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Merck

N5037

Sigma-Aldrich

Anti-Neurabin II (C-terminal) antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonym(e):

Anti-Neural-tissue Specific F-actin Binding Protein II, Anti-PP1bp134, Anti-Protein Phosphatase 1 Regulatory Subunit 9B, Anti-Spinophilin

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About This Item

MDL-Nummer:
UNSPSC-Code:
12352203
NACRES:
NA.43

Biologische Quelle

rabbit

Konjugat

unconjugated

Antikörperform

affinity isolated antibody

Antikörper-Produkttyp

primary antibodies

Klon

polyclonal

Form

buffered aqueous solution

Mol-Gew.

antigen 140 kDa

Speziesreaktivität

rat, mouse, canine

Methode(n)

immunoprecipitation (IP): 10-20 μg using rat brain extract (S1 fraction)
indirect immunofluorescence: 10-20 using MDCK cells.
microarray: suitable
western blot: 1-2 μg/mL using mouse and rat brain extracts (S1 fraction)

UniProt-Hinterlegungsnummer

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

Allgemeine Beschreibung

Neurabin II belongs to a family of F-actin-binding proteins, highly enriched in dendritic spines and involved in neurite formation. It consists of an F-actin binding domain at the N-terminus, a single PDZ-interacting-domain and a C-terminal coiled-coil domain.

Immunogen

synthetic peptide corresponding to amino acids 800-817 located at the C-terminal region of rat neurabin II. The sequence is identical in human and mouse neurabin II and not found in neurabin I.

Anwendung

Anti-Neurabin II (C-terminal) antibody has been used in
  • immunoblotting
  • immunoprecipitation
  • immunocytochemistry

Biochem./physiol. Wirkung

Neurabins appear to function as bridging proteins by targeting other proteins to the synapse or by linking plasma membrane proteins to the actin cytoskeleton. Neurabin II binds to several proteins including F-actin, protein phosphatase 1 (PP1), at least two subfamilies of G-protein coupled receptors (GPCRs), the α2 adrenergic receptor (α2AR) subtypes and the D2 dopamine receptor. Neurabin II blocks arrestin function in vitro and in vivo at GPCRs and has been also shown to modulate, in vitro and in vivo, both glutaminergic synaptic transmission and the formation and function of dendritic spines. Neurabin II and neurabin I target PP1 subunits that are highly concentrated in dendritic spines and post-synaptic densities. Phosphorylation of neurabin II modulates its interaction with actin filaments, via the anchoring of the neurabin II-PP1 complex within dendritic spines, thereby contributing to the efficacy and plasticity of synaptic transmission.

Physikalische Form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Haftungsausschluss

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.

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Lagerklassenschlüssel

10 - Combustible liquids

WGK

nwg

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


Analysenzertifikate (COA)

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Die Dokumentenbibliothek aufrufen

Neurabin-II/spinophilin an actin filament-binding protein with one pdz domain localized at cadherin-based cell-cell adhesion sites
Satoh A, et al.
The Journal of Biological Chemistry, 273(6), 3470-3475 (1998)
The neuronal actin-binding proteins, neurabin I and neurabin II, recruit specific isoforms of protein phosphatase-1 catalytic subunits
Terry-Lorenzo R T, et al.
Test, 277(31), 27716-27724 (2002)
Reduced dendritic spine density in auditory cortex of subjects with schizophrenia
Sweet R A, et al.
Neuropsychopharmacology, 34(2), 374-374 (2009)
The human tumor suppressor arf interacts with spinophilin/neurabin II, a type 1 protein-phosphatase-binding protein
Vivo M, et al.
Test, 276(17), 14161-14169 (2001)
Different behavior of l-afadin and neurabin-II during the formation and destruction of cell-cell adherens junction
Sakisaka T, et al.
Oncogene, 18(8), 1609-1609 (1999)

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