
- MCL1 determines the Bax dependency of Nbk/Bik-induced apoptosis.
- findings not only illustrate MCL1 as an aberrantly expressed reprogramming oncoprotein in follicular lymphomas but also highlight MCL1 as key therapeutic target
- High MCL-1 expression is associated with B-cell chronic lymphocytic leukemia
- the pro-survival activity of MCL-1 proceeds via inhibition of BAX function at mitochondria, downstream of its activation and translocation to this organelle.
- distinctions in the behaviors of Bcl-B and Mcl-1 relative to the other anti-apoptotic Bcl-2 family members, where Bcl-B and Mcl-1 display reciprocal abilities to bind and neutralize Bax and Bak.
- Transcription regulation assays with MCL-1 promoter deletion mutants showed that most of the p53 inhibitory effect was mediated by the -41 to +16 bp promoter binding sites only for TATA-binding protein and other basal transcription factors.
- This study identifies mitogen-activated protein kinase/ERK/Mcl-1 as an important survival signaling pathway in the resistance of melanoma cells to Fas-mediated apoptosis.
- Demonstrate that CUGBP2 inhibits Mcl-1 expression by inhibiting Mcl-1 mRNA translation, resulting in driving the cells to apoptosis during the G(2) phase of the cell cycle.
- Anti-myeloma effect of homoharringtonine with concomitant targeting of the myeloma-promoting molecules, Mcl-1, XIAP, and beta-catenin
- Polymorphisms in MCL1 might be one of genetic factors for the risk of clinical tuberculosis development.
- deregulated PKB/AKT stabilizes Mcl-1 expression in a mammalian target of rapamycin (mTOR)-dependent pathway
- Mcl-1, perhaps acting as an adaptor protein, in controlling the ATR-mediated regulation of Chk1 phosphorylation
- Inhibition of the proteasome by cobalt chloride leads to the accumulation of Mcl-1 which acts to limit cobalt chloride induced apoptosis.
- MCL-1 expression is activated by Triiodothyronine, which increases its promoter activity by a non-genomic mechanism using the PI3-K signal transduction pathway.
- The close correlation between Mcl-1 expression and V(H) gene mutation status, CD38 expression, and ZAP-70 expression offers a biologic explanation for their association with adverse prognosis in CLL.
- Bcl-x(L) and, to a lower extent, Mcl-1, are important anti-apoptotic factors in colorectal carcinoma.
- These findings suggest that calpain inhibition delays neutrophil apoptosis via cyclic AMP-independent activation of PKA and PKA-mediated stabilization of Mcl-1 and XIAP.
- HPV 16/18 up-regulates the expression of interleukin-6 and antiapoptotic Mcl-1 in non-small cell lung cancer
- Erk could phosphorylate Mcl-1 at two consensus residues, Thr 92 and 163, which is required for the association of Mcl-1 and Pin1, resulting in stabilization of Mcl-1
- Mutations also dramatically decrease the levels of MLC1 in cells from megalencephalic leukoencephalopathy with subcortical cysts patients.
- IL-3 up-regulates the expression of the antiapoptotic proteins cIAP2, Mcl-1, and Bcl-X(L) and induces a rapid and sustained de novo expression of the serine/threonine kinase Pim1 that closely correlates with cytokine-enhanced survival.
- Mcl-1 up-regulation is primarily required to maintain apoptosis resistance in C. trachomatis-infected cells
- Mcl-1 expression may therefore be useful in predicting poor response to chemoimmunotherapy.
- multiple copy number alterations in chromosome regions implicated in malignancy progression and indicated a strong expression of MAP2K4 and MCL1 genes in rhabdomyosarcoma