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Validated All-in-One™ qPCR Primer for PAK1(NM_002576.4) Search again
Product ID:
HQP012156
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
IDDMSSD, PAKalpha, alpha-PAK, p65-PAK
Gene Description:
p21 (RAC1) activated kinase 1
Target Gene Accession:
NM_002576.4(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
PAK proteins are critical effectors that link RhoGTPases to cytoskeleton reorganization and nuclear signaling. PAK proteins, a family of serine/threonine p21-activating kinases, include PAK1, PAK2, PAK3 and PAK4. These proteins serve as targets for the small GTP binding proteins Cdc42 and Rac and have been implicated in a wide range of biological activities. PAK1 regulates cell motility and morphology. Alternativelt spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq].
Gene References into function
- Pak1 forms homodimers in vivo and its dimerization is regulated by the intracellular level of GTP-Cdc42 or GTP-Rac1
- PAK1 primes MEK1 for phosphorylation by Raf-1 kinase during cross-cascade activation of the ERK pathway.
- binding of the Rho family member Cdc42 to PLD1 and the subsequent stimulation of its enzymatic activity are distinct events
- Pak1 interacts with and phosphorylates histone H3 and may thus influence the Pak1-histone H3 pathway, which in turn may influence mitotic events in breast cancer cells
- FLNa may be essential for Pak1-induced cytoskeletal reorganization
- Cdc42/Rac1-dependent activation of PAK may trigger early platelet shape change, at least in part through the regulation of cortactin binding to PAK.
- p21-activated kinase 1 (PAK1) interacts with the Grb2 adapter protein to couple to growth factor signaling
- phorbol ester induced cell migration is accompanied by selective and transient down-regulation of PAK1, which coincided with the formation of stress fibres.
- role in phosphorylating Raf-1 regulates Raf-1 autoinhibition
- results identify a novel signaling pathway linking estrogen action to Pak1 signaling, and Pak1 to FKHR, suggesting that Pak1 is an important mediator of estrogen's cell survival functions
- Activated Cdc42 at the leading edge of a neutrophil in culture helps orient the cell's axis in a signaling complex with G beta gamma, PAK1, and PIXalpha.
- G beta gamma binds PAK1 and, via PAK-associated PIX alpha, activates Cdc42 which, in turn, activates PAK1. In this pathway, PAK1 is not only an effector for Cdc42, but it also functions as a scaffold protein required for Cdc42 activation.
- PAK1 regulates contact inhibition during epithelial wound healing.
- PAK1 copy number gains were observed in 30% of ovarian carcinomas and PAK1 protein was expressed in 85% of tumors. PAK1 gains were associated with high grade.
- Pak1 regulation of cyclin D1 expression might involve an NF-kappaB-dependent pathway; Pak1 is up-regulated in breast tumors
- Tat induces actin cytoskeletal rearrangements through PAK1 in human umbilical vein endothelial cells
- Phosphorylation of p41-ARC protein by p21-activated kinase 1.
- PAK2 is constitutively activated in certain breast cancer cell lines and that this active PAK is mislocalized to atypical focal adhesions in the absence of high levels of activated Rho GTPases.
- Src- & ROS-dependent PDK1 activation leads to site-specific PAK1 phosphorylation. This is critically important for PDGF-induced VSMC migration, a process integral to the vascular response to injury that leads to vessel occlusion & plaque formation.
- Pak-1 has a role in human colorectal tumor invasiveness and motility
- Pak is activated by Down syndrome cell adhesion molecule (DSCAM)
- These results support a role for Pak1-mediated RhoGDI phosphorylation as a mechanism for Cdc42-mediated Rac activation, and suggest the possibility of Rac-induced positive feed-forward regulation of Rac activity.
- PAK is a central regulator of endothelial permeability induced by multiple growth factors and cytokines via an effect on cell contractility
- cell signaling kinase Pak1 is a novel regulator of glucose metabolism through its phosphorylation and regulation of PGM activity.
- NF-kappaB- and C/EBPbeta-driven interleukin-1beta gene expression and PAK1-mediated caspase-1 activation play essential roles in interleukin-1beta release from Helicobacter pylori lipopolysaccharide-stimulated macrophages
- epithelial cell motility is modulated by integrin engagment through RhoA/ROCK and PAK1
- PAK1 negatively regulates the activity of NET1
- These findings define the nuclear localization signals (NLSs) of Pak1, its association with chromatin, and the resulting modulation of transcription, thus opening new avenues to further the search for nuclear Pak1 functions.
- ArgBP2gamma is a physiological substrate of Akt, functions as an adaptor for Akt and PAK1, and plays a role in Akt/PAK1 cell survival pathway
- Pak1-SHARP interaction plays an essential role in enhancing the corepressor functions of SHARP, thereby modulating Notch1 signaling in human cancer cells.
- PAK1 phosphorylation of tubulin cofactor B (TCoB)is essential for the polymerization of new microtubules.
- The regulation of phosphorylation and function of Snail by Pak1 represents a novel mechanism by which a signaling kinase might contribute to the process of epithelial-mesenchymal transition.
- Pak1-dependent Raf-1 phosphorylation regulates its mitochondrial localization, phosphorylation of BAD, and Bcl-2 association
- PAK1 recruitment to the T cell-antigen-presenting cell interface required interaction with PIX.
