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Product listing: GMPS Antibody, UniProt ID P49915 #14602 to NBC1/SLC4A4 Antibody, UniProt ID Q9Y6R1 #11867

$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, 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, Monkey

Application Methods: Western Blotting

Background: Hexokinase catalyzes the conversion of glucose to glucose-6-phosphate, the first step in glycolysis. Four distinct mammalian hexokinase isoforms, designated as hexokinase I, II, III, and IV (glucokinase), have been identified. Hexokinases I, II, and III are associated with the outer mitochondrial membrane and are critical for maintaining an elevated rate of aerobic glycolysis in cancer cells (Warburg Effect) (1) in order to compensate for the increased energy demands associated with rapid cell growth and proliferation (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: Hexokinase catalyzes the conversion of glucose to glucose-6-phosphate, the first step in glycolysis. Four distinct mammalian hexokinase isoforms, designated as hexokinase I, II, III, and IV (glucokinase), have been identified. Hexokinases I, II, and III are associated with the outer mitochondrial membrane and are critical for maintaining an elevated rate of aerobic glycolysis in cancer cells (Warburg Effect) (1) in order to compensate for the increased energy demands associated with rapid cell growth and proliferation (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Heme oxygenase (HO) is the rate-limiting enzyme in the catabolism of heme that results in the release of carbon monoxide, iron, and biliverdin (1). The products of this enzymatic reaction play important biological roles in antioxidant, anti-inflammatory and cytoprotective functions (2). Heme oxygenase comprises two isozymes, including the constitutively expressed HO-2 isozyme and the inducible HO-1 isozyme (3). Inducible HO-1 is expressed as an adaptive response to several stimuli, including heme, metals, and hormones (4). The induction of HO-1 has been implicated in numerous disease states, such as transplant rejection, hypertension, atherosclerosis, Alzheimer disease, endotoxic shock, diabetes, inflammation, and neurological disorders (1,5).

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

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

Background: HSL (hormone-sensitive lipase) catalyzes the hydrolysis of triacylglycerol, the rate-limiting step in lipolysis. Lipolytic stimuli activate adenylyl cyclase and thus increase intracellular cAMP levels, which in turn activate protein kinase A (PKA). PKA phosphorylates HSL at Ser563, Ser659, and Ser660, which stimulates HSL activity (1,2). In contrast, AMPK phosphorylates HSL at Ser565, which reduces HSL phosphorylation at Ser563 by PKA and inhibits HSL activity (2,3). Recent work indicates that phosphorylation at Ser600 by p44/42 MAPKs also enhances the enzymatic activity of HSL (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: IDH1 is one of three isocitrate dehydrogenases that catalyze the oxidative decarboxylation of isocitrate to α-ketoglutarate (α-KG). These enzymes exist in two distinct subclasses that utilize either NAD or NADP+ respectively, as an electron acceptor (1). IDH1 is the NADP+-dependent isocitrate dehydrogenase found in the cytoplasm and peroxisomes. IDH2 and 3 are mitochondrial enzymes that also function in the Krebs cycle. IDH1 is inactivated by phosphorylation at Ser113 and contains a clasp-like domain wherein both polypeptide chains in the dimer interlock (2,3). IDH1 is expressed in a wide range of species and also in organisms that lack a complete citric acid cycle. Mutations in IDH1 have been reported in glioblastoma (4), acute myeloid leukemia (5,6), and other malignancies (7). IDH1 appears to function as a tumor suppressor that, when mutationally inactivated, contributes to tumorigenesis in part through induction of the HIF-1 pathway (8).

