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Polyclonal Antibody Immunoprecipitation Regulation of Cell Growth

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Enolase is an important glycolytic enzyme involved in the interconversion of 2-phosphoglycerate to phosphoenolpyruvate. Mammalian enolase exists as three subunits: enolase-1 (α-enolase), enolase-2 (γ-enolase) and enolase-3 (β-enolase) that can form both homo- and heterodimers. Expression of the enolase isoforms differs in a tissue specific manner (1). Enolase-1 plays a key role in anaerobic metabolism under hypoxic conditions and may act as a cell surface plasminogen receptor during tissue invasion (2,3). Abnormal expression of enolase-1 is associated with tumor progression in some cases of breast and lung cancer (4-7). Alternatively, an enolase-1 splice variant (MBP-1) binds the c-myc promoter p2 and may function as a tumor suppressor. For this reason enolase-1 is considered as a potential therapeutic target in the treatment of some forms of cancer (8).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: RMP (RPB5-Mediating Protein), also known as URI (Unconventional prefoldin RBP5 Interactor), was described as an unconventional member of the prefoldin (PFD) family of chaperones that are involved in actin and tubulin folding (1-4). Like conventional members of the α-class of PFDs, RMP contains N- and C-terminal α-helical coiled-coil structures connected by two β hairpins. In addition, RMP possesses an RPB5-binding segment and a long C-terminal acidic segment. It is posited that RMP exists as a component of a macromolecular complex within human cells and functions as a molecular scaffold to assemble a PFD complex containing other PFDs and proteins with functions in transcription and ubiquitination. Indeed, evidence is provided that RMP negatively modulates RNA polymerase II-dependent transcription by binding to TFIIF (5) and RBP5 (6) and is involved in mTOR signaling by coordinating the regulation of nutrient availability with gene expression (1). In accord with its ability to coordinate gene expression with nutrient availability, RMP was shown to be a mitochondrial substrate of S6K1. S6K1-mediated phosphorylation of RMP at Ser371 triggers a series of biochemical events that constitute a negative feedback loop, in part, aimed at restraining S6K1 survival signaling and ensuring that the mitochondrial threshold for apoptosis corresponds to availability of nutrients and growth factors (7).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The NDRG (N-Myc downstream-regulated gene) family consisting of NDRG1, NDRG2, NDRG3, and NDRG4 are structurally related proteins with roles in cell proliferation, differentiation, apoptosis, stress responses, and cell migration/metastasis (1-3). NDRG1 was originally identified as a protein that was upregulated in N-Myc knockout mice (1). Proteins in the NDRG family, particularly NDRG1 and NDRG2, have been reported to be down-regulated in various cancer tissues and have been suggested to function as a tumor suppressors (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Insulin-like growth factor-binding proteins (IGFBPs) play an integral role in modifying insulin-like growth factor (IGF) actions in a wide variety of cell types. This family contains six members that are structurally related but encoded by distinct genes. IGFBPs have a high affinity for IGFs. Some members of the IGFBP family have been consistently shown to inhibit IGF actions by preventing them from gaining access to the IGF receptors, while others potentiate IGF actions by facilitating the ligand-receptor interaction (1-3). IGFBP2 is the second most abundant IGFBP in the circulation and is present in various other biological fluids and tissues of many vertebrate species. Serum IGFBP2 levels are elevated in conditions such as shock, fasting, hypoxemia or after traumata, suggesting complex regulation of IGFBP2 expression (4). IGFBP2 is overexpressed in many malignancies and is often correlated with an increasingly malignant status of the tumor, pointing to a potential involvement of IGFBP2 in tumorigenesis (5).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: BAP1 (BRCA1-Associated Protein 1) was originally identified as a BRCA1 associated, nuclear localized ubiquitin hydrolase that suppresses cell growth (1). The protein belongs to the UCH family of deubiquitinases, with a UCH domain in its N-terminal segment and a BRCA1 interaction domain as well as a nuclear localization signal in its C-terminal segment (1). Frequent gene locus rearrangement, deletion and null mutation of BAP1 have been found in lung and breast cancers (1,2). Mutation analysis in vivo in cancer cell line survival and in animal tumorigenesis indicate that both the deubiquitinase activity and the nuclear localization signal are required for BAP1 function as a tumor suppressor (3). BAP1 does not have direct deubiquitination activity towards the autoubiquitinyled BRCA1/BARD1 E3 complex (4), but its interaction with BARD1 inhibits BRCA1/BARD1 E3 activity by interfering with the compex dimerization process (5). In addition to its interaction with BRCA1/BARD1, BAP1 has also been shown to interact with and deubiquitinylate HCF-1, thereby controlling its stability (6).Phosphorylation of Ser592 on BAP1 was identified at Cell Signaling Technology (CST) using PhosphoScan®, CST's LC-MS/MS platform for phosphorylation site discovery (7).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The suppressor of cytokine signaling (SOCS) family members are negative regulators of cytokine signal transduction that inhibit the Jak/Stat pathway (1-3). The SOCS family consists of at least 8 members including the originally identified cytokine-inducible SH2-containing protein (CIS1), as well as SOCS1-7. Each SOCS family member contains a central SH2 domain and a conserved carboxy-terminal motif designated as the SOCS box. These proteins are important regulators of cytokine signaling, proliferation, differentiation, and immune responses.

