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MARK2 encodes a member of the Par-1 family of serine/threonine protein kinases. Zusätzlich bieten wir Ihnen MAP/microtubule Affinity-Regulating Kinase 2 Antikörper (111) und und viele weitere Produktgruppen zu diesem Protein an.
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In cell-based assays, Mark2 depletion indeed reduces Dvl (zeige DVL2 Proteine) gene expression and interrupts neural stem cell (NSCs) growth and differentiation, which are likely to be mediated through a decrease in class IIa HDAC (zeige HDAC3 Proteine) phosphorylation and reduced H3K4ac and H3K27ac occupancies at the Dvl1 (zeige DVL1 Proteine)/2 promoters.
HIV-1 did not stimulate widespread FEZ1 (zeige LZTS1 Proteine) phosphorylation but, instead, bound microtubule (MT) affinity-regulating kinase 2 (MARK2) to stimulate FEZ1 (zeige LZTS1 Proteine) phosphorylation on viral cores.
Low expression of Mark2 is associated with uterine cervical neoplasms.
In this study, through quantitative analysis of the complex formation between CagA (zeige S100A8 Proteine) and PAR1b, the authors found that several CagA (zeige S100A8 Proteine) species have acquired elevated PAR1b-binding activity via duplication of the CagA (zeige S100A8 Proteine) multimerization motifs, while others have lost their PAR1b-binding activity.
In the modeled structure of inactive MARK2, activation segment occludes the enzyme active site and assumes a relatively stable position.
In conclusion, baicalin and DDP (zeige TIMM8A Proteine) were synergistic at inhibiting proliferation and invasion of human lung cancer cells at appropriate dosages and incubation time in the presence or absence of DDP (zeige TIMM8A Proteine) resistance. The attenuation of DDP (zeige TIMM8A Proteine) resistance was associated with downregulation of MARK2 and p-Akt (zeige AKT1 Proteine).
MARK2 plays a role in promoting malignant phenotypes of lung cancer.
Phosphorylation of RNF41 (zeige RNF41 Proteine) by Par-1b regulates basolateral membrane targeting of laminin-111 receptors.
induces asymmetric inheritance of plasma membrane domains via LGN (zeige GPSM2 Proteine)-dependent mitotic spindle orientation in proliferating hepatocytes
Perturbation of PAR1b and SHP2 (zeige PTPN11 Proteine) by CagA (zeige S100A8 Proteine) underlies the oncogenic potential of CagA (zeige S100A8 Proteine).
These results indicate that the basal localization of Par-1b in the outer epithelial cells is required for myoepithelial cell compression, and Par-1b is required for myoepithelial differentiation, regardless of its localization.
data suggest ectopic PAR1 (zeige F2R Proteine) expression is not tolerated in mouse platelets and indicate a different approach is required to develop a small animal model for the purpose of any future preclinical testing of PAR (zeige AFG3L2 Proteine) antagonists as anti-platelet drugs
a model whereby MARK2 negatively regulates insulin (zeige INS Proteine) sensitivity in peripheral tissue through inhibition of KSR1 (zeige KSR1 Proteine)
ROCK1 (zeige ROCK1 Proteine)/PAR-1b-dependent regulation of basement membrane placement is required for the coordination of tissue polarity and the elaboration of tissue structure in the developing submandibular salivary gland.
PAR1b plays a novel role in the maintenance of mature dendritic spine morphology by regulating microtubule growth and the accumulation of p140Cap (zeige SRCIN1 Proteine) in dendritic spines.
Par-1b is a regulator of glucose metabolism and adiposity in the whole animal
Interaction of MARK2 with CaMKI (zeige CAMK1 Proteine) results in a novel, calcium-dependent pathway that plays an important role in neuronal differentiation.
Akt (zeige AKT1 Proteine) enhances the activity of PAR1 (zeige F2R Proteine) to promote tau hyperphosphorylation at S262/S356, a tau species that is not recognized by the CHIP/Hsp90 (zeige HSP90 Proteine) complex
Coreduction of MARK2 and DCX (zeige DCX Proteine) resulted in a partial restoration of the normal neuronal migration phenotype in vivo. The kinetic behavior of the centrosomes reflected the different molecular mechanisms activated when either protein was reduced.
This gene encodes a member of the Par-1 family of serine/threonine protein kinases. The protein is an important regulator of cell polarity in epithelial and neuronal cells, and also controls the stability of microtubules through phosphorylation and inactivation of several microtubule-associating proteins. The protein localizes to cell membranes. Multiple transcript variants encoding different isoforms have been found for this gene.
ELKL motif kinase 1
, PAR1 homolog b
, Ser/Thr protein kinase PAR-1B
, serine/threonine protein kinase EMK
, serine/threonine-protein kinase MARK2
, serine/threonine kinase