Description: FABP1 is primarily expressed in the liver where it is involved in the binding, transport and metabolism of long-chain fatty acids (LCFAs) and other hydrophobic molecules. Altered expression of the protein has been linked to metabolic conditions including obesity. [Wiki]

Description: Fatty acid binding protein 1, liver, also known as FABP1 or FABPL, is a human gene locating at 2p11. FABP1 encodes the fatty acid binding protein found in liver. Fatty acid binding proteins are a family of small, highly conserved, cytoplasmic proteins that bind free fatty acids, their CoA derivatives, bilirubin, organic anions, and other small molecules. FABP1 and FABP6 (the ileal fatty acid binding protein) are also able to bind bile acids. It is thought that FABPs roles include fatty acid uptake, transport, and metaboism. The liver form of FABP may be identical to the major liver protein-1 (Lvp-1), which is encoded by a gene situated within 1 cM of Ly-2.

Description: Fatty acid binding protein 1, liver, also known as FABP1 or FABPL, is a human gene locating at 2p11. FABP1 encodes the fatty acid binding protein found in liver. Fatty acid binding proteins are a family of small, highly conserved, cytoplasmic proteins that bind free fatty acids, their CoA derivatives, bilirubin, organic anions, and other small molecules. FABP1 and FABP6 (the ileal fatty acid binding protein) are also able to bind bile acids. It is thought that FABPs roles include fatty acid uptake, transport, and metaboism. The liver form of FABP may be identical to the major liver protein-1 (Lvp-1), which is encoded by a gene situated within 1 cM of Ly-2.

Description: This gene encodes the fatty acid binding protein found in liver. Fatty acid binding proteins are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. This protein and FABP6 (the ileal fatty acid binding protein) are also able to bind bile acids. It is thought that FABPs roles include fatty acid uptake, transport, and metabolism. [RefSeq]

Description: Antibody raised against liver Arginase

Description: Antibody raised against liver Arginase

Description: Recombinant Fab monoclonal FABP antibody (liver specific)

Description: Primary antibody against Liver Canuliculi(HSA98), CF680R conjugate, Concentration: 0.1mg/mL

Description: Primary antibody against Liver Canuliculi(HSA98), CF680R conjugate, Concentration: 0.1mg/mL

Description: Primary antibody against Liver Canuliculi(HSA98), CF543 conjugate, Concentration: 0.1mg/mL

Description: Primary antibody against Liver Canuliculi(HSA98), CF543 conjugate, Concentration: 0.1mg/mL

Description: Primary antibody against Liver Canuliculi(HSA98), CF405M conjugate, Concentration: 0.1mg/mL

Description: Primary antibody against Liver Canuliculi(HSA98), CF405M conjugate, Concentration: 0.1mg/mL

Description: Primary antibody against Liver Canuliculi(HSA98), CF555 conjugate, Concentration: 0.1mg/mL

Description: Primary antibody against Liver Canuliculi(HSA98), CF555 conjugate, Concentration: 0.1mg/mL

Description: Primary antibody against Liver Canuliculi(HSA98), CF660R conjugate, Concentration: 0.1mg/mL

Description: Primary antibody against Liver Canuliculi(HSA98), CF660R conjugate, Concentration: 0.1mg/mL

Description: Primary antibody against Liver Canuliculi(HSA98), CF680 conjugate, Concentration: 0.1mg/mL

Description: Primary antibody against Liver Canuliculi(HSA98), CF680 conjugate, Concentration: 0.1mg/mL

Description: Primary antibody against Liver Canuliculi(HSA98), CF770 conjugate, Concentration: 0.1mg/mL

Description: Primary antibody against Liver Canuliculi(HSA98), CF770 conjugate, Concentration: 0.1mg/mL

Description: Primary antibody against Liver Canuliculi(HSA98), PerCP conjugate, Concentration: 0.1mg/mL

Description: Primary antibody against Liver Canuliculi(HSA98), RPE conjugate, Concentration: 0.1mg/mL

Description: Primary antibody against Liver Canuliculi(HSA98), APC conjugate, Concentration: 0.1mg/mL

Description: Primary antibody against Liver Canuliculi(HSA98), Alkaline Phosphatase conjugate, Concentration: 0.1mg/mL

Description: Primary antibody against Liver Canuliculi(HSA98), Alkaline Phosphatase conjugate, Concentration: 0.1mg/mL

Description: Primary antibody against Liver Canuliculi(HSA98), Horseradish Peroxidase conjugate, Concentration: 0.1mg/mL

Description: Primary antibody against Liver Canuliculi(HSA98), Horseradish Peroxidase conjugate, Concentration: 0.1mg/mL

