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Die folgenden MAPmates™ sollten nicht zusammen analysiert werden: -MAPmates™, die einen unterschiedlichen Assaypuffer erfordern. -Phosphospezifische und MAPmate™ Gesamtkombinationen wie Gesamt-GSK3β und Gesamt-GSK3β (Ser 9). -PanTyr und locusspezifische MAPmates™, z.B. Phospho-EGF-Rezeptor und Phospho-STAT1 (Tyr701). -Mehr als 1 Phospho-MAPmate™ für ein einziges Target (Akt, STAT3). -GAPDH und β-Tubulin können nicht mit Kits oder MAPmates™, die panTyr enthalten, analysiert werden.
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96-Well Plate
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48-602MAG
Buffer Detection Kit for Magnetic Beads
1 Kit
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ABS1520
Sigma-AldrichAnti-GRASP55 Antibody
Anti-GRASP55 Antibody is an antibody against GRASP55 for use in Western Blotting, Immunocytochemistry.
More>>Anti-GRASP55 Antibody is an antibody against GRASP55 for use in Western Blotting, Immunocytochemistry. Less<<
Anti-GRASP55 Antibody : SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
Golgi reassembly stacking protein of 55 kDa (also called Golgi reassembly-stacking protein of 55 kDa, GRASP55, or Grs2) is encoded by the gene designated as Gorasp2 in rat & mouse (GORASP2/GRS2/GOLPH6 in human). Golgi stack formation involves two homologous peripheral Golgi proteins, GRASP55 and GRASP65, localized to the medial-trans and cis cisternae, respectively. GRASP55 and GRASP65 stack mammalian Golgi cisternae via a common mechanism of phosphorylation-regulated oligomerization. GRASP55 stacks Golgi membranes by forming oligomers through its N-terminal GRASP domain. This process is regulated by phosphorylation within the C-terminal serine/proline-rich domain. Expression of nonphosphorylatable GRASP55 mutants enhances Golgi stacking in interphase cells and inhibits Golgi disassembly during mitosis. Knockdown of either GRASP55 or GRASP65 by siRNA reduces the number of cisternae per Golgi stack, while simultaneous knockdown of both GRASP proteins leads to disassembly of the entire stack. (PMID 20083603). Cat. No. ABS1520, Anti-GRASP55, is a rabbit polyclonal antiserum raised against a recombinant immunogen encompassing region within the C-terminal half of rat GRASP55.
Anti-GRASP55 Antibody is an antibody against GRASP55 for use in Western Blotting, Immunocytochemistry.
Key Applications
Western Blotting
Immunocytochemistry
Application Notes
Western Blotting Analysis: A representative lot detected GRASP55 in HeLa cell lysate (Xiang, Y., and Wang, Y. (2010). J. Cell Biol. 188(2):237-251). Western Blotting Analysis: A representative lot detected GRASP55 in CHO cells and mouse brain lysate (Joshi, G., et al (2014). PNAS. 111(13):E1230-1239). Immunocytochemistry Analysis: A representative lot detected GRASP55 in HeLa cells (Xiang, Y., and Wang, Y. (2010). J. Cell Biol. 188(2):237-251). Immunocytochemistry Analysis: A representative lot detected GRASP55 in CHO cells (Joshi, G., et al (2014). PNAS. 111(13):E1230-1239).
Biological Information
Immunogen
Recombinant protein corresponding to the C-terminal of rat GRASP55.
Epitope
C-terminal
Concentration
Please refer to lot specific datasheet.
Host
Rabbit
Species Reactivity
Mouse
Human
Hamster
Species Reactivity Note
Mouse, Human, Hamster. Predicted to react with Rat based on 100% sequence homology.
Evaluated by Western Blotting in mouse brain tissue lysate.
Western Blotting Analysis: A 1:500 dilution of this antibody detected GRASP55 in 10 µg of mouse brain tissue lysate.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage Conditions
Stable for 1 year at -20°C from date of receipt. Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.
Aβ-induced Golgi fragmentation in Alzheimer's disease enhances Aβ production. Joshi, G; Chi, Y; Huang, Z; Wang, Y Proceedings of the National Academy of Sciences of the United States of America
111
E1230-9
2014
Golgi fragmentation occurs in neurons of patients with Alzheimer's disease (AD), but the underlying molecular mechanism causing the defects and the subsequent effects on disease development remain unknown. In this study, we examined the Golgi structure in APPswe/PS1E9 transgenic mouse and tissue culture models. Our results show that accumulation of amyloid beta peptides (Aβ) leads to Golgi fragmentation. Further biochemistry and cell biology studies revealed that Golgi fragmentation in AD is caused by phosphorylation of Golgi structural proteins, such as GRASP65, which is induced by Aβ-triggered cyclin-dependent kinase-5 activation. Significantly, both inhibition of cyclin-dependent kinase-5 and expression of nonphosphorylatable GRASP65 mutants rescued the Golgi structure and reduced Aβ secretion by elevating α-cleavage of the amyloid precursor protein. Our study demonstrates a molecular mechanism for Golgi fragmentation and its effects on amyloid precursor protein trafficking and processing in AD, suggesting Golgi as a potential drug target for AD treatment.
In vitro studies have suggested that Golgi stack formation involves two homologous peripheral Golgi proteins, GRASP65 and GRASP55, which localize to the cis and medial-trans cisternae, respectively. However, no mechanism has been provided on how these two GRASP proteins work together to stack Golgi cisternae. Here, we show that depletion of either GRASP55 or GRASP65 by siRNA reduces the number of cisternae per Golgi stack, whereas simultaneous knockdown of both GRASP proteins leads to disassembly of the entire stack. GRASP55 stacks Golgi membranes by forming oligomers through its N-terminal GRASP domain. This process is regulated by phosphorylation within the C-terminal serine/proline-rich domain. Expression of nonphosphorylatable GRASP55 mutants enhances Golgi stacking in interphase cells and inhibits Golgi disassembly during mitosis. These results demonstrate that GRASP55 and GRASP65 stack mammalian Golgi cisternae via a common mechanism.
