Anti-RACK1 GNB2L1 Antibody Picoband®

Guanine nucleotide-binding protein subunit beta-2-like 1, also known as RACK1 is a 32kDa protein that in humans is encoded by the GNB2L1 gene. It is mapped to 5q35.3. GNB2L1 is a major component of translating ribosomes, which harbor significant amounts of PKC. This gene can provide a physical and functional link between PKC signaling and ribosome activation. GNB2L1 is also a mediator of agonist-induced Ca (2+) release. What’ s more, GNB2L1 is an essential component of an oxygen-independent mechanism for regulating HIF1A stability. Overexpression of GNB2L1 and PKC-alpha suppressed CLOCK-BMAL1 transcriptional activity, and GNB2L1 stimulated phosphorylation of BMAL1 by PKC-alpha in vitro.

Guanine nucleotide-binding protein subunit beta-2-like 1; Cell proliferation-inducing gene 21 protein; Guanine nucleotide-binding protein subunit beta-like protein 12.3; Human lung cancer oncogene 7 protein; HLC-7; Receptor for activated C kinase; Receptor of activated protein kinase C 1; RACK1; Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed; GNB2L1; HLC7, PIG21

E.coli-derived human RACK1 recombinant protein (Position: T2-R317) . Human RACK1 shares 100% amino acid (aa) sequence identity with both mouse and rat RACK1.

In the liver, expressed at higher levels in activated hepatic stellate cells than in hepatocytes or Kupffer cells. Up-regulated in hepatocellular carcinomas and in the adjacent non-tumor liver tissue. .

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. 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. Binds to Y.pseudotuberculosis yopK which leads to inhibition of phagocytosis and survival of bacteria following infection of host cells. Enhances phosphorylation of HIV-1 Nef by PKCs. Promotes migration of breast carcinoma cells by binding to and activating RHOA. .

Store at -20°C for one year from date of receipt. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for six months. Avoid repeated freeze-thaw cycles.

Cell membrane; Peripheral membrane protein. Cytoplasm. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton. Nucleus. Perikaryon . Cell projection, dendrite . Cell projection, phagocytic cup. Recruited to the plasma membrane through interaction with KRT1 which binds to membrane-bound ITGB1. Also associated with the membrane in oncogene-transformed cells. PKC activation induces translocation from the perinuclear region to the cell periphery. In the brain, detected mainly in cell bodies and dendrites with little expression in axonal fibers or nuclei. Localized to phagocytic cups following infection by Y.pestis.