20% off purchase of 3 or more products* | Learn More >>

Polyclonal Antibody Heme Metabolic Process

Also showing Polyclonal Antibody Western Blotting Heme Metabolic Process

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Heme oxygenase (HO) is the rate-limiting enzyme in the catabolism of heme that results in the release of carbon monoxide, iron, and biliverdin (1). The products of this enzymatic reaction play important biological roles in antioxidant, anti-inflammatory and cytoprotective functions (2). Heme oxygenase comprises two isozymes, including the constitutively expressed HO-2 isozyme and the inducible HO-1 isozyme (3). Inducible HO-1 is expressed as an adaptive response to several stimuli, including heme, metals, and hormones (4). The induction of HO-1 has been implicated in numerous disease states, such as transplant rejection, hypertension, atherosclerosis, Alzheimer disease, endotoxic shock, diabetes, inflammation, and neurological disorders (1,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Heme oxygenase (HO) is the rate-limiting enzyme in the catabolism of heme that results in the release of carbon monoxide, iron, and biliverdin (1). The products of this enzymatic reaction play important biological roles in antioxidant, anti-inflammatory and cytoprotective functions (2). Heme oxygenase comprises two isozymes, including the constitutively expressed HO-2 isozyme and the inducible HO-1 isozyme (3). Inducible HO-1 is expressed as an adaptive response to several stimuli, including heme, metals, and hormones (4). The induction of HO-1 has been implicated in numerous disease states, such as transplant rejection, hypertension, atherosclerosis, Alzheimer disease, endotoxic shock, diabetes, inflammation, and neurological disorders (1,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Glucuronidation is a major pathway that enhances the elimination of lipophilic xenobiotics and endobiotics to more more water soluble compounds for excretion (1,2). The UDP-glucuronosyltransferase (UGT) superfamily catalyzes the glucuronidation of the glycosyl group of a nucleotide sugar to a variety of endogenous and exogenous compounds. Over 100 UGT mammalian gene products have been described and have been divided into subfamilies based on sequence identities (3). The UGT1 subfamily consists of a number of gene products resulting from alternative splicing. These UGT products can differ in tissue expression and substrate specificity. Also, marked differences in the individual expression of UGT isoforms can account for differences in drug metabolism.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: ABCG2 (BCRP1/ABCP/MXR) is a member of the ATP-binding cassette transporter family that functions as ATP-dependent transporters for a wide variety of chemical compounds and are associated with drug-resistance in cancer cells (1-6). ABCG2 is a heavily glycosylated transmembrane protein with six transmembrane spanning regions consistent with it functioning as a half-transporter. The ABC family can exist as either full-length transporters or as half-transporters that form functional transporters through homo- or heterodimerization. High expression of ABCG2 was found in placenta as well as cell lines selected for resistance to a number of chemotherapeutic drugs, including mitoxantrone, doxorubicin, topotecan and flavopiridol. In rodents, the highest expression of ABCG2 was found in kidney (8). ABCG2 expression has also been observed in stem cell populations, particularly in hematopoietic and neuronal stem cells and is downregulated with differentiation (9-12).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The ATPase inhibitor factor 1 (ATPIF1) gene encodes a mitochondrial ATPase inhibitor that limits ATP depletion when mitochondrial respiration is impaired (1). ATPIF1 becomes activated following a drop in pH, binding to β-F1-ATPase, thereby inhibiting the hydrolase activity of the H+-ATP synthase (1,2). In addition to its role as an ATP hydrolase, ATPIF1 has also been shown to play a regulatory role in cellular energy metabolism by triggering the induction of aerobic glycolysis in cancer cells resulting in their Warburg phenotype (3,4). Research studies demonstrate that the overexpression of ATPIF1 in several human carcinomas further supports its participation in oncogenesis and provides insight into the altered metabolism of cancer cells, which includes the reprogramming of energetic metabolism toward glycolysis (3).