Microsize antibodies for $99 | Learn More >>

Monoclonal Antibody Negative Regulation of Transporter Activity

$348
100 µl
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated α-Synuclein (D37A6) XP® Rabbit mAb #4179.
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Western Blotting

Background: α-Synuclein is a protein of 140-amino acids expressed abundantly in the brain. α-Synuclein is also the main component of pathogenic Lewy bodies and Lewy neurites. Research studies have shown that mutations of the α-synuclein gene are linked to Parkinson's disease (1).

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

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

Background: α-Synuclein is a protein of 140-amino acids expressed abundantly in the brain. α-Synuclein is also the main component of pathogenic Lewy bodies and Lewy neurites. Research studies have shown that mutations of the α-synuclein gene are linked to Parkinson's disease (1).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: α-Synuclein is a protein of 140-amino acids expressed abundantly in the brain. α-Synuclein is also the main component of pathogenic Lewy bodies and Lewy neurites. Research studies have shown that mutations of the α-synuclein gene are linked to Parkinson's disease (1).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

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

Background: α-Synuclein is a protein of 140-amino acids expressed abundantly in the brain. α-Synuclein is also the main component of pathogenic Lewy bodies and Lewy neurites. Research studies have shown that mutations of the α-synuclein gene are linked to Parkinson's disease (1).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: α-Synuclein is a protein of 140-amino acids expressed abundantly in the brain. α-Synuclein is also the main component of pathogenic Lewy bodies and Lewy neurites. Research studies have shown that mutations of the α-synuclein gene are linked to Parkinson's disease (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Glucokinase regulatory protein (GCKR, GKRP) regulates the activity and localization of glucokinase, an important metabolic regulator of glucose uptake, glycogen synthesis, and glucose production in hepatocytes (1). GKRP plays a key role in glucose homeostasis as it inhibits glucokinase activity and sequesters this metabolic enzyme in hepatocyte nuclei; in response to changes in glucose concentration, GCKR promotes the release of glucokinase into the cytoplasm (2). During conditions of low blood glucose levels, GCKR binds to fructose-6-phosphate, which leads to GCKR binding to glucokinase and the subsequent nuclear localization and inactivation of glucokinase. After feeding, GCKR binds fructose-1-phosphate, which disrupts the interaction between GCKR and glucokinase and releases active glucokinase to cytoplasm (1-3). Polymorphisms in the corresponding GCKR gene are associated with atypical plasma triglyceride levels, fasting glucose and insulin levels, and glucokinase activity (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Ubiquitin regulatory X domain-containing protein 8 (UBXD8, also known as ETEA and FAF2) is a hairpin-anchored endoplasmic reticulum (ER) protein involved in ER associated degradation (ERAD). It influences this process by promoting translocation of misfolded proteins from the ER lumen to the cytoplasm for proteasome-mediated degradation (1). UBXD8 is a sensor for unsaturated fatty acids. In the absence of fatty acids UBXD8 binds to and targets INSIG1 for degradation, ultimately resulting in activation of SREBP-1. Under this condition, UBXD8 also inhibits triglyceride synthesis by blocking the conversion of diacylglycerols into triglycerides. Unsaturated fatty acids trigger UBXD8 polymerization and dissociation of UBXD8/INSIG1 complex, leading to feedback inhibition of SREBP-1 (2, 3). This induces UBXD8 to translocate from the ER to lipid droplets, where it binds to ATGL and inhibits its lipase activity (4, 5). The complex containing p97 and UBXD8 is reported to promote disassembly of the ribonucleoprotein complex to control mRNA stability (6). In addition, UBXD8 binds to and promotes degradation of neurofibromin (NF1), suggesting a role in regulating Ras activity (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: IHC-Leica® Bond™, Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: IFIT1 (interferon-induced protein with tetratricopeptide repeats 1) belongs to the IFIT family of proteins, which consists of four members in humans (IFIT1, IFIT2, IFIT3, and IFIT5) and three members in mice (IFIT1, IFIT2, and IFIT3) (1). IFIT1 expression is induced by Type