Magic™ Anti-PAK1 + PAK2 + PAK3 polyclonal antibody (DPABH-29020)

Rabbit Anti-Rat PAK1 + PAK2 + PAK3 (Phospho T402) polyclonal antibody for WB

Specifications


Host Species
Rabbit
Antibody Isotype
IgG
Species Reactivity
Mouse, Rat, Human
Immunogen
Synthetic Phosphopeptide corresponding to amino acid residues surrounding the phospho Thr402 of rat p21 Activated Kinase 2 (PAK2). The peptide sequence used is identical in PAK1, 2 and 3.
Conjugate
Unconjugated

Applications


Application Notes
WB: 1/1000
*Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own experiment using appropriate negative and positive controls.

Target


Alternative Names
Alpha PAK; Beta PAK; Gamma PAK; Oligophrenin 3; OPHN3; p21 Activated Kinase 1 + 2 + 3

Citations


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Custom Antibody Labeling


We offer labeled antibodies using our catalogue antibody products and a broad range of intensely fluorescent dyes and labels including HRP, biotin, ALP, Alexa Fluor® dyes, DyLight® Fluor dyes, R-phycoerythrin (R-PE), at scales from less than 100 μg up to 1 g of IgG antibody. Learn More

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References


Promoting Glucose Transporter-4 vesicle Trafficking along Cytoskeletal Tracks: PAK-Ing Them Out

FRONTIERS IN ENDOCRINOLOGY

Authors: Tunduguru, Ragadeepthi; Thurmond, Debbie C.

Glucose is the principal cellular energy source in humans and maintenance of glucose homeostasis is critical for survival. Glucose uptake into peripheral skeletal muscle and adipose tissues requires the trafficking of vesicles containing glucose transporter-4 (GLUT4) from the intracellular storage compartments to the cell surface. Trafficking of GLUT4 storage vesicles is initiated via the canonical insulin signaling cascade in skeletal muscle and fat cells, as well as via exercise-induced contraction in muscle cells. Recent studies have elucidated steps in the signaling cascades that involve remodeling of the cytoskeleton, a process that underpins the mechanical movement of GLUT4 vesicles. This review is focused upon an alternate phosphoinositide-3 kinase-dependent pathway involving Ras-related C3 botulinum toxin substrate 1 signaling through the p21-activated kinase p21-activated kinase 1 and showcases related signaling events that co-regulate both the depolymerization and re-polymerization of filamentous actin. These new insights provide an enriched understanding into the process of glucose transport and yield potential new targets for interventions aimed to improve insulin sensitivity and remediate insulin resistance, pre-diabetes, and the progression to type 2 diabetes.

Effect of sphingosine-1-phosphate on L-type calcium current and Ca2+ transient in rat ventricular myocytes

MOLECULAR AND CELLULAR BIOCHEMISTRY

Authors: Egom, Emmanuel Eroume-A; Bae, James S. H.; Capel, Rebecca; Richards, Mark; Ke, Yunbo; Pharithi, Rebabonye B.; Maher, Vincent; Kruzliak, Peter; Lei, Ming

Modulation of Ca2+ homoeostasis in cardiac myocytes plays a major role in beat-to-beat regulation of heart function. Previous studies suggest that sphingosine-1-phosphate (S1P), a biologically active sphingomyelin metabolite, regulates Ca2+ handling in cardiac myocytes, but the underlying mechanism is unclear. In the present study, we tested the hypothesis that S1P-induced functional alteration of intracellular Ca2+ handling includes the L-type calcium channel current (I-Ca,I-L) via a signalling pathway involving P21-activated kinase 1 (Pak1). Our results show that, in rat ventricular myocytes, S1P (100 nM) does not affect the basal activity of I-Ca,I-L but is able to partially reverse the effect of the beta-adrenergic agonist Isoproterenol (ISO, 100 nM) on I-Ca,I-L. S1P (25 nM) also significantly prevents ISO (5 nM)-induced Ca2+ waves and diastolic Ca2+ release in these cells. Our further molecular characterisation demonstrates that Pak1 activity is increased in myocytes treated with S1P (25 nM) compared with those myocytes without treatment of S1P. By immunoprecipitation we demonstrate that Pak1 and protein phosphatase 2A (PP2A) are associated in ventricular tissue indicating their functional interaction. Thus the results indicate that S1P attenuates beta-adrenergic stress-induced alteration of intracellular Ca2+ release and L-type Ca2+ channel current at least in part via Pak1-PP2A-mediated signalling.

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