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Validated All-in-One™ qPCR Primer for PTPN6(NM_080548.4) Search again
Product ID:
HQP015860
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
HCP, HCPH, HPTP1C, PTP-1C, SH-PTP1, SHP-1, SHP-1L, SHP1
Gene Description:
protein tyrosine phosphatase non-receptor type 6
Target Gene Accession:
NM_080548.4(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 is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. N-terminal part of this PTP contains two tandem Src homolog (SH2) domains, which act as protein phospho-tyrosine binding domains, and mediate the interaction of this PTP with its substrates. This PTP is expressed primarily in hematopoietic cells, and functions as an important regulator of multiple signaling pathways in hematopoietic cells. This PTP has been shown to interact with, and dephosphorylate a wide spectrum of phospho-proteins involved in hematopoietic cell signaling. Multiple alternatively spliced variants of this gene, which encode distinct isoforms, have been reported. [provided by RefSeq].
Gene References into function
- The Lyn/CD22/SHP-1 pathway is important in autoimmunity. Naive and tolerant B-cells differ in their calcium signaling in response to antigenic stimulation.
- peripheral blood monocytes treated for 5--8 days with GM-CSF (i.e. mature Mphi) acquired the capacity to assemble tyrosine phosphatase SHP-1 with CD9, alpha3-beta1 integrin and their CD46.
- SHP-1 is recruited to the NK cell immune synapse within 1 min in both cytolytic and noncytolytic conjugates, allowing clear distinction between noncytolytic and cytolytic interactions at this early time.
- interacts with siglec-11
- evidence of cytokine-regulated SHP-1 nuclear localization mediated by a bipartite nuclear localization signal, suggesting that SHP-1 regulates nuclear signaling in cell growth control.
- ILT2 triggering on cutaneous T-cell lymphoma (CTCL) cells leads to the recruitment of SHP-1 and to the specific inhibition of CTCL malignant cell proliferation in Sezary syndrome induced by CD3/T-cell receptor. (TCR) stimulation.
- In the T cell line HUT-78, JAK3 was found to be highly phosphorylated. These results suggest that SHP-1 might be involved in maintaining the IL-2R/JAK3 signaling pathway under control and point towards a role of SHP-1 in the pathogenesis of the disease.
- Functional loss of SHP1 is associated with the pathogenesis of leukemias/lymphomas.
- participation in regulation of Stat6 dephosphorylation
- crystal structure of the C-terminal truncated human SHP-1 in the inactive conformation at 2.8-A resolution and refined the structure to a crystallographic R-factor of 24.0%
- SHP-1 may be involved in the regulation of beta-catenin transcriptional function and in the negative control of intestinal epithelial cell proliferation
- show the existence of multiple transcripts of SHP-1 in human transformed T cells and normal PBMCs and give evidence supporting the concept that SHP-1 can negatively regulate growth of malignant T cells
- SHP-1 plays a pivotal role in reorganization of cytoskeletal architecture by inducing actin dephosphorylation.
- A blockade in early signaling events observed with TCR antagonists occurs via a negative intracellular signal that is mediated by SHP-1.
- Associates with phosphorylated Fc gamma RIIa to modulate signaling events in myeloid cells
- Vav1 trapping was independent of actin polymerization, suggesting that inhibition of cellular cytotoxicity occurs through an early dephosphorylation of Vav1 by SHP-1, which blocks actin-dependent activation signals.
- SHP-1 inhibits PRL receptor and EPO receptor signaling by recruitment and targeting of SOCS-1 to Jak2, highlighting a new mechanism of SHP-1 regulation of cytokine-receptor signaling.
- Down-regulation of SHP1 is associated with adult T-cell leukemia
- SHP1 gene silencing is one of the events critical to the onset of malignant lymphomas/leukemias in humans.
- hypermethylated in multiple myeloma
- SHP-1 can dephosphorylate alpha-actinin in vitro and in vivo.
- CNS myelination was significantly reduced in SHP-1-deficient mice relative to their normal littermates at multiple times during the active period of myelination.