I Interferons resulting from viral infection (2). IFIT1 is an antiviral protein that directly binds viral RNA that has a 5’ triphosphate group (PPP-RNA) (2). In humans, the viral PPP-RNA bound IFIT1 forms a complex with IFIT2 and IFIT3 to sequester the viral PPP-RNA and prevent replication (2). IFIT1 has also been shown to inhibit translation by binding to the eukaryotic initiation factor-3 (eIF-3) (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: CRYAB (αB-Crystallin) is a member of the small heat shock protein (sHSP also known as HSP20) family (1). This protein was initially found to be overexpressed in the eye lens, and later also detected at high levels in heart and skeletal muscle tissues (2,3). CRYAB functions mainly as a molecular chaperone, responding to stress by binding unfolded target proteins to prevent aggregation (4,5). Research studies have shown that elevated expression of CRYAB in neurological disease and stroke patients protects tissue and cells from damage under extreme stress, leading to the investigation of CRYAB as a potential therapeutic target (6-9). Researchers also found that expression of the missense mutation of CRYAB (R120G) in the mouse model causes cardiomyopathy due to abnormal desmin aggregation (10). At the molecular level, CRYAB is involved in multiple biological processes, such as inhibiting apoptosis by binding and inhibiting caspase and proapoptotic Bax and Bcl-xS protein functions (11,12), promoting angiogenesis by binding and stabilizing VEGF for secretion (13), and regulating cytoskeletal organization through association with actin filament, intermediate filament, and cardiac titin (14-16).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: Fatty acid binding proteins (FABPs) bind to fatty acids and other lipids to function as cytoplasmic lipid chaperones (1,2). They participate in the transport of fatty acids and other lipids to various cellular pathways (2). Research studies have shown that common variants of the human liver fatty acid binding protein gene FABP1 play a role in the development of type 2 diabetes and insulin resistance (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Phospholamban (PLN) was identified as a major phosphoprotein component of the sarcoplasmic reticulum (SR) (1). Its name, "lamban", is derived from the greek word "lambano" meaning "to receive", so named due to the fact that phospholamban is heavily phosphorylated on serine and threonine residues in response to cardiac stimulation (1). Although originally thought to be a single 20-25 kDa protein due to its electrophoretic mobility on SDS-PAGE, PLN is actually a 52 amino acid, 6 kDa, membrane-spanning protein capable of forming stable homooligomers, even in the presence of SDS (2). Despite very high expression in cardiac tissue, phospholamban is also expressed in skeletal and smooth muscle (3). Localization of PLN is limited to the SR, where it serves as a regulator of the sarco-endoplasmic reticulum calcium ATPase, SERCA (4). PLN binds directly to SERCA and effectively lowers its affinity for calcium, thus reducing calcium transport into the SR. Phosphorylation of PLN at Ser16 by Protein Kinase A or myotonic dystrophy protein kinase and/or phosphorylation at Thr17 by Ca2+/calmodulin-dependent protein kinase results in release of PLN from SERCA, relief of this inhibition, and increased calcium uptake by the SR (reviewed in 5,6). It has long been held that phosphorylation at Ser16 and Thr17 occurs sequentially, but increasing evidence suggests that phosphorylation, especially at Thr17, may be differentially regulated (reviewed in 7,8).Rodent models of heart failure have shown that the expression level and degree of phosphorylation of PLN are critical in modulating calcium flux and contractility (reviewed in 9-11). Deletion or decreased expression of PLN promotes increased calcium flux and increased cardiac contractility, whereas overexpression of PLN results in sequestration of SERCA, decreased calcium flux, reduced contractility, and rescue of cardiac dysfunction and failure in mouse models of hypertension and cardiomyopathy (reviewed in 10). Distinct mutations in PLN have been detected in humans, resulting either in decreased or no expression of PLN protein (12,13) or binding defects between PLN, SERCA and/or regulatory proteins (14,15), both of which result in cardiac myopathy and heart failure. Interestingly, while the human phenotype of most PLN defects mimic those seen in rodent and vice versa, there are some instances where the type and severity of cardiac disease resulting from PLN mutations in rodent and human differ, making a consensus mechanism elusive.

