85133 Results for: "4-Amino-2-hydroxybenzohydrazide&amp"

Supplier: Bioss

CD39, also known as ectonucleoside triphosphate diphosphohydrolase 1 (ENP1), is an integral membrane glycoprotein that acts as an extracellular nucleotide-hydrolyzing enzyme. CD39 inhibits ADP-induced platelet aggregation by hydrolyzing ADP to AMP and ultimately generating adenosine. Intracellular CD39 undergoes glycosylation at 6 N-glycosylation sites and translocates to the membrane in order to be an active enzyme. CD39L1 is a 495 amino acid multi-pass membrane protein that requires calcium and magnesium cofactors to hydrolyze ATP and other nucleotides in the regulation of purigenic neurotransmission. CD39L1 is expressed in kidney, colon, heart, testis, pancreas, brain, prostate, skeletal muscle, small intestine and ovaries. There are two isoforms of CD39L1 that are produced as a result of alternative splicing events.

Supplier: Biosensis

Adenylate cyclases are enzymes which interact with and are activated by the GTP bound alpha subunits of trimeric G-proteins. Activated adenylate cyclases are responsible for the production of the important "second messenger" signalling molecule cyclic-AMP, which is generated from ATP. The type III adenylate cyclase enzyme is localized in the membranes surrounding the cilia in neurons, and our antibody is an excellent marker of neuronal cilia in the brain and in cells in tissue culture. Adenylate cyclase type III is a large complex molecule of, in the human, 1145 amino acids with a deduced molecular weight of 129kDa. The protein may be variably glycosylated, so that on SDS-PAGE and western blots it runs as a diffuse band of about 160kDa in cortex and about 200kDa in olfactory epithelium. The molecule has a complex structure, with 12 transmembrane domains and two cyclase domains. Each cyclase domain is immediately C-terminal to 6 transmembrane segments, but only the second, C-terminal cyclase is believed to be catalytically active.

Supplier: Prosci

For WB starting dilution is: 1:1000 For IHC-P starting dilution is: 1:50~100

Supplier: Bioss

Ubiquitination is an important molecular mechanism by which abnormal or short-lived proteins are targeted for degradation by the concerted efforts of at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2J2 (Ubiquitin-conjugating enzyme E2 J2), also known as NCUBE2 (Non-canonical ubiquitin-conjugating enzyme 2), is a 259 amino acid single pass type IV membrane protein that that belongs to the E2 ubiquitin-conjugating enzyme family and is involved in protein degradation. Localized to the membrane of the endoplasmic reticulum (ER), UBE2J2 catalyzes the attachment of ubiquitin to misfolded membrane proteins, thereby targeting them for proteasomal destruction. This ATP-dependent reaction yields AMP, a diphosphate and a ubiquitin-tagged protein and may be a method of quality control within the ER. Two isoforms of UBE2J2 exist due to alternative splicing events.

Supplier: Bioss

Ubiquitination is an important molecular mechanism by which abnormal or short-lived proteins are targeted for degradation by the concerted efforts of at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2J2 (Ubiquitin-conjugating enzyme E2 J2), also known as NCUBE2 (Non-canonical ubiquitin-conjugating enzyme 2), is a 259 amino acid single pass type IV membrane protein that that belongs to the E2 ubiquitin-conjugating enzyme family and is involved in protein degradation. Localized to the membrane of the endoplasmic reticulum (ER), UBE2J2 catalyzes the attachment of ubiquitin to misfolded membrane proteins, thereby targeting them for proteasomal destruction. This ATP-dependent reaction yields AMP, a diphosphate and a ubiquitin-tagged protein and may be a method of quality control within the ER. Two isoforms of UBE2J2 exist due to alternative splicing events.

