20% off purchase of 3 or more products* | Learn More >>

Product listing: GKAP Antibody, UniProt ID O14490 #13602 to Gα(i) Antibody, UniProt ID P63096 #5290

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Western Blotting

Background: Guanylate kinase-associated protein (GKAP, DLGAP1 or SAPAP1) is part of the postsynaptic scaffolding complex that includes the PSD-95, SAP90, and SHANK proteins (1-3). GKAP links the synaptic protein SHANK to a PSD-95 complex that includes NMDA glutamate receptors (3,4). Synaptic activity induces ubiquitination of GKAP protein by the E3 ubiquitin ligase TRIM3, which results in decreased GKAP protein levels through degradation (5,6). GKAP protein turnover is regulated by a CaMKII-dependent, bidirectional mechanism. Synaptic over-excitation leads to CaMKIIα-mediated GKAP phosphorylation at Ser346, which induces polyubiquitination of GKAP and removal of the scaffold protein from synapses. In contrast, during low-level synaptic activity CaMKIIβ phosphorylates GKAP, which triggers dissociation of GKAP from the motor protein complex responsible for GKAP transport to the base of the synapse and its subsequent incorporation into the postsynaptic density (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Glycine decarboxylase (GLDC) is a component of a mitochondrial protein complex that catalyzes the degradation of glycine (1). The glycine cleavage system is composed of three distinct enzymes (P-, T- and L-proteins) and an additional component (H-protein) that transfers a glycine methylamine group from one enzyme to another. The GLDC protein (P-protein) is the decarboxylase that binds the methylamine group for transfer to the T-protein (2). Tumor-initiating cells in the primary non-small cell lung cancer (NSCLC) express high levels of GLDC and LIN28B, both of which are essential for the proliferation of tumor-initiating cells (3). GLDC is an oncogene that promotes tumorigenesis through its metabolic activity (3). Mutations in the corresponding GLDC gene account for the majority of reported cases of glycine encephalopathy, which is a metabolic disorder characterized by the accumulation of glycine, lethargy, hypotonia, intractable seizures, and death (4).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: GLI was first identified as a gene amplified in a malignant glioma (1) capable of transforming primary cells in cooperation with adenovirus E1A (2). GLI belongs to the Kruppel family of zinc finger proteins that includes three mammalian GLI proteins: GLI1, GLI2, and GLI3 (3). These GLI proteins are similar to the Drosophila homolog Cubitus interruptus (Ci) and function as transcription factors activated by the Hedgehog signaling pathway. Hedgehog signaling plays an important role in animal development, and research studies have shown that this pathway is aberrantly activated in many types of cancers (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: GLI was first identified as a gene amplified in a malignant glioma (1) capable of transforming primary cells in cooperation with adenovirus E1A (2). GLI belongs to the Kruppel family of zinc finger proteins that includes three mammalian GLI proteins: GLI1, GLI2, and GLI3 (3). These GLI proteins are similar to the Drosophila homolog Cubitus interruptus (Ci) and function as transcription factors activated by the Hedgehog signaling pathway. Hedgehog signaling plays an important role in animal development, and research studies have shown that this pathway is aberrantly activated in many types of cancers (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: GLI was first identified as a gene amplified in a malignant glioma (1) capable of transforming primary cells in cooperation with adenovirus E1A (2). GLI belongs to the Kruppel family of zinc finger proteins that includes three mammalian GLI proteins: GLI1, GLI2, and GLI3 (3). These GLI proteins are similar to the Drosophila homolog Cubitus interruptus (Ci) and function as transcription factors activated by the Hedgehog signaling pathway. Hedgehog signaling plays an important role in animal development, and research studies have shown that this pathway is aberrantly activated in many types of cancers (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Glioma tumor suppressor candidate region gene 2 protein (GLTSCR2), also known as protein interacting with carboxyl terminus-1 (PICT-1), displays tumor suppressor activity, in part, by interacting with the C-terminal region of PTEN and preventing its degradation. Disruption of this interaction upregulates activity of the PI3K/Akt signaling axis and promotes cell transformation (1,2). Further evidence to support the tumor suppressor role of GLTSCR2 lies in the finding that GLTSCR2 is localized to the tumor suppressive region of chromosome 19q, which is subject to lesions in human brain tumors (3). Indeed, research studies have demonstrated that GLTSCR2 harbors nonsense mutations and deletions in glioblastomas, which lead to a decrease in GLTSCR2 protein expression (4). GLTSCR2 has also been shown to exert tumor suppressor activity through its involvement in the nucleolar stress response. Research studies indicate that in response to ribosomal stress, GLTSCR2 translocates from the nucleolus to the nucleoplasm where it binds and stabilizes p53 tumor suppressor, which results in inhibition of cell cycle progression (5).

