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Rabbit Anti-RACK1 Recombinant Antibody (D59D5) (CBMAB-R1023-CN)

This product is a Rabbit antibody that recognizes RACK1. The antibody D59D5 can be used for immunoassay techniques such as: WB, IP.
See all RACK1 antibodies

Summary

Host Animal
Rabbit
Specificity
Human, Mouse, Rat, Monkey
Clone
D59D5
Antibody Isotype
IgG
Application
WB, IP

Basic Information

Specificity
Human, Mouse, Rat, Monkey
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Target

Full Name
Receptor For Activated C Kinase 1
Introduction
RACK1 (Receptor For Activated C Kinase 1) is a Protein Coding gene. Diseases associated with RACK1 include Wells Syndrome. Among its related pathways are TNF signaling (REACTOME) and IGF1 pathway.
Entrez Gene ID
Human10399
Mouse14694
Rat83427
Monkey708526
UniProt ID
HumanP63244
MouseP68040
RatP63245
MonkeyG7MV11
Alternative Names
Receptor For Activated C Kinase 1; Guanine Nucleotide Binding Protein (G Protein), Beta Polypeptide 2-Like 1; Guanine Nucleotide-Binding Protein Subunit Beta-Like Protein 12.3; Guanine Nucleotide-Binding Protein Subunit Beta-2-Like 1; Cell Proliferation-Inducing Gene 21 Protein; Small Ribosomal Subunit Protein RACK1; Human Lung Cancer Oncogene 7 Protein; GNB2L1; HLC-7; Protein Homologous To Chicken B Complex Protein, Guanine Nucleotide Binding;
Function
Scaffolding protein involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes. Component of the 40S ribosomal subunit involved in translational repression (PubMed:23636399).
Involved in the initiation of the ribosome quality control (RQC), a pathway that takes place when a ribosome has stalled during translation, by promoting ubiquitination of a subset of 40S ribosomal subunits (PubMed:28132843).
Binds to and stabilizes activated protein kinase C (PKC), increasing PKC-mediated phosphorylation. May recruit activated PKC to the ribosome, leading to phosphorylation of EIF6. Inhibits the activity of SRC kinases including SRC, LCK and YES1. Inhibits cell growth by prolonging the G0/G1 phase of the cell cycle. Enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional activity of the BMAL1-CLOCK heterodimer. Facilitates ligand-independent nuclear translocation of AR following PKC activation, represses AR transactivation activity and is required for phosphorylation of AR by SRC. Modulates IGF1R-dependent integrin signaling and promotes cell spreading and contact with the extracellular matrix. Involved in PKC-dependent translocation of ADAM12 to the cell membrane. Promotes the ubiquitination and proteasome-mediated degradation of proteins such as CLEC1B and HIF1A. Required for VANGL2 membrane localization, inhibits Wnt signaling, and regulates cellular polarization and oriented cell division during gastrulation. Required for PTK2/FAK1 phosphorylation and dephosphorylation. Regulates internalization of the muscarinic receptor CHRM2. Promotes apoptosis by increasing oligomerization of BAX and disrupting the interaction of BAX with the anti-apoptotic factor BCL2L. Inhibits TRPM6 channel activity. Regulates cell surface expression of some GPCRs such as TBXA2R. Plays a role in regulation of FLT1-mediated cell migration. Involved in the transport of ABCB4 from the Golgi to the apical bile canalicular membrane (PubMed:19674157).
Promotes migration of breast carcinoma cells by binding to and activating RHOA (PubMed:20499158).
(Microbial infection) Binds to Y.pseudotuberculosis yopK which leads to inhibition of phagocytosis and survival of bacteria following infection of host cells.
(Microbial infection) Enhances phosphorylation of HIV-1 Nef by PKCs.
(Microbial infection) In case of poxvirus infection, remodels the ribosomes so that they become optimal for the viral mRNAs (containing poly-A leaders) translation but not for host mRNAs.
(Microbial infection) Contributes to the cap-independent internal ribosome entry site (IRES)-mediated translation by some RNA viruses.
Biological Process
Biological Process activation of cysteine-type endopeptidase activity involved in apoptotic processManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process cell cycleIEA:UniProtKB-KW
Biological Process cellular response to glucose stimulusManual Assertion Based On ExperimentIDA:ParkinsonsUK-UCL
Biological Process cellular response to growth factor stimulusManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process cytoplasmic translation1 PublicationIC:ComplexPortal
Biological Process gastrulationIEA:UniProtKB-KW
Biological Process negative regulation of cell growthManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process negative regulation of endoplasmic reticulum unfolded protein responseManual Assertion Based On ExperimentTAS:ParkinsonsUK-UCL
Biological Process negative regulation of gene expressionManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process negative regulation of hydrogen peroxide-induced neuron deathManual Assertion Based On ExperimentIGI:ParkinsonsUK-UCL
Biological Process negative regulation of peptidyl-serine phosphorylationManual Assertion Based On ExperimentIMP:ParkinsonsUK-UCL
Biological Process negative regulation of phagocytosisManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process negative regulation of protein bindingManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process negative regulation of protein kinase B signalingManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process negative regulation of smoothened signaling pathwayManual Assertion Based On ExperimentIDA:FlyBase
Biological Process negative regulation of translationISS:UniProtKB
Biological Process negative regulation of Wnt signaling pathwayISS:UniProtKB
Biological Process pigmentationIEA:Ensembl
Biological Process positive regulation of apoptotic processManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process positive regulation of cell migrationManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process positive regulation of cyclic-nucleotide phosphodiesterase activityManual Assertion Based On ExperimentIMP:BHF-UCL
Biological Process positive regulation of gastrulationISS:UniProtKB
Biological Process positive regulation of Golgi to plasma membrane protein transportManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process positive regulation of GTPase activityManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process positive regulation of intrinsic apoptotic signaling pathwayManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process positive regulation of mitochondrial depolarizationManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process positive regulation of proteasomal ubiquitin-dependent protein catabolic processManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process positive regulation of protein phosphorylationManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process positive regulation of protein-containing complex assemblyManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process protein ubiquitinationManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process regulation of cell cycleManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process regulation of cell divisionISS:UniProtKB
Biological Process regulation of establishment of cell polarityISS:UniProtKB
Biological Process regulation of protein localizationISS:UniProtKB
Biological Process rescue of stalled ribosomeManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process rhythmic processIEA:UniProtKB-KW
Cellular Location
Cell membrane
Cytoplasm
Cytoplasm, perinuclear region
Nucleus
Perikaryon
Cell projection, dendrite
Cell projection, phagocytic cup
Recruited to the plasma membrane through interaction with KRT1 which binds to membrane-bound ITGB1 (PubMed:17956333).
Also associated with the membrane in oncogene-transformed cells (PubMed:11884618).
PKC activation induces translocation from the perinuclear region to the cell periphery (PubMed:11279199).
In the brain, detected mainly in cell bodies and dendrites with little expression in axonal fibers or nuclei (By similarity).
Localized to phagocytic cups following infection by Y.pestis (PubMed:21347310).
PTM
Phosphorylated on Tyr-228 and/or Tyr-246 by SRC. This is required for binding to SRC.
(Microbial infection) Phosphorylated by vaccinia virus B1 kinase on serine and threonine residues; this phosphorylation remodels the ribosome properties, favoring the viral mRNA translation.
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For research use only. Not intended for any clinical use.

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