Fumarase/FH Recombinant Protein | FH recombinant protein

Recombinant Fumarase/FH protein

Cat. Num. AAA389337

• Gene Names: FH; MCL; LRCC; HLRCC; MCUL1
• Synonyms: Fumarase/FH; Recombinant Fumarase/FH protein; Fumarate Hydratase; (S)-malate hydro-lyase (fumarate-forming); FH recombinant protein

• Host: E Coli
• Form/Format: Recombinant Fumarase/FH protein is supplied in 25mM Tris-HCl pH7.4, 300mM NaCl, 10% glycerol, and 0.5mM TCEP.

• Protein Species: Human
• Tag: His-Tag
• Notes: This product was manufactured as described in Protein Details. Where possible, We has developed functional or activity assays for recombinant proteins. Additional characterization such as enzyme kinetic activity assays, inhibitor screening or other biological activity assays may not have been performed for every product. All available data for a given product is shown on the lot-specific Technical Data Sheet.
• Dry Ice Shipment: Extra charge fee may add to your shipping cost as dry ice is required to ship this product.
• Preparation and Storage: Recombinant proteins in solution are temperature sensitive and must be stored at -80 degree C to prevent degradation. Avoid repeated freeze/thaw cycles and keep on ice when not in storage.; Shipping Temp: Dry Ice

SDS-Page

(Recombinant Fumarase / FH protein gel 10% SDS-PAGE with Coomassie blue staining MW: 58.2 kDa Purity: >70%)

Related Product Information for FH recombinant protein

Short Description: Full-length Fumarase/FH protein (accession number NP_000134.2) was expressed in E Coli with an N-terminal 6xHis-tag. The molecular weight of the protein is 58.2 kDa.

Background: Fumarase (Fumarate Hydratase), also called as FH, 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. Fumarase (FH) catalyzes the reversible hydration and dehydration of fumarate to malate in the tricarboxylic-acid cycle to facilitate a transition step in the production of energy in the form of NADH. In the cytosol, FH metabolizes fumarate, which is a byproduct of the urea cycle and amino acid catabolism. Besides, FH translocates from the cytosol into the nucleus upon DNA damage. They are very important targets both in the study of human metabolic disorders and as potential therapeutic targets in neglected tropical diseases and tuberculosis.

Product Categories/Family for FH recombinant protein

Recombinant Proteins

NCBI and Uniprot Product Information

• NCBI GI #: 19743875
• NCBI GeneID: 2271
• NCBI Accession #: NP_000134.2
• NCBI GenBank Nucleotide #: NM_000143.3
• UniProt Accession #: P07954
• Molecular Weight: 54,637 Da
• NCBI Official Full Name: fumarate hydratase, mitochondrial
• NCBI Official Synonym Full Names: fumarate hydratase
• NCBI Official Symbol: FH
• NCBI Official Synonym Symbols: MCL; LRCC; HLRCC; MCUL1
• NCBI Protein Information: fumarate hydratase, mitochondrial; fumarase
• UniProt Protein Name: Fumarate hydratase, mitochondrial
• UniProt Gene Name: FH
• UniProt Synonym Gene Names: Fumarase
• UniProt Entry Name: FUMH_HUMAN

NCBI Description

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. [provided by RefSeq, Jul 2008]

Uniprot Description

FH: a metabolic enzyme that participates in the tricarboxylic acid cycle that catalyzes the conversion of (S)-malate into fumarate + H2O. There are two substrate binding sites: the catalytic A site, and the non-catalytic B site that may play a role in the transfer of substrate or product between the active site and the solvent. Alternatively, the B site may bind allosteric effectors. Fumarate accumulates in the cell when FH is inactivated. Fumarate inhibits the dioxygenases that hydroxylate the transcription factor HIF and leads to its degradation by VHL. Since HIF turns on oncogenic pathways, FH has apparent tumor suppressor activity. Defects in FH are the cause of hereditary leiomyomatosis and renal cell cancer (HLRCC), a highly metastatic form of RCC. Defects in FH are the cause of fumarase deficiency (FD) also known as fumaricaciduria. FD is characterized by progressive encephalopathy, developmental delay, hypotonia, cerebral atrophy and lactic and pyruvic acidemia. Cells derived from a patient with HLRCC exhibit compromised oxidative phosphorylation, dependence on anaerobic glycolysis, rapid glycolytic flux, and overexpression of lactate dehydrogenase A (LDHA) and GLUT1. Two human isoforms are produced by alternative initiation. The longer isoform is mitochondrial, while the shorter form, missing residues 1-43, is cytoplasmic.

Protein type: Lyase; Tumor suppressor; Carbohydrate Metabolism - citrate (TCA) cycle; EC 4.2.1.2; Mitochondrial

Chromosomal Location of Human Ortholog: 1q42.1

Cellular Component: tricarboxylic acid cycle enzyme complex; mitochondrion; mitochondrial matrix; cytoplasm

Molecular Function: fumarate hydratase activity

Biological Process: cellular metabolic process; fumarate metabolic process; tricarboxylic acid cycle; homeostasis of number of cells within a tissue

Disease: Fumarase Deficiency