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Rat Carboxylic Acid Binding

Also showing Mouse Carboxylic Acid Binding, Human Carboxylic Acid Binding

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

Application Methods: Western Blotting

Background: Glutamate oxaloacetate transaminase 1 (GOT1) catalyzes the interconversion of aspartate and oxaloacetate (1). The increased transamination primarily catalyzed by GOT1 leads to elevated levels of 2-hydroxyglutarate, which promotes methylation of the Foxp3 gene locus, inhibits Foxp3 expression and activates T helper 17 (TH17) cell differentiation (2). In addition, GOT1 is critical to the survival of cells with electron transport chain inhibition by generating aspartate, a metabolite determining the proliferation of these cells (3-4). Studies also show that GOT1 plays a key role in the noncanonical glutamine pathway that supports liver tumorigenesis (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Aldo-keto reductase family 1 member C2 (AKR1C2) is a member of a large superfamily of aldo-keto reductases that metabolize an array of substrates in a NADPH-dependent manner. AKR1C2 is the 3-α-hydroxysteroid dehydrogenase (3α-HSD) responsible for metabolizing and inactivating the androgen hormone 5α-dihydrotestosterone (DHT) to 3α-androstanediol (1). Research studies demonstrate an increase in AKR1C2 expression in cases of advanced prostate cancer (2). Both AKR1C2 and the related reductase, AKR1C3, are implicated in enhancing PI3K/Akt signaling in prostate cancer by reducing prostaglandin D2 to the more stable 9α, 11β-PGF2α (2). In addition, research studies demonstrate an increase in AKR1C2 expression in some ovarian endometriosis specimens, suggesting the participation of AKR1C2 in the promotion of progesterone metabolism in ovarian endometriosis (3).

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

Application Methods: Western Blotting

Background: FIH (Factor inhibiting HIF-1, HIF asparagine hydroxylase) is a dioxygen-dependent asparaginyl hydroxylase that modifies target protein function by hydroxylating target protein asparagine residues (1-3). Hypoxia-inducible factor (HIF), a transcriptional activator involved in control of cell cycle in response to hypoxic conditions, is an important target for FIH regulation. FIH functions as an oxygen sensor that regulates HIF function by hydroxylating at Asn803 in the carboxy-terminal transactivation domain (CAD) of HIF (4,5). During normoxia, FIH uses cellular oxygen to hydroxylate HIF-1 and prevent interaction of HIF-1 with transcriptional coactivators, including the CBP/p300-interacting transactivator. Under hypoxic conditions, FIH remains inactive and does not inhibit HIF, allowing the activator to regulate transcription of genes in response to low oxygen conditions (4-6). FIH activity is regulated in through interaction with proteins, including Siah-1, which targets FIH for proteasomal degradation (7). The Cut-like homeodomain protein CDP can bind the FIH promoter region to regulate FIH expression at the transcriptional level (8). Phosphorylation of HIF at Thr796 also can prevent FIH hydroxylation on Asn803 (9). Potential FIH substrates also include proteins with ankyrin repeat domains, such as Iκ-B, Notch, and ASB4 (10-12).

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

Application Methods: Western Blotting

Background: Phosphoenolpyruvate carboxykinase 1 (PCK1, PEPCK1 or PEPCK-C) is a cytosolic enzyme responsible for the conversion of oxaloacetate to phosphoenolpyruvate (1). PCK1 is involved in controlling the rate-limiting step of gluconeogenesis in the liver, which generates glucose from non-carbohydrate substrates such as lactate and glycerol (2). The deacetylase SirT1 stimulates transcription of PCK1 and glucose-6-phosphatase to activate gluconeogenesis (3). Depending on nutritional state, Stat3 can inhibit PCK1 and glucose-6-phosphatase expression and suppress gluconeogenesis (4). Relatively high glucose concentration can result in acetylation of PCK1 by P300 acetyltransferase, promoting an interaction between PCK1 and the E3 ligase UBR5 that leads to the PCK1 destabilization (5).