Supplier: Prosci

HINT1 Antibody: Histidine triad nucleotide-binding protein 1 (HINT1) is a member of the histidine triad (HIT) protein family, a group of small nucleotide-binding and -hydrolyzing proteins. HINT1 interacts with several diverse proteins and has been suggested to have tumor suppressive activities. HINT1 catalyzes the hydrolysis of adenosine 5'-monophoramidate substrates such as AMP-morpholidate, but its enzymatic function does not appear to play a role in its tumor suppression. Recent experiments demonstrate that HINT1 forms a complex with POSH and JNK in vivo, inhibiting AP-1 activity and the phosphorylation of c-Jun, and this action could contribute to the tumor suppressor activity of HINT1. Other studies raise the possibility of HINT1 as a candidate gene for schizophrenia.

Supplier: Bioss

Ubiquitination is an important molecular mechanism by which abnormal or short-lived proteins are targeted for degradation by the concerted efforts of at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2J2 (Ubiquitin-conjugating enzyme E2 J2), also known as NCUBE2 (Non-canonical ubiquitin-conjugating enzyme 2), is a 259 amino acid single pass type IV membrane protein that that belongs to the E2 ubiquitin-conjugating enzyme family and is involved in protein degradation. Localized to the membrane of the endoplasmic reticulum (ER), UBE2J2 catalyzes the attachment of ubiquitin to misfolded membrane proteins, thereby targeting them for proteasomal destruction. This ATP-dependent reaction yields AMP, a diphosphate and a ubiquitin-tagged protein and may be a method of quality control within the ER. Two isoforms of UBE2J2 exist due to alternative splicing events.

Supplier: Bioss

Ubiquitination is an important molecular mechanism by which abnormal or short-lived proteins are targeted for degradation by the concerted efforts of at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2J2 (Ubiquitin-conjugating enzyme E2 J2), also known as NCUBE2 (Non-canonical ubiquitin-conjugating enzyme 2), is a 259 amino acid single pass type IV membrane protein that that belongs to the E2 ubiquitin-conjugating enzyme family and is involved in protein degradation. Localized to the membrane of the endoplasmic reticulum (ER), UBE2J2 catalyzes the attachment of ubiquitin to misfolded membrane proteins, thereby targeting them for proteasomal destruction. This ATP-dependent reaction yields AMP, a diphosphate and a ubiquitin-tagged protein and may be a method of quality control within the ER. Two isoforms of UBE2J2 exist due to alternative splicing events.

Supplier: Rockland Immunochemical

SESTRIN2, also known as Hi95, is a member of the sestrin family of PA26-related proteins and is induced following DNA damage or oxidative stress (1). SESTRIN2 and the related protein SESTRIN1 interact with the NRF2 suppressor KEAP1, the autophagy substrate p62 and the ubiquitin ligase RBX1 to protect cells against oxidative stress by activating NRF2 and promoting the p62-dependent autophagic degradation of KEAP1 (2). SESTRIN2 also negatively regulates TOR signaling by activating AMP-activated protein kinase (AMPK) and TSC2 phosphorylation (3), thereby protecting cells against energetic stress-induced death (4).

Supplier: Bioss

PKA (or cAPK) is a cyclic AMP dependent protein kinase. When activated by the second messenger cAMP, PKA mediates diverse cellular mechanisms, including proliferation, ion transport, regulation of metabolism, plus gene transcription. PKA is comprised of two dimers of two subunits, R (regulatory) and C (catalytic). Two families of R subunit (RI and RII) and three C subunit isoforms (C alpha, C beta, and C gamma) have been identified each possessing distinct cAMP binding properties and resulting in different phosphorylation states. C subunit is activated through autophosphorylation and direct phosphorylation at Thr197 by PDK-1. Tissue specific expression of C gamma, indicates pressure on C gamma during evolution, acting to modulate it in a functionally specific way. Certain amino acid substitutions make C gamma a distinct member of the cAMP dependent subfamily of protein kinases, and suggest that C gamma may be distinct in its protein substrate specificity or its interaction with the different regulatory subunits.