$260
100 µl
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: Epitope tags are useful for the labeling and detection of proteins using immunoblotting, immunoprecipitation, and immunostaining techniques. Because of their small size, they are unlikely to affect the tagged protein’s biochemical properties.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Immunohistochemistry (Frozen), Immunohistochemistry (Paraffin)

Background: Glucose homeostasis is regulated by a variety of hormones including glucagon. Glucagon is synthesized as the precursor molecule proglucagon and is proteolytically processed to yield the mature peptide in α cells of the pancreatic islets. Glucagon causes the release of glucose from glycogen and stimulates gluconeogenesis in the liver (1,2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Glucose-6-phosphate dehydrogenase (G6PD) catalyses the first, and rate-limiting, step of the pentose phosphate pathway (1). The NADPH generated from this reaction is essential to protect cells from oxidative stress (1). Research studies have shown that p53 interacts with G6PD and inhibits its activity, therefore suppressing glucose consumption through the pentose phosphate pathway (2). In cancer cells with p53 mutations, the increased glucose consumption is directed towards increased biosynthesis, which is critical for cancer cell proliferation (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Glutaminase catalyzes the conversion of glutamine to glutamate, the first and rate-limiting step of glutaminolysis (1). Both kidney-type glutaminase (GLS1) and liver-type glutaminase (GLS2) are found in mammals (2). GLS1-mediated glutathione synthesis plays an essential role in redox homeostasis and contributes to increased survival of postimplantation bone cells preconditioned to the hypoxic and ischemic environment in the bone defect site (3). In addition, KEAP1–NRF2-mutant LUAD (KRAS-mutant lung adenocarcinoma) tumors are dependent on increased glutaminolysis (1). Furthermore, recent studies showed higher glutaminolysis and glucose production from glutamine in human primary hepatocytes with GLS2 gain-of-function missense mutations (4). These findings suggest GLS1 and GLS2 as potential targets in the therapy of bone regeneration and in the treatments to diseases such as cancer and hyperglycemia, respectively (1, 3-4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry, Immunoprecipitation, Western Blotting