$260
100 µl
$630
300 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: Type I insulin-like growth factor receptor (IGF-IR) is a transmembrane receptor tyrosine kinase that is widely expressed in many cell lines and cell types within fetal and postnatal tissues (1-3). Receptor autophosphorylation follows binding of the IGF-I and IGF-II ligands. Three tyrosine residues within the kinase domain (Tyr1131, Tyr1135, and Tyr1136) are the earliest major autophosphorylation sites (4). Phosphorylation of these three tyrosine residues is necessary for kinase activation (5,6). Insulin receptors (IRs) share significant structural and functional similarity with IGF-I receptors, including the presence of an equivalent tyrosine cluster (Tyr1146/1150/1151) within the kinase domain activation loop. Tyrosine autophosphorylation of IRs is one of the earliest cellular responses to insulin stimulation (7). Autophosphorylation begins with phosphorylation at Tyr1146 and either Tyr1150 or Tyr1151, while full kinase activation requires triple tyrosine phosphorylation (8).

$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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: IGFBP7 (also known as Mac25, TAF, or IGFBP-rP1) belongs to the IGFBP superfamily, which plays an integral role in regulating insulin-like growth factor (IGF) actions in a wide variety of cell types. There are six known high-affinity IGF binding family members (IGFBP1-6), and ten low-affinity IGF binding members. These family members are structurally related, but encoded by distinct genes (1,2). IGFBP7 is a low-affinity IGF binding protein (1). The protein functions through its binding to secreted growth factors including IGF1, insulin, and activin (3,4). IGFBP7 levels have been related to cancer development and tissue injury. Loss of expression of IGFBP7 has been associated with poor survival in multiple cancer types (5,6) and with tumor chemotherapy resistance (7,8). IGFBP7 also has been identified as a cell cycle arrest biomarker for human acute kidney injury (AKI) and serves as a prognostic indicator for early stage AKI development (9-11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin)

Background: The maintenance of glucose homeostasis is an essential physiological process that is regulated by hormones. An elevation in blood glucose levels during feeding stimulates insulin release from pancreatic β cells through a glucose sensing pathway (1). Insulin is synthesized as a precursor molecule, proinsulin, which is processed prior to secretion. A- and B-peptides are joined together by a disulfide bond to form insulin, while the central portion of the precursor molecule is cleaved and released as the C-peptide. Insulin stimulates glucose uptake from blood into skeletal muscle and adipose tissue. Insulin deficiency leads to type 1 diabetes mellitus (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: IRAP (also known as LNPEP) was originally described as an insulin-responsive aminopeptidase found in Glut4-containing vesicles (1). It is essentially always in the same compartments as Glut4 and has identical insulin-stimulated translocation patterns as Glut4 (2). IRAP is therefore considered to be a surrogate marker for Glut4 (2). IRAP was later found to be a critical enzyme that regulates the expression and activity of several essential hormones and regulatory proteins, including the Glut4 transporter (3,4). This membrane associated, zinc-dependent cystinyl aminopeptidase acts as both a receptor for angiotensin IV as well as the enzyme that catalyzes the synthesis of this essential hormone from its angiotensinogen precursor (5). IRAP catalyzes the hydrolysis of several peptide hormones, including oxytocin and vasopressin (4). Abnormal IRAP expression or activity is associated with several forms of cancer in humans, including renal and endometrial cancers (6,7).

$260
100 µl
$630
300 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Insulin receptor substrate 1 (IRS-1) is one of the major substrates of the insulin receptor kinase (1). IRS-1 contains multiple tyrosine phosphorylation motifs that serve as docking sites for SH2-domain containing proteins that mediate the metabolic and growth-promoting functions of insulin (2-4). IRS-1 also contains over 30 potential serine/threonine phosphorylation sites. Ser307 of IRS-1 is phosphorylated by JNK (5) and IKK (6) while Ser789 is phosphorylated by SIK-2, a member of the AMPK family (7). The PKC and mTOR pathways mediate phosphorylation of IRS-1 at Ser612 and Ser636/639, respectively (8,9). Phosphorylation of IRS-1 at Ser1101 is mediated by PKCθ and results in an inhibition of insulin signaling in the cell, suggesting a potential mechanism for insulin resistance in some models of obesity (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Insulin Receptor Substrate 2 (IRS-2) is one of the major substrates of the insulin receptor kinase (1). In vertebrates, IRS-2 functions as a scaffolding protein to coordinate separate branches of the Insulin/IGF-signaling cascades (2). IRS-2 is essential for normal nutrient homeostasis because it mediates both peripheral insulin action and the effect of IGF-1 on B-cell growth. Mice lacking IRS-2 fail to maintain sufficient compensatory insulin secretion and develop diabetes as young adults (3).