Description: There are at least four distinct but related alkaline phosphatases: intestinal, placental, placental-like, and liver/bone/kidney (tissue non-specific). The genes for the first three are located together on chromosome 2 while the tissue non-specific form is located on chromosome 1. This protein is a membrane bound glycosylated enzyme that is not expressed in any particular tissue and is, therefore, referred to as the tissue-nonspecific form of the enzyme. The exact physiological function of the alkaline phosphatases is not known. A proposed function of this form of the enzyme is matrix mineralization, however, mice that lack a functional form of this enzyme show normal skeletal development. This enzyme has been linked directly to a disorder known as hypophosphatasia, a disorder that is characterized by hypercalcemia and includes skeletal defects. The character of this disorder can vary, however, depending on the specific mutation since this determines age of onset and severity of symptoms.

Description: There are at least four distinct but related alkaline phosphatases: intestinal, placental, placental-like, and liver/bone/kidney (tissue non-specific). The genes for the first three are located together on chromosome 2 while the tissue non-specific form is located on chromosome 1. This protein is a membrane bound glycosylated enzyme that is not expressed in any particular tissue and is, therefore, referred to as the tissue-nonspecific form of the enzyme. The exact physiological function of the alkaline phosphatases is not known. A proposed function of this form of the enzyme is matrix mineralization, however, mice that lack a functional form of this enzyme show normal skeletal development. This enzyme has been linked directly to a disorder known as hypophosphatasia, a disorder that is characterized by hypercalcemia and includes skeletal defects. The character of this disorder can vary, however, depending on the specific mutation since this determines age of onset and severity of symptoms.

Description: LKB1 is a tumor suppressor serine/threonine-protein kinase that controls the activity of AMP-activated protein kinase (AMPK) family members, thereby playing a role in various processes such as cell metabolism, cell polarity, apoptosis and DNA damage response. Acts by phosphorylating the T-loop of AMPK family proteins, thus promoting their activity: phosphorylates PRKAA1, PRKAA2, BRSK1, BRSK2, MARK1, MARK2, MARK3, MARK4, NUAK1, NUAK2, SIK1, SIK2, SIK3 and SNRK but not MELK. Also phosphorylates non-AMPK family proteins such as STRADA, PTEN and possibly p53/TP53. Acts as a key upstream regulator of AMPK by mediating phosphorylation and activation of AMPK catalytic subunits PRKAA1 and PRKAA2 and thereby regulates processes including: inhibition of signaling pathways that promote cell growth and proliferation when energy levels are low, glucose homeostasis in liver, activation of autophagy when cells undergo nutrient deprivation, and B-cell differentiation in the germinal center in response to DNA damage. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton. Required for cortical neuron polarization by mediating phosphorylation and activation of BRSK1 and BRSK2, leading to axon initiation and specification. Involved in DNA damage response: interacts with p53/TP53 and recruited to the CDKN1A/WAF1 promoter to participate in transcription activation. Able to phosphorylate p53/TP53; the relevance of such result in vivo is however unclear and phosphorylation may be indirect and mediated by downstream STK11/LKB1 kinase NUAK1. Also acts as a mediator of p53/TP53-dependent apoptosis via interaction with p53/TP53: translocates to the mitochondrion during apoptosis and regulates p53/TP53-dependent apoptosis pathways. In vein endothelial cells, inhibits PI3K/Akt signaling activity and thus induces apoptosis in response to the oxidant peroxynitrite (in vitro). Regulates UV radiation-induced DNA damage response mediated by CDKN1A. In association with NUAK1, phosphorylates CDKN1A in response to UV radiation and contributes to its degradation which is necessary for optimal DNA repair. [UniProt]

Description: STK11, is a member of the serine/threonine kinase family, regulates cell polarity and functions as a tumor suppressor. Mutations in STK11 have been associated with Peutz-Jeghers syndrome, an autosomal dominant disorder characterized by the growth of polyps in the gastrointestinal tract, pigmented macules on the skin and mouth, and other neoplasms.

Description: LKB1 is a tumor suppressor serine/threonine-protein kinase that controls the activity of AMP-activated protein kinase (AMPK) family members, thereby playing a role in various processes such as cell metabolism, cell polarity, apoptosis and DNA damage response. Acts as a key upstream regulator of AMPK by mediating phosphorylation and activation of AMPK catalytic subunits PRKAA1 and PRKAA2 and thereby regulates processes including: inhibition of signaling pathways that promote cell growth and proliferation when energy levels are low, glucose homeostasis in liver, activation of autophagy when cells undergo nutrient deprivation, and B-cell differentiation in the germinal center in response to DNA damage. [UniProt]