Supplier: Bioss

PKA (or cAPK) is a cyclic AMP dependent protein kinase. When activated by the second messenger cAMP, PKA mediates diverse cellular mechanisms, including proliferation, ion transport, regulation of metabolism, plus gene transcription. PKA is comprised of two dimers of two subunits, R (regulatory) and C (catalytic). Two families of R subunit (RI and RII) and three C subunit isoforms (C alpha, C beta, and C gamma) have been identified each possessing distinct cAMP binding properties and resulting in different phosphorylation states. C subunit is activated through autophosphorylation and direct phosphorylation at Thr197 by PDK-1. Tissue specific expression of C gamma, indicates pressure on C gamma during evolution, acting to modulate it in a functionally specific way. Certain amino acid substitutions make C gamma a distinct member of the cAMP dependent subfamily of protein kinases, and suggest that C gamma may be distinct in its protein substrate specificity or its interaction with the different regulatory subunits.

Supplier: Prosci

LKB1 Antibody: The LKB1 serine/threonine protein kinase was initially identified as a tumor suppressor gene mutated in human Peutz-Jeghers syndrome (PJS), a condition resulting in the growth of numerous intestinal polyps classed as hamartomas. LKB1 exists as a heterotrimeric complex with two other proteins, Ste20-related adaptor protein (STRAD) and MO25. Together, this complex can phsophorylate and activate the AMP-activate protein kinase (AMPK). Following AMPK activation by LKB1, AMPK then phosphorylates TSC1 and TSC2, key components of the metabolism-regulating TOR signaling pathway, which antagonizes the activation for the TOR pathway. LKB1 has also been shown to play a fundamental role in controlling the spatial orientation of structures required to maintain an ordered, polarized epithelium.

Supplier: Prosci

This gene is a member of the type IV, cyclic AMP (cAMP)-specific, cyclic nucleotide phosphodiesterase (PDE) family. Cyclic nucleotides are important second messengers that regulate and mediate a number of cellular responses to extracellular signals, such as hormones, light, and neurotransmitters. The cyclic nucleotide phosphodiesterases (PDEs) regulate the cellular concentrations of cyclic nucleotides and thereby play a role in signal transduction. This gene encodes a protein that specifically hydrolyzes cAMP. Altered activity of this protein has been associated with schizophrenia and bipolar affective disorder. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.

Supplier: Prosci

GPAT1 Antibody: Glycerol-3-phosphate acyltransferase 1 (GPAT1), one of four known GPAT isoforms, is located on the mitochondrial outer membrane, allowing reciprocal regulation with carnitine palmitoyltransferase-1. It is thought to be critical for the development of hepatic steatosis; steatosis triggered by GPAT1 overexpression leads to hepatic and possibly peripheral insulin resistance. GPAT1 is transcriptionally upregulated by insulin and sterol regulatory element binding protein (SREBP-1) and downregulated by AMP-activated protein kinase. Mice deficient in GPAT1 exhibit decreased triacylglycerol (TAG) in cardiomyocytes even in high-fat diets, suggesting that GPAT1 contributes significantly to TAG accumulation in heart tissue during lipogenic or high fat diets.

Supplier: Prosci

It is well known that the control of gene expression involves activation of protein kinase cascades that regulate transcription factors within the nucleus (Karin and Hunter, 1995). The cyclic AMP response element binding protein (CREB) is one of the best characterized stimulus-induced transcription factors (Montminy, 1997). This transcription factor is a component of intracellular signaling events that regulate a wide range of biological functions, from spermatogenesis to circadian rhythms and memory (Shaywitz and Greenberg, 1999; Silva et al., 1998). A variety of protein kinases including protein kinase A (PKA), mitogenactivated protein kinases (MAPKs), and Ca2+/calmodulin-dependent protein kinases (CaMKs) phosphorylate CREB at serine 133 (Ser133), and phosphorylation of Ser133 are required for CREB-mediated transcription (Johannessen et al., 2004; Kornhauser et al., 2002).

Supplier: Novus Biologicals

The Adenylate Cyclase 2 Antibody from Novus Biologicals is a rabbit polyclonal antibody to Adenylate Cyclase 2. This antibody reacts with human. The Adenylate Cyclase 2 Antibody has been validated for the following applications: Immunohistochemistry, Immunohistochemistry-Paraffin.