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

Application Methods: Western Blotting

Background: Insulin Receptor Substrate 2 (IRS-2) is one of the major substrates of the insulin receptor kinase (1). In vertebrates, IRS-2 functions as a scaffolding protein to coordinate separate branches of the Insulin/IGF-signaling cascades (2). IRS-2 is essential for normal nutrient homeostasis because it mediates both peripheral insulin action and the effect of IGF-1 on B-cell growth. Mice lacking IRS-2 fail to maintain sufficient compensatory insulin secretion and develop diabetes as young adults (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: BTB/POZ domain-containing protein KCTD5 is a member of the potassium channel tetramerization domain family of proteins that play a role in transcriptional repression, cytoskeletal regulation, and ion channel gating (1). KCTD5 interacts with bound ubiquitin proteins and cullin3, and acts as a dependent E3 ligase substrate adaptor through interactions with its BTB domain (2). KCTD5 has been identified as a negative regulator of the AKT pathway by acting as an off switch for G-protein coupled receptor signaling by triggering proteolysis of Gβγ heterodimers dissociated from the Gα subunit (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Rat

Application Methods: Western Blotting

Background: L-asparaginase (ASRGL1) catalyzes the conversion of L-asparagine to L-aspartate. Research studies have shown that intracellular asparagine can suppress apoptosis in a large number of human tumors (1). In addition, acute lymphocytic leukemia cells frequently depend upon serum asparagine for their viability, as they lack asparagine synthetase (ASNS). Deprivation of asparagine by L-asparaginase has therefore been developed as a therapeutic treatment for acute lymphocytic leukemia (2-3). In KRAS mutant non-small cell lung carcinoma (NSCLC) cells, PI3K/Akt signaling was shown to be required for ASNS expression, suggesting combinatorial Akt inhibition and L-asparaginase treatment as a therapeutic strategy for NSCLC (3). Research studies on a breast cancer model have furthermore shown that restriction of asparagine can suppress cancer metastasis (4).

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

Application Methods: Western Blotting

Background: LACTB is a serine beta-lactamase-like protein that is most prominently expressed in skeletal muscle, heart and liver (1). It contains an amino-terminal transmembrane domain and is localized to the mitochondrial intermembrane space, where it is polymerized into stable filaments that promote intramitochondrial membrane organization and micro-compartmentalization (2). Studies in multiple breast cancer cell types have shown that LACTB can function as a tumor suppressor by promoting decreased levels of phosphatidylserine decarboxylase (PISD), leading to reduced cell proliferation (3). In accordance with this, levels of LACTB have been shown to be downregulated in hepatocellular carcinoma and colorectal cancer and associated with poor prognosis in both (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: L-type amino acid transporter 1 (LAT1), also known as Solute carrier family 7 member 5 (SLC7A5), is a high-affinity neutral transporter of larger amino acids. It facilitates the cellular amino acid uptake in a sodium independent manner (1-2) and selectively transports D-and L-isomers of small neutral amino acids (3). LAT1 also regulates amino acid exchange in conjunction with solute carrier family 1 member 5 (SLC1A5) (2,4-6). Transport of thyroid hormones across the placenta is established via LAT1 during normal fetal development (7). LAT1 promotes neuronal cell proliferation by regulating the transport of amino acids across the blood brain barrier (8). LAT1 is upregulated in various cancer types including breast cancer, lung cancer, prostate cancer, and gliomas (9,10). High expression of LAT1 is detected in non-small cell lung cancer with lymph node metastases(9,11,12). Increased LAT1 expression is a novel biomarker of high grade malignancy in prostate cancers (12). Inhibition of LAT1 suppresses tumor cell growth in several tumor types (10,13).

