"mthlcyclohexanol&amp"

Supplier: ProSci Inc.

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. At least two isoforms of GPAT1 are known to exist.

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).

Supplier: AbFrontier

Mitogen- and stress-activated protein kinases (MSK2) is nuclear kinase that act downstream of mitogen-activated protein/extracellular signal-regulated kinase pathways. It contains two kinase domains in the N-terminal and C-terminal region, respectively. MSK2 is activated in response to mitogenic stimuli via Erk1/2MAPK pathway and also by stress stimuli via p38MAPK pathway. Signals from mitogens and cellular stresses are involved in many functions including cell proliferation, differentiation, and survival through the phosphorylation of cyclic AMP response element-binding protein (CREB) at Ser133 which is catalyzed by MSK2. Recently, MSK2 has been shown to be required for stress-induced phosphorylation of histone H3-Ser and transcriptional activation of several immediate early genes.

Supplier: Biorbyt

Anti-AMPD3 Rabbit Polyclonal Antibody

Supplier: ProSci Inc.

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 Inc.

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: Biorbyt

Anti-CAP1 Rabbit Polyclonal Antibody

Supplier: Biorbyt

Anti-PPP1R1B Rabbit Polyclonal Antibody

Supplier: Biorbyt

Anti-PPP1R1B Rabbit Polyclonal Antibody

Supplier: Antibodies.com

cAMP ELISA kit is a competitive Enzyme-Linked Immunosorbent Assay (cELISA) designed for the in vitro quantitative determination of cAMP in cell lysate and other liquid samples.

Supplier: ProSci Inc.

Cyclic AMP-dependent transcription factor ATF-1(ATF1) which contains 1 bZIP (basic-leucine zipper) domain and 1 KID (kinase-inducible) domain, belongs to the bZIP family. It influences cellular physiologic processes by regulating the expression of downstream target genes, which are related to growth, survival, and other cellular activities. ATF1 binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular promoters. It also binds to the Tax-responsive element (TRE) of HTLV-I. ATF1 mediates PKA-induced stimulation of CRE-reporter genes, represses the expression of FTH1 and other antioxidant detoxification genes, triggers cell proliferation and transformation. ATF1 is phosphorylated at serine 63 in its kinase-inducible domain by serine/threonine kinases, cAMP-dependent protein kinase A, calmodulin-dependent protein kinase I/II, mitogen- and stress-activated protein kinase and CDK3. Its phosphorylation enhances its transactivation and transcriptional activities, and enhances cell transformation.

Supplier: Biorbyt

Anti-AMPD3 Rabbit Polyclonal Antibody (FITC (Fluorescein))

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

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

CECR1 is a member of the adenosine and AMP deaminases family. It may act as a growth factor and have adenosine deaminase activity. It is a candidate gene for cat eye syndrome. Two transcript variants encoding distinct isoforms have been identified for this gene.Adenosine deaminase is an enzyme that is present in most tissues and exists predominantly as a monomer, although in some tissues it is associated with adenosine deaminase-binding protein. Adenosine deaminase degrades extracellular adenosine, which is toxic for lymphocytes. A novel family of growth factors that share sequence similarity to adenosine deaminase has been identified. The cat eye syndrome critical region protein (CECR) family includes CECR1, CECR2, CECR3, CECR4, CECR5, CECR6, CECR7, CECR8 and CECR9. The genes encoding CECR proteins are candidates for Cat Eye Syndrome (CES), a developmental disorder associated with the duplication of a 2 Mb region of 22q11.2. CES is characterized by the combination of coloboma of the iris and anal atresia with fistula, downslanting palpebral fissures, preauricular tags and/or pits, frequent occurrence of heart and renal malformations, and normal or near-normal mental development. CECR family members are widely expressed. Specifically, CECR1 has the highest expression in adult heart, lung, lymphoblasts and placenta. CECR2 is also involved in neurulation and chromatin remodeling. Mutations in the CECR2 gene result in neural tube defects.