Supplier: Prosci

The protein encoded by this gene is a catalytic subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status. In response to cellular metabolic stresses, AMPK is activated, and thus phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. Studies of the mouse counterpart suggest that this catalytic subunit may control whole-body insulin sensitivity and is necessary for maintaining myocardial energy homeostasis during ischemia.

Supplier: Peprotech

GPR15L is a newly identified ligand for GPR15, a member of the G protein-coupled receptor (GPCR) family. Upon ligation, GPR15L acts as a potent chemoattractant for GPR15-expressing T cells and together they mediate lymphocyte recruitment to the large intestine and skin. GPR15L is constitutively expressed by colon epithelial cells where its expression is minimally altered by intestinal inflammation. Conversely, GPR15L is nearly undetectable in adult epidermis but highly upregulated during wound healing and inflammation, particularly in psoriasis. Significant expression of GPR15L is also seen in additional mucosal epithelial cells, including those of the stomach, esophagus, and urinary tract. While maintaining similar expression patterns and intramolecular disulfide cysteine bridges found in members of the CC chemokine family, GPR15L differs from classic CC and CXC chemokines, whose active sites are found on the N-terminus, in that it relies on its C-terminus for receptor interaction. GPR15L was first identified as an antimicrobial peptide (AMP) due to its broad spectrum of antimicrobial activity, a property shared with many chemokines. GPR15L binds to an additional receptor, SUSD2, and early studies have indicated that both are downregulated in colon cancer tissue resulting in inhibited colon cancer growth. PeproTech's E. coli-derived Recombinant Human GPR15L consists of 57 amino acid residues and has a calculated molecular weight of 6.5 kDa.

Supplier: Rockland Immunochemical

Histidine triad nucleotide-binding protein 1 (HINT1) is a member of the histidine triad (HIT) protein family, a group of small nucleotide-binding and -hydrolyzing proteins. HINT1 interacts with several diverse proteins and has been suggested to have tumor suppressive activities. HINT1 catalyzes the hydrolysis of adenosine 5'-monophoramidate substrates such as AMP-morpholidate, but its enzymatic function does not appear to play a role in its tumor suppression. Recent experiments demonstrate that HINT1 forms a complex with POSH and JNK in vivo, inhibiting AP-1 activity and the phosphorylation of c-Jun, and this action could contribute to the tumor suppressor activity of HINT1. Other studies raise the possibility of HINT1 as a candidate gene for schizophrenia.

Supplier: Rockland Immunochemical

The LKB1 serine/threonine protein kinase was initially identified as a tumor suppressor gene mutated in human Peutz-Jeghers syndrome (PJS), a condition resulting in the growth of numerous intestinal polyps classed as hamartomas. LKB1 exists as a heterotrimeric complex with two other proteins, Ste20-related adaptor protein (STRAD) and MO25. Together, this complex can phsophorylate and activate the AMP-activate protein kinase (AMPK). Following AMPK activation by LKB1, AMPK then phosphorylates TSC1 and TSC2, key components of the metabolism-regulating TOR signaling pathway, which antagonizes the activation for the TOR pathway. LKB1 has also been shown to play a fundamental role in controlling the spatial orientation of structures required to maintain an ordered, polarized epithelium.

Supplier: Rockland Immunochemical

Glycerol-3-phosphate acyltransferase 1 (GPAT1), one of four known GPAT isoforms, is located on the mitochondrial outer membrane, allowing reciprocal regulation with carnitine palmitoyltransferase-1. It is thought to be critical for the development of hepatic steatosis; steatosis triggered by GPAT1 overexpression leads to hepatic and possibly peripheral insulin resistance. GPAT1 is transcriptionally upregulated by insulin and sterol regulatory element binding protein (SREBP-1) and downregulated by AMP-activated protein kinase. Mice deficient in GPAT1 exhibit decreased triacylglycerol (TAG) in cardiomyocytes even in high-fat diets, suggesting that GPAT1 contributes significantly to TAG accumulation in heart tissue during lipogenic or high fat diets. At least two isoforms of GPAT1 are known to exist.