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

Application Methods: Western Blotting

Background: Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and NADH to lactate and NAD+. When the oxygen supply is too low for mitochondrial ATP production, this reaction recycles NADH generated in glycolysis to NAD+, which reenters glycolysis. The major form of LDH found in muscle cells is the A (LDHA) isozyme. The LDHA promoter contains HIF-1α binding sites (1). LDHA expression is induced under hypoxic conditions (2). During intensive and prolonged muscle exercise, lactate accumulates in muscle cells when the supply of oxygen does not meet demand. When oxygen levels return to normal, LDH converts lactate to pyruvate to generate ATP in the mitochondrial electron transport chain.

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

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

Background: Lipin 1 was identified as a nuclear protein required for adipose tissue development (1). The expression of Lipin 1 is induced during adipocyte differentiation (1). The abnormal development of adipose tissues caused by mutations in the lipin 1 gene results in lipodystrophy, a condition associated with low body fat, fatty liver, hypertriglyceridemia, and insulin resistance (1). Lipin 1 plays a role in lipid metabolism in various tissues and cell types including liver, muscle, adipose tissues, and neuronal cell lines (2-4). It has dual functions at the molecular level: Lipin 1 serves as a transcriptional coactivator in liver, and a phosphatidate phosphatase in triglyceride and phospholipid biosynthesis pathways (5). Lipin 1 is regulated by mTOR, illustrating a connection between adipocyte development and nutrient-sensing pathways (6). It also mediates hepatic insulin signaling by TORC2/CRTC2 (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Cytosolic malic enzyme (ME1) catalyzes the conversion of malate and NADP+ to pyruvate and NADPH (1,2). NADPH is then used for fatty acid biosynthesis and lipogenesis (1,2). Cytosolic malic enzyme was shown to mediate high fat diet-induced adiposity (1). Mitochondrial malic enzyme (ME2) preferentially uses NAD+ to catalyze the conversion of malate to pyruvate with the concomitant generation of NADH (2). Recent studies have demonstrated that the tumor suppressor p53 regulates cell metabolism and proliferation by repressing the expression of both cytosolic malic enzyme and mitochondrial malic enzyme (3).

