No Products on your Comparison List.
Your basket is empty.
Find out more
Show all species
Show all synonyms
Select your species and application
anti-Human CYP3A7 Antibodies:
anti-Rat (Rattus) CYP3A7 Antibodies:
anti-Mouse (Murine) CYP3A7 Antibodies:
Go to our pre-filtered search.
Human Monoclonal CYP3A7 Primary Antibody for IHC (p), ELISA - ABIN533617
Kumarakulasingham, Rooney, Dundas, Telfer, Melvin, Curran, Murray: Cytochrome p450 profile of colorectal cancer: identification of markers of prognosis. in Clinical cancer research : an official journal of the American Association for Cancer Research 2005
Show all 3 Pubmed References
Cow (Bovine) Polyclonal CYP3A7 Primary Antibody for WB - ABIN2776998
Sim, Edwards, Boobis, Ingelman-Sundberg: CYP3A7 protein expression is high in a fraction of adult human livers and partially associated with the CYP3A7*1C allele. in Pharmacogenetics and genomics 2005
Show all 2 Pubmed References
CYP3A7 rs2257401 is associated with tacrolimus pharmacokinetics in kidney transplantation.
our data indicate an alternative binding mode for testosterone in CYP3A7 that favors the 2alpha-hydroxylation, suggesting significant structural differences in its active site compared with CYP3A4/5
polymorphisms may modify the response to dietary methylmercury exposure during early life development
Methylation status of cytosine in the CYP3A7 proximal promoter correlated with changes in developmental expression of mRNA.
Occupancy by modified histones was consistent with chromatin structural changes contributing to the mechanisms regulating CYP3A7 ontogeny.
All three neonicotinoid pesticides induced the expression of CYP3A7 in H295R cells; induction was reversed by co-treatment of H295R cells with exogenous estriol. CYP3A7 is normally expressed in fetal liver and is a key enzyme involved in estriol synthesis.
The CYP3A7*1C allele is associated with a lower urinary estrone levels, a more pronounced reduction in 2-hydroxylation pathway estrone metabolites (EMs) and a lower ratio of 2-hydroxylation:16alpha-hydroxylation EMs in premenopausal women.
data suggested that hepatocyte nuclear factor 4 alpha and glucocorticoid receptor, and epigenetic changes of H3K4me2 and H3K27me3 are associated with the ontogenic expressions of CYP3A4/3A7 in the livers of the Chinese Han population.
These results suggest the existence of a marked inter-individual variability regarding the presence of the isoforms of CYP3A. In addition, since sorafenib is metabolized by CYP3A4, but not by CYP3A7, an overexpression of CYP3A4 may lead to an increase in the degradation of the drug and then to clinical ineffectiveness.
CYP3A7*1C influences outcome are required.
CYP3A4, CYP3A7, UGT2B11 and UGT2B15 genes are significantly downregulated in melanosis coli.
Differences in the expression of nuclear receptors might determine the variability in CYP3A4 and CYP3A7 expression observed in foetal liver.
Only CYP1A1, CYP1B1, CYP3A4, CYP3A5 and CYP3A7 expressed in lymphocytes and monocytes.
Report CYP3A7 metabolism of inhaled glucocorticoids.
Report distinctive response patterns of HIF-1alpha, CYP3A4 and CYP3A7 to cobalt chloride in human fetal liver cells.
Expression and regulation of human fetal-specific CYP3A7 in mice
There were no statistically significant differences in the distribution of CYP3A7 polymorphic alleles between testicular cancer cases and controls suggesting no contribution to individual susceptibility to testicular cancer.
Recombinant CYP3A4, CYP3A5 and CYP3A7 metabolized R- and S-warfarin to 10- and 4'-hydroxywarfarin with efficiencies that depended on the individual enzymes.
Data show that both isoforms of CYP3A7 did not metabolize the anti-cancer drug sorafenib, and suggest that CYP3A7 activity does not influence the effectiveness of this anti-cancer drug against HCC.
The single nucleotide polymorphism P450 oxidoreductase*28 seems to be a better genetic marker of the variability of total CYP3A activity in vivo than CYP3A4, CYP3A5 and CYP3A7 genetic variants.
This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This enzyme hydroxylates testosterone and dehydroepiandrosterone 3-sulphate, which is involved in the formation of estriol during pregnancy. The enzyme also metabolizes some drugs such as aflatoxin B1. This gene is part of a cluster of cytochrome P450 genes on chromosome 7q21.1. Transcript variants have been described, but it is not known whether these transcripts are normally produced. This gene undergoes readthrough transcription with the downstream CYP3AP1 pseudogene, resulting in an isoform with a novel C-terminus, as represented in GeneID:100861540.
cytochrome P450 3A7
, aryl hydrocarbon hydroxylase
, cytochrome P450, subfamily IIIA, polypeptide 7
, cytochrome P450-HFLA
, flavoprotein-linked monooxygenase
, microsomal monooxygenase
, xenobiotic monooxygenase