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The protein encoded by FH is an enzymatic component of the tricarboxylic acid (TCA) cycle, or Krebs cycle, and catalyzes the formation of L-malate from fumarate. Additionally we are shipping FH Antibodies (194) and FH Kits (24) and many more products for this protein.
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we aimed in this study to examine these common functional pathways in uterine leiomyomas (ULM)with different driver mutations. We collected ULM with MED12, HMGA2, and FH mutations and examined the selected markers by immunohistochemistry.
Induction of ferroptosis in fumarate hydratase-inactivated tumors represents an opportunity for synthetic lethality in cancer.
A case series of 2 sisters in their 20s who presented with isolated uterine leiomyomas and were found to carry a novel mutation for the fumarate hydratase gene.
The clinical spectrum associated with hereditary leiomyomatosis and renal cell carcinoma (show MOK Proteins) syndrome in French FH mutation carriers has been reassessed.
As with many emerging cancer syndromes, the phenotypic spectrum ofhereditary leiomyomatosis and renal cell cancer( HLRCC) is likely to expand as the FH gene becomes incorporated on more multiplex germline panels, which will also help to clarify the potential involvement of other tumor types in HLRCC
We show that the mechanism of fumarate hydratase distribution is alternative transcription initiation from a broad promoter.
fumarate increases ferritin (show FTL Proteins) gene transcription by activating the NRF2 (show GABPA Proteins) (nuclear factor [erythroid-derived 2]-like 2) transcription factor.
FH-Ser75 phosphorylation level inversely correlates with the OGT (show OGT Proteins) level and poor prognosis in pancreatic cancer patients. Report mechanism underlying transcription regulation by FH and the linkage between dysregulated OGT (show OGT Proteins) activity and growth advantage of cancer cells under glucose deficiency.
Loss of FH immunohistochemical (IHC) expression in cutaneous leiomyomas is a sensitive and specific marker for detection of hereditary leiomyomatosis and renal cell carcinoma (show MOK Proteins) (HLRCC). FH expression by IHC was absent in 9 specimens and retained in 85 specimens and 2 cases were equivocal with minimal FH expression while succinate dehydrogenase B (show SDHB Proteins) expression was retained in 95 specimens and equivocal in 1 specimen.
LSH (show HELLS Proteins) promoted cancer progression in part by regulating expression of fumarate hydratase (FH).
roles for fumarate metabolism in hematopoietic stem cell (HSC) maintenance and hematopoietic differentiation and reveal a differential requirement for mitochondrial Fh1 in normal hematopoiesis and leukemia propagation.
Adipose-Specific Deficiency of Fumarate Hydratase in Mice Protects Against Obesity, Hepatic Steatosis, and Insulin (show INS Proteins) Resistance.
Reexpression of cytosolic FH in FH1-deficient mice is critical for the suppression of renal cyst development and restoration of defects in the arginine biosynthesis pathway.
Tumor-derived FH and SDH (show SDS Proteins) mutations accumulate fumarate and succinate, leading to enzymatic inhibition of multiple alpha-KG-dependent dioxygenases and consequent alterations of genome-wide histone and DNA methylation (show HELLS Proteins).
identification of a metabolic pathway that is induced in Fh1-deficient cells to demonstrate that inhibition of haem oxygenation is synthetically lethal when combined with Fh1 deficiency, providing a new potential target for treating HLRCC patients
These experiments demonstrated that upregulation of HIF-1alpha (show HIF1A Proteins) occurs as a direct consequence of FH inactivation.
progression of tumors where FH is lost might be boosted by activation of the MET oncogene (show RAB1A Proteins), which is able to drive cell-autonomous tumor progression
The protein encoded by this gene is an enzymatic component of the tricarboxylic acid (TCA) cycle, or Krebs cycle, and catalyzes the formation of L-malate from fumarate. It exists in both a cytosolic form and an N-terminal extended form, differing only in the translation start site used. The N-terminal extended form is targeted to the mitochondrion, where the removal of the extension generates the same form as in the cytoplasm. It is similar to some thermostable class II fumarases and functions as a homotetramer. Mutations in this gene can cause fumarase deficiency and lead to progressive encephalopathy.
fumarate hydratase, mitochondrial
, fumarate hydratase
, fumarate hydratase 1