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunofluorescence (Frozen)

Background: Vasopressin is a neuroendocrine peptide that is released to the circulation by magnocellular neurons whose cell bodies are mainly found in the paraventricular and the supraoptic nuclei of the hypothalamus. It was first isolated from pituitary gland extracts and synthesized in 1951 (1). Vasopressin acts by activating G protein-coupled, V1a, V1b (also known as V3) and V2 receptors and plays a fundamental role in the maintenance of water homeostasis. One of its main functions is body water retention (2), hence its alternative name antidiuretic hormone or ADH. Vasopressin also leads to increased arterial blood pressure by raising peripheral vascular resistance (3). Vasopressin is also involved in other physiological processes such as acute heart failure (4), pain (5), and metabolic syndrome (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: ApoAI (Apolipoprotein A1) is a major component of high density lipoprotein (HDL, the “good cholesterol”) in plasma. It is produced in the liver and small intestine. ApoA1 is a cofactor for lecithin cholesterolacyltransferase (LCAT) that is responsible for the formation of plasma cholesteryl esters and promotes cholesterol efflux from tissues to the liver for excretion. Defects in ApoA1 are associated with high density lipoprotein deficiency (HDLD) and systemic non-neuropathic amyloidosis (1-3).

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Arrestin proteins function as negative regulators of G protein-coupled receptor (GPCR) signaling. Cognate ligand binding stimulates GPCR phosphorylation, which is followed by binding of arrestin to the phosphorylated GPCR and the eventual internalization of the receptor and desensitization of GPCR signaling (1). Four distinct mammalian arrestin proteins are known. Arrestin 1 (also known as S-arrestin) and arrestin 4 (X-arrestin) are localized to retinal rods and cones, respectively. Arrestin 2 (also known as β-arrestin 1) and arrestin 3 (β-arrestin 2) are ubiquitously expressed and bind to most GPCRs (2). β-arrestins function as adaptor and scaffold proteins and play important roles in other processes, such as recruiting c-Src family proteins to GPCRs in Erk activation pathways (3,4). β-arrestins are also involved in some receptor tyrosine kinase signaling pathways (5-8). Additional evidence suggests that β-arrestins translocate to the nucleus and help regulate transcription by binding transcriptional cofactors (9,10).

$260
100 µl
APPLICATIONS
REACTIVITY
Bovine, Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Endothelial nitric-oxide synthase (eNOS) is an important enzyme in the cardiovascular system. It catalyzes the production of nitric oxide (NO), a key regulator of blood pressure, vascular remodeling, and angiogenesis (1,2). The activity of eNOS is regulated by phosphorylation at multiple sites. The two most thoroughly studied sites are the activation site Ser1177 and the inhibitory site Thr495 (3). Several protein kinases including Akt/PKB, PKA, and AMPK activate eNOS by phosphorylating Ser1177 in response to various stimuli (4,5). In contrast, bradykinin and H2O2 activate eNOS activity by promoting both Ser1177 phosphorylation and Thr495 dephosphorylation (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Dog, Human, Monkey

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

Background: Protein phosphatase 1 (PP1) is a ubiquitous eukaryotic protein serine/threonine phosphatase involved in the regulation of various cell functions. Substrate specificity is determined by the binding of a regulatory subunit to the PP1 catalytic subunit (PP1c). It is estimated that over fifty different regulatory subunits exist (1).The myosin phosphatase holoenzyme is composed of three subunits: PP1c, a targeting/regulatory subunit (MYPT/myosin-binding subunit of myosin phosphatase), and a 20 kDa subunit of unknown function (M20). MYPT binding to PP1cδ alters the conformation of the catalytic cleft and increases enzyme activity and specificity (2). Two MYPT isoforms that are 61% identical have been described. MYPT1 is widely expressed, while MYPT2 expression appears to be exclusive to heart and brain (3). Related family members include MBS85, MYPT3, and TIMAP (4).Myosin phosphatase regulates the interaction of actin and myosin in response to signaling through the small GTPase Rho. Rho activity inhibits myosin phosphatase via Rho-associated kinase (ROCK). Phosphorylation of MYPT1 at Thr696 and Thr853 results in phosphatase inhibition and cytoskeletal reorganization (5,6).

$305
100 µl
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated eNOS (D9A5L) Rabbit mAb #32027.
APPLICATIONS
REACTIVITY
Bovine, Human, Mouse, Rat

Application Methods: Western Blotting

Background: Endothelial nitric-oxide synthase (eNOS) is an important enzyme in the cardiovascular system. It catalyzes the production of nitric oxide (NO), a key regulator of blood pressure, vascular remodeling, and angiogenesis (1,2). The activity of eNOS is regulated by phosphorylation at multiple sites. The two most thoroughly studied sites are the activation site Ser1177 and the inhibitory site Thr495 (3). Several protein kinases including Akt/PKB, PKA, and AMPK activate eNOS by phosphorylating Ser1177 in response to various stimuli (4,5). In contrast, bradykinin and H2O2 activate eNOS activity by promoting both Ser1177 phosphorylation and Thr495 dephosphorylation (6,7).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Akt, also referred to as PKB or Rac, plays a critical role in controlling survival and apoptosis (1-3). This protein kinase is activated by insulin and various growth and survival factors to function in a wortmannin-sensitive pathway involving PI3 kinase (2,3). Akt is activated by phospholipid binding and activation loop phosphorylation at Thr308 by PDK1 (4) and by phosphorylation within the carboxy terminus at Ser473. The previously elusive PDK2 responsible for phosphorylation of Akt at Ser473 has been identified as mammalian target of rapamycin (mTOR) in a rapamycin-insensitive complex with rictor and Sin1 (5,6). Akt promotes cell survival by inhibiting apoptosis through phosphorylation and inactivation of several targets, including Bad (7), forkhead transcription factors (8), c-Raf (9), and caspase-9. PTEN phosphatase is a major negative regulator of the PI3 kinase/Akt signaling pathway (10). LY294002 is a specific PI3 kinase inhibitor (11). Another essential Akt function is the regulation of glycogen synthesis through phosphorylation and inactivation of GSK-3α and β (12,13). Akt may also play a role in insulin stimulation of glucose transport (12). In addition to its role in survival and glycogen synthesis, Akt is involved in cell cycle regulation by preventing GSK-3β-mediated phosphorylation and degradation of cyclin D1 (14) and by negatively regulating the cyclin dependent kinase inhibitors p27 Kip1 (15) and p21 Waf1/Cip1 (16). Akt also plays a critical role in cell growth by directly phosphorylating mTOR in a rapamycin-sensitive complex containing raptor (17). More importantly, Akt phosphorylates and inactivates tuberin (TSC2), an inhibitor of mTOR within the mTOR-raptor complex (18,19).