- Mice lacking SHIP-1 have defects in the erythroid and myeloid compartments similar to those in mice lacking Lyn or SHP-1.
- inactivation of Ros by SHP-1-mediated dephosphorylation plays a role in the regulation of complex stability
- TFG is a novel protein able to modulate SHP-1 activity.
- transformation of TF-1 cells with FLT3/ITD mutations suppressed the activity of SHP-1 by approximately 3-fold
- SHP-1 may be a novel target molecule to sensitize erythropoietin action in hemodialysis patients with hyporesponsive anemia
- SHP-1 acts at multiple stages of hematopoietic differentiation to alter lineage balance. Expression of WT SHP-1 reduced myeloid colony numbers while increasing the numbers of secondary embryoid bodies and mixed hematopoietic colonies obtained
- SRIF inhibitory effects on thyroid medullary carcinoma cell proliferation are mediated, at least in part, by SHP-1, which acts through a MAPK-dependent mechanism
- STAT3 may transform cells by inducing epigenetic silencing of SHP-1 in cooperation with DNMT1 and histone deacetylase 1
- Shp-1 mediates the antiproliferative activity of tissue inhibitor of metalloproteinase-2
- Our results suggest an alteration of the SHP-1 modulation by GM-CSF in lipid rafts of PMN with aging. These alterations could contribute to the decreased GM-CSF effects on PMN.
- SHP1 activation, association with Src and dephosphorylation of specific proteins were dependent on extracellular calcium and maintenance of a higher cytosolic calcium plateau.
- Protein phosphatase 6 specifically down-regulates transforming growth factor beta-activated kinase 1 (TAK1) through dephosphorylation of threonine-187 in the activation loop, suppressing inflammatory responses via TAK1 signaling pathways.
- increased activity of inhibitory molecules, such as Src homology domain-containing protein tyrosine phosphatase-1 (SHP-1) and suppressors of cytokine signalling (SOCS), is responsible for age-related failure of GM-CSF to stimulate neutrophil functions
- findings provide an insight into the structure of the hematopoietic cell-specific P2 promoter of the SHP-1 gene and identify PU.1 as the transcriptional activator of the P2 promoter
- These data suggest a mechanism of IC-mediated inhibition of IFN-gamma signaling, which requires the ITAM-containing FcgammaRI, as well as the ITIM-dependent phosphatase SHP-1, ultimately resulting in the suppression of STAT1 phosphorylation.
- SHP-1 loss correlates with, and may contribute to, progression of cutaneous T-cell lymphoma
- novel mechanism regulating GH signaling in which estrogen receptor modulators enhance GH activation of the JAK2/STAT5 pathway in a cell-type-dependent manner by attenuating protein tyrosine phosphatase activities
- In human erythrocytes SHP-1 is present in membranes from resting cells, but in 5% of the protein amount. SHP-1 ensures band 3 dephosphorylation.
- SHP-1 and SHP-2, two structurally related cytoplasmic protein-tyrosine phosphatases with different cellular functions and cell-specific expression patterns, were compared for their intrinsic susceptibility to oxidation by H(2)O(2).
- A novel 6-mer motif SKHKED within the carboxyl terminus of SHP-1 is necessary and sufficient for lipid raft localization and for the function of SHP-1 as a negative regulator of T-cell receptor signaling.
- Thus the phosphorylation and dephosphorylation of caspase-8, mediated by Lyn and SHP-1, respectively, represents a novel, dynamic post-translational mechanism for the regulation of neutrophil apoptosis
- Mononuclear leukocytes of multiple sclerosis patients have a deficiency in SHP-1 and increased inflammatory gene expression.
- SHP-1 plays an important role in regulating oxidative stress.
- TIMP1 functions as a differentiating and survival factor of GC B cells by modulating CD44 and SHP1 in the late centrocyte/post-GC stage, regardless of EBV infection.
- Downregulation of platelet responsiveness upon contact with LDL by the protein-tyrosine phosphatases SHP-1 and SHP-2.
- Deletion of the SHP-1 gene by small interfering RNA abolished the ability of boswellic acid to inhibit STAT3 activation.