Background: Glycogen is a polysaccharide of glucose and serves as an energy storage in mammalian muscle and liver (1). Glycogen synthase catalyzes the rate-limiting step of glycogen biosynthesis and has two major isoforms in mammals -- muscle isoform (GYS1) and liver isoform (GYS2) respectively (1). Glycogen synthase kinase-3α (GSK-3α) and glycogen synthase kinase-3β (GSK-3β) phosphorylate glycogen synthase at multiple sites in its C-terminus (Ser641, Ser645, Ser649 and Ser653) inhibiting its activity (2, 3). Hypoxia alters glycogen metabolism including temporal changes of GYS1 expression and phosphorylation in cancer cells, suggesting the role of metabolic reprogramming of glycogen metabolism in cancer growth (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Guanine monophosphate synthase (GMPS) catalyzes the conversion of xanthosine 5’-monophosphate (XMP) into GMP during the final step of de novo guanine nucleotide synthesis. In addition to comprising the building blocks for DNA and RNA, guanine nucleotides also provide GTP for many signaling pathways that are important for multiple cellular processes (1). Chromosomal translocations involving MLL and GMPS is reported in some patients diagnosed with acute myeloid leukemia (2). Research studies indicate that genotoxic stress or nucleotide deprivation prompts translocation of GMPS to the nucleus where it complexes with USP7 and p53 to promote p53 stabilization (3). Additional studies show that the nuclear GMPS-USP7 protein complex deubiquitinates histone H2B in Drosophila (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Heterotrimeric guanine nucleotide-binding proteins, G proteins, transduce ligand binding to G protein-coupled receptors (GPCRs) into intracellular responses (1). G proteins are comprised of 3 subunits, alpha (Gα), beta (Gβ), and gamma (Gγ). Upon activation of GPCRs, the receptor promotes the exchange of GDP to GTP of Gα, changing the confirmation of the switch regions within Gα. The receptor bound heterotimeric G protein (inactive) is then released, and dissociates into the GTP-bound Gα (active) monomer and the Gβ/Gγ heterodimer (1,2). Gα activates adenylyl cyclase, which converts ATP to the second messenger cAMP. Gα also activates phosphoinositide-specific phospholipase C (PLC), which catalyzes hydrolysis of the phospholipid of phosphatidylinositol 4,5-biphosphate (PIP2), releasing the second messengers IP3 and 1,2-diacylglycerol (DAG). IP3 activates IP3 receptors to release Ca2+ from the ER. DAG is an activator of protein kinase C (PKC), which in turn activates the Erk1/2 pathway (1,3). The primary function of the Gβ/Gγ heterodimer is to inhibit Gα, although it may also activate second messengers (e.g. PLC pathway) or gate ion channels (e.g. GIRK) (1). Guanine nucleotide-binding protein b3 (GNB3) is an isoform of the b subunit. Research studies have shown that a polymorphism in the GNB3 gene, C825T, is associated with hypertension, obesity, and depression (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: GP130 is a signal-transducing subunit shared by the receptors for the IL-6 family of cytokines (1-3). The binding of a ligand to its receptor induces the dimerization of GP130, leading to activation of the Jak tyrosine kinase and to tyrosine phosphorylation of GP130. These events lead to the activation of multiple signal-transduction pathways, such as the Stat, Ras-MAPK and PI3 kinase pathways, whose activation is controlled by distinct regions of GP130 (4-7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: Glucose-6-phosphate isomerase (GPI) is a multi-functional protein belonging to the glucose phosphate isomerase family (1,2). As an intracellular metabolic enzyme, GPI plays a pivotal role in glycolysis and gluconeogenesis by catalyzing the interconversion of D-glucose-6-phosphate and D-fructose-6-phosphate (3). GPI is also secreted, where it functions as a cytokine (referred to as Autocrine Motility Factor, AMF), acting via the E3-ubiquitin-protein ligase AMFR/gp78 (4). In normal tissues, GPI/AMF has been shown to promote both immune cell maturation and neuronal cell survival (5,6). It is also secreted in abundance by some tumor cells (7), where it has been shown to promote tumor cell migration and metastasis (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Glutathione peroxidase 1 (GPX1) is a cytosolic selenoprotein which reduces hydrogen peroxide to water (1). GPX1 is the most abundant and ubiquitous among the five GPX isoforms identified so far (2). It is an important component in the anti-oxidative defense in cells and is associated with a variety of disease conditions, such as colon cancer (3), coronary artery disease (4) and insulin resistance (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: GTPase Regulator Associated with Focal Adhesion Kinase-1 (GRAF1), is a GTPase-activating protein for the small G proteins RhoA and Cdc42 (1). It is composed of an N-terminal BAR domain, a PH domain, a RhoGAP domain, a proline-rich domain, and a C-terminal SH3 domain. GRAF1 contributes to the clathrin-independent carriers/GPI-enriched early endosomal compartments (CLIC/GEEC) pathway, and was the first specific protein component of this endocytic pathway to be discovered (2). GRAF1 was identified as an important protein necessary for adeno-associated virus 2 infection (3). In addition, research studies have linked GRAF1 to mental retardation (4), skeletal muscle differentiation (5), and myeloid leukemia (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Peptide ELISA (DELFIA), Western Blotting