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The discoidin domain receptors (DDRs) are receptor tyrosine kinases with a discoidin homology repeat in their extracellular domains, activated by binding to extracellular matrix collagens. So far, two mammalian DDRs have been identified: DDR1 and DDR2 (1). They are widely expressed in human tissues and may have roles in smooth muscle cell-mediated collagen remodeling (2). Research studies have implicated aberrant expression and signaling of DDRs in human diseases related to increased matrix degradation and remodeling, such as cardiovascular disease, liver fibrosis, and tumor invasion (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Neurite outgrowth inhibition protein (Nogo, RTN4) is a reticulon family protein that was identified as an axonal growth inhibitor of the central nervous system (CNS). Nogo occurs as three major isoforms (Nogo-A, Nogo-B, and Nogo-C) that share a common carboxy terminus of 188 amino acids. Nogo-A is transmembrane protein enriched in the endoplasmic reticulum and expressed at high levels in the CNS, and more weakly in skeletal and heart muscle (1-3). Expression of Nogo-A decreases with increasing age during brain development. In the adult CNS, negative regulation of neuronal growth leads to stabilization of the CNS wiring at the expense of extensive plastic rearrangements. Nogo-A meditates inhibition of neurite growth together with the nogo receptor 1 (NgR1), the p75 neurotrophin receptor p75NTR, and the transmembrane LINGO1 protein. This Nogo receptor signaling complex activates the RhoA/ROCK pathway, which collapses neuronal growth cones and inhibits axonal growth in the CNS following traumatic brain injury. Research studies suggest that inhibition of Nogo A may be beneficial to patients with traumatic brain injury. Nogo-B and Nogo-C inhibit BACE1 activity and amyloid precursor protein processing, suggesting a role in cell survival (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Members of the ADAM (a disintegrin and a metalloprotease) family of multidomain membrane proteins influence cell signaling and adhesion by shedding cell surface proteins, such as cytokines and growth factors. This process influences cell-extracellular matrix (ECM) adhesion and ECM remodeling. Conserved domains found in most ADAM family proteins include a prodomain, a zinc-dependent metalloprotease domain, a disintegrin domain, a carboxy-terminal cysteine-rich domain, an EGF-like sequence, and a short cytoplasmic tail (1,2).The ADAM metallopeptidase domain 10 (ADAM10) is a plasma membrane proteinase that cleaves membrane-bound proteins targeted for regulated intramembrane proteolysis (RIP). The ADAM10 prodomain acts as a chaperone that stabilizes mature ADAM protein folding, and prevents target-protein shedding through inhibition of ADAM10 proteinase activity (3,4). Mature ADAM10 is the major α-secretase responsible for cleavage of Notch, APP, cadherins, and prion protein (5-7). The ADAM10 protein cleaves receptor tyrosine kinases and their associated ligands and displays a wide range of regulatory functions across related signaling pathways (8). Research studies using knockout mice demonstrate that loss of ADAM10 results in defects in cortex formation, lymphocyte development, and cardiovascular development (9-11). Increased ADAM10 protein expression correlates with progression of many types of cancer (i.e. gastric cancer, hepatocellular carcinoma, and brain glioma), due to increased cancer cell migration, metastasis, and invasion (12-14). Mutations in the corresponding ADAM10 gene result in a rare, autosomal dominant pigmentation disorder known as reticulate acropigmentation of Kitamura (15).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: p130 Cas (Crk-associated substrate) is a docking protein containing multiple protein-protein interaction domains. The amino-terminal SH3 domain may function as a molecular switch regulating CAS tyrosine phosphorylation, as it interacts with focal adhesion kinase (FAK) (1) and the FAK-related kinase PYK2 (2), as well as the tyrosine phosphatases PTP-1B (3) and PTP-PEST (4). The carboxy-terminal Src binding domain (SBD) contains a proline-rich motif that mediates interaction with the SH3 domains of Src-family kinases (SFKs) and a tyrosine phosphorylation site (Tyr668 and/or Tyr670) that can promote interaction with the SH2 domain of SFKs (5). The p130 Cas central substrate domain, the major region of tyrosine phosphorylation, is characterized by 15 tyrosines present in Tyr-X-X-Pro (YXXP) motifs, including Tyr165, 249, and 410. When phosphorylated, most YXXP motifs are able to serve as docking sites for proteins with SH2 or PTB domains including adaptors, C-Crk, Nck, and inositol 5'-phosphatase 2 (SHIP2) (6). The tyrosine phosphorylation of p130 Cas has been implicated as a key signaling step in integrin control of normal cellular behaviors including motility, proliferation, and survival. Aberrant Cas tyrosine phosphorylation may contribute to cell transformation by certain oncoproteins (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Serum and glucocorticoid-inducible kinase (SGK) is a serine/threonine kinase closely related to Akt (1). SGK is rapidly induced in response to a variety of stimuli, including serum, glucocorticoid, follicle stimulating hormone, osmotic shock, and mineralocorticoids. SGK activation can be accomplished via HGF PI3K-dependent pathways and by integrin-mediated PI3K-independent pathways (2,3). Induction and activation of SGK has been implicated in activating the modulation of anti-apoptotic and cell cycle regulation (4-6). SGK also plays an important role in activating certain potassium, sodium, and chloride channels, suggesting its involvement in the regulation of processes such as cell survival, neuronal excitability, and renal sodium excretion (2). SGK is negatively regulated by ubiquitination and proteasome degradation (7).