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

Application Methods: Western Blotting

Background: Malic enzymes catalyze oxidative decarboxylation of malate to pyruvate (1). The malic enzyme family in mammalian cells includes the cytosolic malic enzyme 1 (ME1) and two mitochondrial malic enzymes (ME2 and ME3) (1, 2). ME1 and ME2 are critical for tumor cell growth and their expression is repressed by tumor suppressor p53 (2). Reduced expression of ME1 and ME2 reciprocally increases the levels and activation of p53, promoting p53-mediated senescence (2). Research studies show ME3 is essential for the survival of pancreatic ductal adenocarcinoma following genomic deletion of ME2 (3). Deletion of ME3 is lethal to ME2-null cancer cells, which has been suggested to provide a potential therapeutic opportunity using collateral lethality (3, 4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Malate dehydrogenase (MDH) is a key enzyme in the tricarboxylic acid cycle and malate/aspartate shuttle (1,2). MDH is widely expressed in organisms from most bacteria to all eukaryotes (2). The cytoplasmic MDH isoenzyme (cMDH or MDH1) primarily reduces oxaloacetate to malate in the malate/aspartate shuttle (1-3). The major function of the mitochondrial MDH isoenzyme (mMDH or MDH2) is to oxidize malate to oxaloacetate in the tricarboxylic acid cycle (1,2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Mitochondrial Rho GTPase 1 (Miro1, RHOT1) and mitochondrial Rho GTPase 2 (Miro2, RHOT2) are atypical Ras GTPase proteins that localize to the outer mitochondrial membrane (1,2). These evolutionarily conserved proteins contain GTP-binding domains and a pair of calcium-binding EF hand domains (1,2). Research studies indicate that Miro1 and Miro2 function in the axonal transport of mitochondria in neurons (2). Both Miro proteins play an essential role in mitochondrial trafficking by attaching mitochondria to essential motor and adaptor proteins (3). Miro GTPase proteins that are anchored to the outer mitochondrial membrane interact with kinesin-binding proteins TRAK1 and TRAK2 to provide a link between mitochondria to microtubules (4). Increased levels of synaptic calcium appears to inhibit mitochondrial trafficking mediated by Miro, suggesting a role for the EF hand as a calcium sensor (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Multi-drug resistance protein 2 (MRP2), also known as cMRP, cMOAT, and ABCC2, is an ATP binding cassette (ABC) transporter and part of the multi-drug resistance (MRP) family (1,2). The MRP proteins are membrane proteins that function as organic anion pumps involved in the cellular removal of cancer drugs (2). MRP2 is associated with resistance to a number of cancer drugs, such as cisplatin, etoposide, doxorubicin, and methotrexate (3-5). MRP2 is predominately expressed on the apical membranes in the liver (6-9) and kidney proximal tubules (10). It is responsible for the ATP-dependent secretion of bilirubin glucuronides and other organic anions from hepatocytes into the bile, a process important for the excretion of endogenous and xenobiotic substances. Loss of MRP2 activity is the cause of Dubin-Johnson syndrome, an autosomal recessive disorder characterized by defects in the secretion of anionic conjugates and the presence of melanin like pigments in hepatocytes (11-13).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: MTAP is an enzyme that is essential for the salvage pathway for both adenine and methionine synthesis. MTAP catalyzes the cleavage of 5’-methylthioadenosine into adenine and 5-methylthio-D-ribose-1-phosphate. Adenine is then used to generate AMP whereas 5-methylthio-D-ribose-1-phosphate is converted into methionine (1,2). MTAP is expressed in all normal cells and tissues, although frequently lost in different human tumors including pancreatic adenocarcinoma, neuroendocrine tumors, non-small cell lung carcinoma and breast carcinoma. MTAP is usually codeleted with p16 (cdkN2a/ARF) (3-5). MTAP overexpression in breast cancer cells inhibits their ability to form colonies in soft agar, thereby implicating its function as a tumor suppressor (6).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: NADK, also known as NAD kinase, is a cytoplasmic protein responsible for maintaining the pool of available NADP+ and NADPH within the cell (1). Using ATP as a phosphate donor, NADK catalyzes the phosphorylation of NAD+ to NADP+. This molecule is then reduced to NADPH and utilized in various metabolic and biosynthetic pathways (2). NADK has been suggested to play a role in glucose metabolism due to the effect NADPH production has on both the insulin secretion and survival of pancreatic β-cells (3). NADPH has a vital role in protecting cells from oxidative stress through its neutralizing effect on reactive oxygen species (ROS), which also accumulate during cell growth (2, 3, 4). Along with the p53 tumor suppression protein, NADK has been a suggested target in cancer therapy due its link to NADPH production and its resulting protective role on growing and proliferating cells (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: NBC1/SLC4A4 is an eletrogenic sodium bicarbonate cotransporter. It mediates the coupled movement of Na+ and HCO3- ions across the basolateral membrane of cells. NBC1 regulates secretion and absorption of bicarbonate and modulates intracellular pH (1-3). There are five isoforms of NBC1 produced by alternative splicing including the most studied isoforms, 1 and 2, which have different N termini. The N terminus of isoform 1 contains multiple consensus phosphorylation sites for various kinases, such as PKA, PKC, and CK II, and may play a regulatory role in the biological function of NBC1 (4). Interaction with carbonic anhydrase II, IV, and IX regulates the transporter acitivity of NBC1 (5-7). NBC1 is expressed in various tissues with the exception of isoform 2, which is mainly expressed in kidney proximal tubules (1). Isoform 1 is expressed in the pancreas and corneal endothelium, and at low levels in other tissues including heart, skeletal muscle, liver, and prostate (4). Research studies have shown that mutations in the NBC1 gene are linked to proximal renal tubular acidosis with ocular abnormalities (also known as renal tubular acidosis II).