Supplier: Prosci

BRSK2 Antibody: BRSK2 was initially identified through a computer screen of the human genome and shows significant homology to the C. elegans neuronal cell polarity regulator SAD1. BRSK2 is expressed in the brain and to a lesser extent in the testes. BRSK2 is a member of the AMP-activated protein kinase subfamily and can be activated by the tumor suppressor kinase LKB1. More recently, it has been shown that both BRSK2 and the related protein BRSK1 are required for mammalian neuronal polarization. While BRSK1- and BRSK2-null mice were viable, double-mutant mice died within two hours of birth. Neurons from these mice showed uniformly-sized neurites as opposed to the normal long axon and multiple shorter dendrites. These neurites also displayed both axonal and dendritic markers. BRSK2 has also been shown to be an autoantigen in paraneoplastic limbic encephalitis. At least four isoforms of BRSK2 are known to exist.

Supplier: Rockland Immunochemical

BRSK2 was initially identified through a computer screen of the human genome and shows significant homology to the C. elegans neuronal cell polarity regulator SAD1. BRSK2 is expressed in the brain and to a lesser extent in the testes. BRSK2 is a member of the AMP-activated protein kinase subfamily and can be activated by the tumor suppressor kinase LKB1. More recently, it has been shown that both BRSK2 and the related protein BRSK1 are required for mammalian neuronal polarization. While BRSK1- and BRSK2-null mice were viable, double-mutant mice died within two hours of birth. Neurons from these mice showed uniformly-sized neurites as opposed to the normal long axon and multiple shorter dendrites. These neurites also displayed both axonal and dendritic markers. BRSK2 has also been shown to be an autoantigen in paraneoplastic limbic encephalitis. At least four isoforms of BRSK2 are known to exist.

Supplier: Bioss

Vasopressin (AVP), the antidiuretic hormone, is a cyclic nonpeptide that is involved in the regulation of body fluid osmolality (1-3). AVP mediates its effects through a family of G-protein coupled receptors, the vasopressin receptors type V1a, V2 and V3 (also designated V1b) (1,2). The AVP receptor V1a is responsible for several functions, including blood vessel constriction, liver glycogenolysis and platelet adhesion (3). It is detected as a full length protein and a shorter protein, which results from proteolytic cleavage of its amino terminus (4). The V1a receptor is coupled to Gq/11 protein, which increases the intracellular calcium concentration (3). The human AVP receptor V2 gene maps to chromosome Xq28 and is expressed in lung and kidney (5,6). Mutations in the V2 receptor result in nephrogenic diabetes insipidus (NDI), a rare X-linked disorder characterized by the inability of the kidney to concentrate urine in response to AVP (5,7). The AVP Receptor V2 activates the Gs protein and the cyclic AMP second messenger system (7). The AVP receptor V3 is preferentially expressed in the pituitary and stimulates the release of adrenocorticotropic hormone (ACTH) in response to AVP by mobilizing intracellular calcium stores (8). AVP receptor antagonists may have potential therapeutic effects in hypertension, congestive heart failure, nephrotic syndrome and ACTH-secreting tumors (2).

Supplier: Bioss

ATF4 is a transcription factor that was originally identified as a widely expressed mammalian DNA binding protein that could bind a tax-responsive enhancer element in the LTR of HTLV1. The encoded protein was also isolated and characterized as the cAMP-response element binding protein 2 (CREB2). The protein encoded by this gene belongs to a family of DNA-binding proteins that includes the AP1 family of transcription factors, cAMP-response element binding proteins (CREBs) and CREB-like proteins. These transcription factors share a leucine zipper region that is involved in protein-protein interactions, located C-terminal to a stretch of basic amino acids that functions as a DNA binding domain (referenced from Entrez gene).