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

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

Background: Retinoblastoma-associated proteins 46 and 48 (RBAP46 and RBAP48; also known as RBBP7 and RBBP4) were first characterized in human cells as proteins that bind to the retinoblastoma (Rb) tumor suppressor protein (1). Since then, these proteins have been shown to be components of many protein complexes involved in chromatin regulation, including the chromatin assembly factor 1 (CAF-1) complex and type B histone acetyltransferase complex HAT1, both of which function in chromatin assembly during DNA replication (2,3). RBAP46 and RBAP48 are also found in the nucleosome remodeling factor complex NURF, the nucleosome remodeling and histone de-acetylation complex NuRD, and the Sin3/HDAC histone de-acetylation complex (4-7). More recently, RBAP46 and RBAP48 were identified as components of the polycomb repressor complex PRC2, which also contains EED and Ezh2 (8). RBAP46 and RBAP48 bind to the histone fold region of histone H4 and are believed to target these chromatin remodeling, histone acetylation, and histone de-acetylation complexes to their histone substrates (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Forkhead box (Fox) proteins are a family of evolutionarily conserved transcription factors defined by the presence of a winged helix DNA binding domain called a Forkhead box (1). In humans, there are over 40 known Fox protein family members, divided into 19 subfamilies, which have evolved to regulate gene transcription in diverse and highly specialized biological contexts throughout development (2). Mutations that disrupt the expression of Fox gene family members have consequently been implicated in a broad array of human disorders, including immunological dysfunction, infertility, speech/language disorders, and cancer (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Ectonucleotide pyrophosphatase-phosphodiesterase 1 (ENPP1) is a single-pass, type II transmembrane protein primarily involved in ATP hydrolysis at the plasma membrane. Targeting of ENPP1 to the basolateral cell surface relies on the presence of a carboxy-terminal di-leucine-based signal (1). ENPP1 plays important roles in bone mineralization and soft tissue calcification (2-5). Mutations in the corresponding ENPP1 gene cause generalized arterial calcification in infancy (GACI) and idiopathic infantile arterial calcification (IIAC) (6,7). ENPP1 inhibits insulin receptor function and overexpression of this enzyme causes insulin resistance and glucose intolerance in mice (8,9). Genetic variants of ENPP1 have been associated with obesity and type 2 diabetes (10-12).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The prohibitins, called PHB1 and PHB2, are highly conserved proteins that are present in multiple compartments in eukaryotic cells. PHB1 is 30kDa tumor suppressor protein involved in cell cycle control (1). PHB1 has been found in mitochondria, the nucleus and the plasma membrane, as well as extracellularly in circulation (2). In mitochondria prohibitins mainly exist as membrane-bound ring complexes and function as chaperones maintaining mitochondrial protein stability during protein synthesis and transportation (3,4). In the nucleus prohibitins interact with transcription factors such as Rb and p53 to regulate target gene transcription (2,5). Extracellular prohibitin can bind and activate C3 to enhance complement activation (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Peroxisome proliferator-activated receptor γ (PPARγ) is a member of the ligand-activated nuclear receptor superfamily and functions as a transcriptional activator (1). PPARγ is preferentially expressed in adipocytes as well as in vascular smooth muscle cells and macrophage (2). Besides its role in mediating adipogenesis and lipid metabolism (2), PPARγ also modulates insulin sensitivity, cell proliferation and inflammation (3). PPARγ transcriptional activity is inhibited by MAP kinase phosphorylation of PPARγ at Ser84 (4,5).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Deleted in breast cancer gene 1 protein (DBC1) was originally identified by its localization to a region of chromosome 8p21 that is homozygously deleted in breast cancer (1). DBC1 is a large, nuclear protein with multiple functions in cell survival. It binds directly to the estrogen receptor α (ERα) hormone-binding domain in a ligand-independent manner and may be a key determinant of ligand-independent ERα expression and survival in human breast cancer cells (2). DBC1 can promote p53-mediated apoptosis by binding to and inhibiting the deacetylase activity of SirT1, resulting in increased p53 acetylation levels and activity (3). DBC1 may be an important regulator of heterochromatin formation as it binds SUV39H1 and inhibits its histone methyltransferase activity (4). Caspase-dependent processing activates the pro-apoptotic activity of DBC1 during Tumor Necrosis Factor-α (TNF-α)-mediated cell death signaling (5). This processing of DBC1 in response to TNF-α is an early event in the onset of apoptosis and results in relocalization of DBC1 to the cytoplasm. Overexpression of the processed, cytoplasmic form of DBC1 results in mitochondrial clustering and matrix condensation and sensitizes cells to TNF-α-mediated apoptosis.