Background: Granzymes are a family of serine proteases expressed by cytotoxic T lymphocytes and natural killer (NK) cells and are key components of immune responses to pathogens and transformed cells (1). Granzymes are synthesized as zymogens and are processed into mature enzymes by cleavage of a leader sequence. They are released by exocytosis in lysosome-like granules containing perforin, a membrane pore-forming protein. Granzyme B has the strongest apoptotic activity of all the granzymes as a result of its caspase-like ability to cleave substrates at aspartic acid residues thereby activating procaspases directly and cleaving downstream caspase substrates (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Peptide ELISA (DELFIA), Western Blotting

Background: Granzymes are a family of serine proteases expressed by cytotoxic T lymphocytes and natural killer (NK) cells and are key components of immune responses to pathogens and transformed cells (1). Granzymes are synthesized as zymogens and are processed into mature enzymes by cleavage of a leader sequence. They are released by exocytosis in lysosome-like granules containing perforin, a membrane pore-forming protein. Granzyme B has the strongest apoptotic activity of all the granzymes as a result of its caspase-like ability to cleave substrates at aspartic acid residues thereby activating procaspases directly and cleaving downstream caspase substrates (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The GRB7 family of adaptor proteins consist of GRB7, GRB10 and GRB14, which all contain an amino-terminal proline-rich SH3 binding domain, followed by PH, PBS, and SH2 domains. Each member of the family has several splice variants (1). It has been reported that GRB10 interacts with many receptor tyrosine kinases (RTKs) as well as downstream signal molecules including Raf, Akt, and Nedd4 (1,2). Although it was originally thought that GRB10 is exclusively phosphorylated at serine residues (3), Src kinase family members have been shown to phosphorylate GRB10 at Tyr67 (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Bovine, Hamster, Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Growth factor receptor-binding protein 2 (GRB2) is an adaptor protein that is involved in RTK signal transduction. The SH2 domain of GRB2 binds to tyrosine phosphorylated proteins such as EGFR, IRS-1, Shc and Gab1 (1). The SH3 domain of GRB2 associates with Sos, which stimulates the GTP binding activity of Ras, leading to the activation of the MAP kinase and other signaling pathways. Phosphorylation of Tyr209 of GRB2 by Bcr-Abl and EGFR abolishes its association with Sos and negatively regulates downstream signaling (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: Gremlin is a secreted antagonist of bone morphogenetic proteins that play important roles during development. Gene targeting generates gremlin deficient mice that die shortly after birth due to absent kidneys and defects in lung septation (1-3). Gremlin also plays a role in cardiomyogenesis and angiogenesis (4,5). TGF-β can induce gremlin expression under pathological conditions. Gremlin colocalizes with TGF-β in tubulointerstitial fibrosis associated with chronic allograft nephropathy and is expressed in diabetic nephropathy in vivo (6-8). Gremlin is widely expressed in cancer associated stromal cells and can enhance cancer cell proliferation (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: G-protein-coupled receptor kinase 2 (GRK2), also known as beta-adrenergic receptor kinase 1 (beta-ARK1), is a member of the GRK family, which phosphorylates the activated form of G-protein-coupled receptors (GPCRs) and initiates the desensitization process of GPCR (1). GRK2 kinase activity and cellular localization are tightly regulated by interactions with activated receptors, G-beta and G-gamma subunits, adaptor proteins, phospholipids, caveolin and calmodulin, as well as by phosphorylation (1). PKC phosphorylation enhances GRK2 activity by promoting its membrane localization and by abolishing the inhibitory association of calmodulin (2,3). PKA phosphorylates GRK2 at Ser685, which facilitates the association of GRK2 with a beta-adrenergic receptor (4). Erk inhibits GRK2 activity via phosphorylation at Ser670 (5). Src phosphorylates GRK2 at multiple tyrosine residues (Tyr13, 86 and 92), which activates GRK2 activity and promotes GRK2 degradation (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Grp75, also known as mortalin, is a member of Hsp70 family of chaperone proteins that is not heat-inducible (1,2). This protein is essential for transporting many mitochondrial proteins from the cytoplasm to mitochondria (3). Grp75 inactivates the tumor suppressor p53 (4). Studies found that Grp75 is overexpressed in many tumor tissues and immortalized human cell lines, suggesting its role in the tumor formation (5). Grp75 is also implicated in cell aging, as its overexpression appears to prolong the life span of human fibroblasts (6).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Secretory proteins are synthesized on polysomes and translocated into the endoplasmic reticulum (ER). Inside ER, these proteins are often modified by disulfide bond formation, amino-linked glycosylation and folding. The ER contains a pool of molecular chaperones, including Grp94, to help ensure correct protein folding. Grp94 is a glucose-regulated protein (1) with sequence homology to Hsp90 (2). In addition to its role in helping to facilitate folding of a number of secretory proteins to their correct conformation (3), studies suggest that Grp94 derived from cancer cells also induces anti-tumor immune responses in mouse tumor models (4, 5). One way in which Grp94 promotes tumor immunogenicity is its ability to bind to and present tumor-derived peptides as antigens (6). Furthermore, Grp94 has also been shown to induce maturation of dendritic cells (7). Taken together, Grp94 functions both as a tumor-specific antigen and as an activator of antigen-presenting cells to elicit an anti-cancer immune response (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Glycogen synthase kinase-3 (GSK-3) was initially identified as an enzyme that regulates glycogen synthesis in response to insulin (1). GSK-3 is a ubiquitously expressed serine/threonine protein kinase that phosphorylates and inactivates glycogen synthase. GSK-3 is a critical downstream element of the PI3K/Akt cell survival pathway whose activity can be inhibited by Akt-mediated phosphorylation at Ser21 of GSK-3α and Ser9 of GSK-3β (2,3). GSK-3 has been implicated in the regulation of cell fate in Dictyostelium and is a component of the Wnt signaling pathway required for Drosophila, Xenopus, and mammalian development (4). GSK-3 has been shown to regulate cyclin D1 proteolysis and subcellular localization (5).