- 1.8 A resolution structure for the free PAK1 kinase domain was determined.
- Data suggest that nischarin, in addition to regulating the p21-activated kinase (PAK) strand of Rac1 signaling, can also regulate other links in the web of Rac1 signaling pathways.
- p21-activated kinase 1 has a role in the suppression of anoikis in breast cancer cells
- the SH3 domain of betaPix specifically interacts with a proline-arginine motif (PxxxPR) present within the ubiquitin ligase Cbl and Pak1 kinase. Cbl and Pak1 compete for binding to betaPix.
- Results show that PAK1 cooperate with different Rho effectors to regulate matrix contraction.
- PI3K through p21-activated kinase 1 regulates FRA-1 proto-oncogene induction by cigarette smoke and the subsequent activation of the Elk1 and cAMP-response element-binding protein transcription factors
- Myosin II-B resides in a complex with p21-activated kinase 1 (PAK1) and atypical protein kinase C (PKC) zeta (aPKCzeta) and the interaction between these proteins is EGF-dependent.
- Our data support a role for Pak1, particular Pak1 localized to the nucleus, in ERalpha signaling and in tamoxifen resistance.
- Phosphorylation of caldesmon by PAK is a dynamic process required to regulate actin dynamics and membrane protrusions in wound-induced cell migration.
- Increased p21-activated kinase-1 expression is associated with invasive potential in uveal melanoma
- Akt1 and Akt2 have opposing roles in Rac/Pak signaling and cell migration
- TGF-ss, via PI3K, recruits the actin cytoskeleton to HER2, which colocalizes with Vav2, activated Rac1, & its effector Pak1 at lamellipodia, leading to prolonged Rac1 activation, enhanced cell motility & survival. Dominant-negative Pak1 abrogates this.
- p70 S6 kinase activates PAK1 and contributes to phosphatidylinositol 3-kinase- and ERK-mediated regulation of HCV RNA replication
- Results demonstrate a novel mechanism of signal termination mediated by the Rho-family GTPases Chp and Cdc42, which results in ubiquitin-mediated degradation of one of their direct effectors, Pak1.
- PAK1 is a physiological upstream kinase for integrin-linked kinase (ILK); PAK1 depletion dramatically increases the nuclear and focal point accumulation of ILK.
- Amplification of PAK1 is associated with recurrence and tamoxifen resistance in postmenopausal breast cancer
- ESE-1 functions are coordinately regulated by Pak1 phosphorylation and beta-TrCP-dependent ubiquitin-proteasome pathways.
- we present a model for Pak1 signaling that provides a mechanism for specifically affecting cardiac cellular processes--REVIEW
- point to Pak1 as an exciting target for therapy of renal cancer, which remains highly refractory to existing treatments
- study reports that elevated (alpha6)beta4 integrin-dependent Rac-Pak1 signaling supports resistance to apoptosis in mammary acini by permitting stress-dependent activation of the p65 subunit of NF-kappaB through Pak1
- Rac1/Pak1/LIMK1 signaling pathway controls cofilin activity within the lamellipodium.
- 16k PRL inhibits cell migration by blocking the Ras-Tiam1-Rac1-Pak1 signaling pathway in endothelial cells
- Pak1 overexpression enhanced htt toxicity in cell models and neurons in parallel with its ability to promote aggregation, while Pak1 knockdown suppressed both aggregation and toxicity
- a VAV1-Rac1-PAK1 signaling axis in mononuclear phagocytes regulating superoxide production in a stimulus-dependent manner.
- In an ovarian carcinoma cohort, RSF1 was amplified in 15% of the cases. It was correlated with serous histology. The 11q13 amplicon in ovarian cancer is likely driven by a cassette of genes rather than by a single oncogene.
- The data indicate that PAK1 is at the interface between junction destabilization and increased motility during morphogenetic events.
- Clathrin-independent endocytosis used by the IL-2 receptor is regulated by Rac1, Pak1 and Pak2.
- p21-activated kinase-aberrant activation and translocation may have a role in Alzheimer disease pathogenesis
- These results provide an insight into the molecular mechanisms of CtBP1/BARS activation in membrane fissioning, and extend the relevance of CtBP1/BARS-induced fission to human viral infection.
- Overexpression of p21-activated kinase 1 may be a key coordinator of aberrant cell survival and proteolysis in breast cancer progression.
- Pak1 and Pak2 mediate tumor cell invasion through distinct signaling mechanisms
- alpha2beta1 integrin clustering defines its own entry pathway that is Pak1 dependent but clathrin and caveolin independent and that is able to sort cargo to caveosomes
- 1) PAK plays a required role in hyperosmotic signaling through the PI3K/pTEN/Cdc42/PP2Calpha/p38 pathway, and 2) PAK and PP2Calpha modulate the effects of this pathway on focal adhesion dynamics.
- PAK1-specific paxillin phosphorylation at Ser(273) is critically involved in positive-feedback regulation.
- Data examine possible allelic imbalance in papillary thyroid cancer at EMSY, CAPN5, and PAK1, as candidate genes within 11q13.5-q14 region using a single nucleotide polymorphism-based analysis.
- Pak1 is a target of miR-7 and that HoxD10 plays a regulatory role in modifying the expression of miR-7.
- Expression of active p21-activated kinase-1 induces Ca2+ flux modification with altered regulatory protein phosphorylation in cardiac myocytes.