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

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

Background: Deleted in breast cancer gene 1 protein (DBC1) was originally identified by its localization to a region of chromosome 8p21 that is homozygously deleted in breast cancer (1). DBC1 is a large, nuclear protein with multiple functions in cell survival. It binds directly to the estrogen receptor α (ERα) hormone-binding domain in a ligand-independent manner and may be a key determinant of ligand-independent ERα expression and survival in human breast cancer cells (2). DBC1 can promote p53-mediated apoptosis by binding to and inhibiting the deacetylase activity of SirT1, resulting in increased p53 acetylation levels and activity (3). DBC1 may be an important regulator of heterochromatin formation as it binds SUV39H1 and inhibits its histone methyltransferase activity (4). Caspase-dependent processing activates the pro-apoptotic activity of DBC1 during Tumor Necrosis Factor-α (TNF-α)-mediated cell death signaling (5). This processing of DBC1 in response to TNF-α is an early event in the onset of apoptosis and results in relocalization of DBC1 to the cytoplasm. Overexpression of the processed, cytoplasmic form of DBC1 results in mitochondrial clustering and matrix condensation and sensitizes cells to TNF-α-mediated apoptosis.

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Neurofibromatosis 2 (NF2) is an autosomal dominant, inherited disorder characterized by the occurrence of vestibular schwannomas, meningiomas, and other nervous system tumors. Both the familial tumors of NF2 and equivalent sporadic tumors found in the general population are caused by inactivation of the NF2 tumor suppressor gene. Merlin (moesin, ezrin, and radixin-like protein) is the NF2 gene product, displaying striking similarity to ezrin, radixin, and moesin (ERM) proteins. Regulation of merlin (also called schwannomin) and ERM proteins involves intramolecular and intermolecular head-to-tail associations between family members (1). Merlin and ERM proteins act as linkers between the plasma membrane and the cytoskeleton, affecting cell morphology, polarity, and signal transduction (2). Merlin is phosphorylated by the Rac/Cdc42 effector p21-activated kinase (PAK) at Ser518, negatively regulating Rac (3,4).

$303
100 µl
$717
300 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The Silent Information Regulator (SIR2) family of genes is a highly conserved group of genes that encode nicotinamide adenine dinucleotide (NAD)-dependent protein deacetylases, also known as class III histone deacetylases. The first discovered and best characterized of these genes is Saccharomyces cerevisiae SIR2, which is involved in silencing of mating type loci, telomere maintenance, DNA damage response, and cell aging (1). SirT1, the mammalian ortholog of Sir2, is a nuclear protein implicated in the regulation of many cellular processes, including apoptosis, cellular senescence, endocrine signaling, glucose homeostasis, aging, and longevity. Targets of SirT1 include acetylated p53 (2,3), p300 (4), Ku70 (5), forkhead (FoxO) transcription factors (5,6), PPARγ (7), and the PPARγ coactivator-1α (PGC-1α) protein (8). Deacetylation of p53 and FoxO transcription factors represses apoptosis and increases cell survival (2,3,5,6). Deacetylation of PPARγ and PGC-1α regulates the gluconeogenic/glycolytic pathways in the liver and fat mobilization in white adipocytes in response to fasting (7,8). SirT1 deacetylase activity is inhibited by nicotinamide and activated by resveratrol. In addition, SirT1 activity may be regulated by phosphorylation, as it is phosphorylated at Ser27 and Ser47 in vivo; however, the function of these phosphorylation sites has not yet been determined (9).