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Merck

N5037

Sigma-Aldrich

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

affinity isolated antibody, buffered aqueous solution

Sinónimos:

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 number:
UNSPSC Code:
12352203
NACRES:
NA.43

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 140 kDa

species reactivity

rat, mouse, canine

technique(s)

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 accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

General description

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.

Application

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

Biochem/physiol Actions

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.

Physical form

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

Disclaimer

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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Storage Class

10 - Combustible liquids

wgk_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Visite la Librería de documentos

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)
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)
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)
Reduced dendritic spine density in auditory cortex of subjects with schizophrenia
Sweet R A, et al.
Neuropsychopharmacology, 34(2), 374-374 (2009)

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