$260
100 µl
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Western Blotting

Background: Epitope tags are useful for the labeling and detection of proteins using immunoblotting, immunoprecipitation, and immunostaining techniques. Because of their small size, they are unlikely to affect the tagged protein’s biochemical properties.

$260
100 µl
APPLICATIONS

Application Methods: Immunoprecipitation, Western Blotting

Background: Epitope tags are useful for the labeling and detection of proteins using immunoblotting, immunoprecipitation, and immunostaining techniques. Because of their small size, they are unlikely to affect the tagged protein’s biochemical properties.

$260
100 µl
APPLICATIONS
REACTIVITY
Bovine, Human, Monkey, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Heterotrimeric guanine nucleotide-binding proteins (G proteins) consist of α, β and γ subunits and mediate the effects of hormones, neurotransmitters, chemokines, and sensory stimuli. To date, over 20 known Gα subunits have been classified into four families, Gα(s), Gα(i/o), Gα(q) and Gα(12), based on structural and functional similarities (1,2). Phosphorylation of Tyr356 of Gα(q)/Gα(11) is essential for activation of the G protein, since phenylalanine substitution for Tyr356 changes the interaction of Gα with receptors and abolishes ligand-induced IP3 formation (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Heterotrimeric guanine nucleotide-binding proteins (G proteins) consist of α, β and γ subunits and mediate the effects of hormones, neurotransmitters, chemokines, and sensory stimuli. To date, over 20 known Gα subunits have been classified into four families, Gα(s), Gα(i/o), Gα(q) and Gα(12), based on structural and functional similarities (1,2). Phosphorylation of Tyr356 of Gα(q)/Gα(11) is essential for activation of the G protein, since phenylalanine substitution for Tyr356 changes the interaction of Gα with receptors and abolishes ligand-induced IP3 formation (3).