Supplier: Bioss

Vasopressin (AVP), the antidiuretic hormone, is a cyclic nonpeptide that is involved in the regulation of body fluid osmolality (1-3). AVP mediates its effects through a family of G-protein coupled receptors, the vasopressin receptors type V1a, V2 and V3 (also designated V1b) (1,2). The AVP receptor V1a is responsible for several functions, including blood vessel constriction, liver glycogenolysis and platelet adhesion (3). It is detected as a full length protein and a shorter protein, which results from proteolytic cleavage of its amino terminus (4). The V1a receptor is coupled to Gq/11 protein, which increases the intracellular calcium concentration (3). The human AVP receptor V2 gene maps to chromosome Xq28 and is expressed in lung and kidney (5,6). Mutations in the V2 receptor result in nephrogenic diabetes insipidus (NDI), a rare X-linked disorder characterized by the inability of the kidney to concentrate urine in response to AVP (5,7). The AVP Receptor V2 activates the Gs protein and the cyclic AMP second messenger system (7). The AVP receptor V3 is preferentially expressed in the pituitary and stimulates the release of adrenocorticotropic hormone (ACTH) in response to AVP by mobilizing intracellular calcium stores (8). AVP receptor antagonists may have potential therapeutic effects in hypertension, congestive heart failure, nephrotic syndrome and ACTH-secreting tumors (2).

Supplier: Bioss

Vasopressin (AVP), the antidiuretic hormone, is a cyclic nonpeptide that is involved in the regulation of body fluid osmolality (1-3). AVP mediates its effects through a family of G-protein coupled receptors, the vasopressin receptors type V1a, V2 and V3 (also designated V1b) (1,2). The AVP receptor V1a is responsible for several functions, including blood vessel constriction, liver glycogenolysis and platelet adhesion (3). It is detected as a full length protein and a shorter protein, which results from proteolytic cleavage of its amino terminus (4). The V1a receptor is coupled to Gq/11 protein, which increases the intracellular calcium concentration (3). The human AVP receptor V2 gene maps to chromosome Xq28 and is expressed in lung and kidney (5,6). Mutations in the V2 receptor result in nephrogenic diabetes insipidus (NDI), a rare X-linked disorder characterized by the inability of the kidney to concentrate urine in response to AVP (5,7). The AVP Receptor V2 activates the Gs protein and the cyclic AMP second messenger system (7). The AVP receptor V3 is preferentially expressed in the pituitary and stimulates the release of adrenocorticotropic hormone (ACTH) in response to AVP by mobilizing intracellular calcium stores (8). AVP receptor antagonists may have potential therapeutic effects in hypertension, congestive heart failure, nephrotic syndrome and ACTH-secreting tumors (2).

Supplier: Bioss

ATF4 is a transcription factor that was originally identified as a widely expressed mammalian DNA binding protein that could bind a tax-responsive enhancer element in the LTR of HTLV1. The encoded protein was also isolated and characterized as the cAMP-response element binding protein 2 (CREB2). The protein encoded by this gene belongs to a family of DNA-binding proteins that includes the AP1 family of transcription factors, cAMP-response element binding proteins (CREBs) and CREB-like proteins. These transcription factors share a leucine zipper region that is involved in protein-protein interactions, located C-terminal to a stretch of basic amino acids that functions as a DNA binding domain (referenced from Entrez gene).

Supplier: ALADDIN SCIENTIFIC

AMP PNP ≥90% (by HPLC)

Supplier: Bioss

Clenbuterol belongs to the group of agonists. In livestock production clenbuterol improves the meat/fat ratio in fattened animals or accelerate the growth. Up to now agonists have not been authorized as adjuvants for fattening. In addition to its lipolytic and anabolic effect, clenbuterol has a relaxing effect on non-striated musculature on which is based its therapeutic use as an antiasthmatic and a tocolytic agent. When employed as a fattening adjuvant, as compared with the therapeutic use, clenbuterol is administered in a 5 to 10 times higher dose. Therefore, it is possible that clenbuterol residues may lead to a risk for consumers after illegal administration.Using the clenbuterol monocalantibody, it is possible to detect clenbuterol and other agonists in urine, muscle and liver both rapidly and with accuracy. Clenbuterol is a long acting beta 2 adrenergic agonist. Like other beta 2 agonists, clenbuterol is believed to act by stimulating production of cyclic AMP through the activation of adenyl cyclase. By definition, Beta 2 agonists have more smooth muscle relaxation activity (bronchial, vascular and uterine smooth muscle) versus its cardiac effects (Beta 1).