PPP1R9B / Neurabin-2 Recombinant Protein | PPP1R9B recombinant protein

Human PPP1R9B / Neurabin-2 Recombinant Protein

• Applications: ELISA, Western Blot
• Purity: >95% by SDS-PAGE
• Synonyms: PPP1R9B / Neurabin-2; Human PPP1R9B / Neurabin-2 Recombinant Protein; Neurabin-2; Neurabin-II; Protein phosphatase 1 regulatory subunit 9B; Spinophilin; PPP1R6; PPP1R9B recombinant protein

• Host: E Coli
• Purity/Purification: >95% by SDS-PAGE
• Form/Format: Liquid; 50mM NaH2PO4, 500mM NaCl Buffer with 500mM Imidazole, 10% Glycerol (PH8.0)
• Concentration: Reconstitution Dependent (varies by lot)
• Sequence Length: 815

• Applicable Applications for PPP1R9B recombinant protein: ELISA (EIA), Western Blot (WB), Antigen Protein (AP), Protein Array
• Species: Human
• Tag: His
• Subunit: Interacts with DCLK2 (By similarity). Possibly exists as a homodimer, homotrimer or a homotetramer. Interacts with F-actin, PPP1CA, neurabin-1, TGN38 and D(2) dopamine receptor. Interacts with RGS1, RGS2, RGS4, RGS19 and ADRA1B, ADRA2A, ADRA2B, ADRA2C, CDKN2A, PPP1R2, RASGFR1 and TIAM1. Interacts (via C-terminus) with SPATA13 (via C-terminal tail). Interacts with ADRA2B.
• Entry Function: Seems to act as a scaffold protein in multiple signaling pathways. Modulates excitatory synaptic transmission and dendritic spine morphology. Binds to actin filaments (F-actin) and shows cross-linking activity. Binds along the sides of the F-actin. May play an important role in linking the actin cytoskeleton to the plasma membrane at the synaptic junction. Believed to target protein phosphatase 1/PP1 to dendritic spines, which are rich in F-actin, and regulates its specificity toward ion channels and other substrates, such as AMPA-type and NMDA-type glutamate receptors. Plays a role in regulation of G-protein coupled receptor signaling, including dopamine D2 receptors and alpha-adrenergic receptors. May establish a signaling complex for dopaminergic neurotransmission through D2 receptors by linking receptors downstream signaling molecules and the actin cytoskeleton. Binds to ADRA1B and RGS2 and mediates regulation of ADRA1B signaling. May confer to Rac signaling specificity by binding to both, RacGEFs and Rac effector proteins. Probably regulates p70 S6 kinase activity by forming a complex with TIAM1 (By similarity). Required for hepatocyte growth factor (HGF)-induced cell migration.
• Preparation and Storage: Store at -20 degree C. Avoid repeated freezing and thawing.

NCBI and Uniprot Product Information

• NCBI GI #: 90101416
• UniProt Accession #: Q96SB3
• NCBI Official Full Name: Neurabin-2
• UniProt Protein Name: Neurabin-2
• Protein Family: Neurabin
• UniProt Gene Name: PPP1R9B
• UniProt Synonym Gene Names: PPP1R6
• UniProt Entry Name: NEB2_HUMAN

Uniprot Description

Spinophilin: actin-binding regulatory subunit of protein phosphatase 1 (PP1). The actin-binding domain of spinophilin is necessary and sufficient for targeting of spinophilin to dendrites and dendritic spines. May play a role in establishing a signaling complex for dopaminergic neurotransmission through D2 receptors by linking receptors downstream signaling molecules and the actin cytoskeleton. Interacts with p14-ARF. Contains one PDZ/DHR domain.

Protein type: Protein phosphatase, regulatory subunit; Adaptor/scaffold

Chromosomal Location of Human Ortholog: 17q21.33

Cellular Component: nucleoplasm; cortical actin cytoskeleton; adherens junction; lamellipodium; cytoplasm; dendritic spine; plasma membrane; synapse; protein phosphatase type 1 complex; filopodium

Molecular Function: protein binding; protein phosphatase inhibitor activity; actin binding; protein phosphatase 1 binding

Biological Process: regulation of synaptic transmission; regulation of protein amino acid phosphorylation; cell migration; regulation of cell growth by extracellular stimulus; filopodium formation; RNA splicing; regulation of exit from mitosis; calcium-mediated signaling; actin filament organization; regulation of cell proliferation; negative regulation of catalytic activity; dendrite development; negative regulation of cell growth; cell cycle arrest