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

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

Background: HDAC6 is a class II histone deacetylase enzyme localized to the cytoplasm and associated with the microtubule network (1). It is involved in the regulation of many cellular processes, including cell migration, immune synapse formation, viral infection, and degradation of misfolded proteins (1). HDAC6 contains two tandem catalytic domains that facilitate the deacetylation of multiple protein substrates, including histones and non-histone proteins such as tubulin, cortactin, and HSP90. Despite the ability to deacetylate histone proteins in vitro, there is no evidence for HDAC6-mediated deacetylation of histones in vivo (2,3). The acetylation/deacetylation of tubulin on Lys40 regulates binding and motility of the kinesin-1 motor protein and subsequent transport of cargo proteins such as JNK-interacting protein 1 (JIP1) (4). The acetylation/deacetylation of cortactin regulates cell motility by modulating the binding of cortactin to F-actin (5). Acetylation/deacetylation of HSP90 modulates chaperone complex activity by regulating the binding of an essential cochaperone protein, p23 (6,7). In addition to its role as a protein deacetylase, HDAC6 functions as a component of the aggresome, a proteinaceous inclusion body that forms in response to an accumulation of misfolded or partially denatured proteins (8). Formation of the aggresome is a protective response that sequesters cytotoxic protein aggregates for eventual autophagic clearance from the cell. HDAC6 contains a zinc finger ubiquitin-binding domain that binds both mono- and poly-ubiquitinated proteins (8). HDAC6 binds to both poly-ubiquitinated misfolded proteins and dynein motors, facilitating the transport of misfolded proteins to the aggresome (9,10). HDAC6 is also required for subsequent recruitment of the autophagic machinery and clearance of aggresomes from the cell (11). Thus, HDAC6 plays a key role in the protection against the deleterious effects of pathological protein aggregation that occurs in various diseases, such as neurodegenerative Huntington’s disease (11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: HDAC6 is a class II histone deacetylase enzyme localized to the cytoplasm and associated with the microtubule network (1). It is involved in the regulation of many cellular processes, including cell migration, immune synapse formation, viral infection, and degradation of misfolded proteins (1). HDAC6 contains two tandem catalytic domains that facilitate the deacetylation of multiple protein substrates, including histones and non-histone proteins such as tubulin, cortactin, and HSP90. Despite the ability to deacetylate histone proteins in vitro, there is no evidence for HDAC6-mediated deacetylation of histones in vivo (2,3). The acetylation/deacetylation of tubulin on Lys40 regulates binding and motility of the kinesin-1 motor protein and subsequent transport of cargo proteins such as JNK-interacting protein 1 (JIP1) (4). The acetylation/deacetylation of cortactin regulates cell motility by modulating the binding of cortactin to F-actin (5). Acetylation/deacetylation of HSP90 modulates chaperone complex activity by regulating the binding of an essential cochaperone protein, p23 (6,7). In addition to its role as a protein deacetylase, HDAC6 functions as a component of the aggresome, a proteinaceous inclusion body that forms in response to an accumulation of misfolded or partially denatured proteins (8). Formation of the aggresome is a protective response that sequesters cytotoxic protein aggregates for eventual autophagic clearance from the cell. HDAC6 contains a zinc finger ubiquitin-binding domain that binds both mono- and poly-ubiquitinated proteins (8). HDAC6 binds to both poly-ubiquitinated misfolded proteins and dynein motors, facilitating the transport of misfolded proteins to the aggresome (9,10). HDAC6 is also required for subsequent recruitment of the autophagic machinery and clearance of aggresomes from the cell (11). Thus, HDAC6 plays a key role in the protection against the deleterious effects of pathological protein aggregation that occurs in various diseases, such as neurodegenerative Huntington’s disease (11).