Recombinant Human Fumarase/FH Protein (His Tag)(Active) | PKSH030901

Recombinant Human Fumarase/FH Protein (His Tag)(Active) | PKSH030901 | Gentaur US, UK & Europe Disrtribition

Synonyms: Fumarate Hydratase Mitochondrial; Fumarase; FH;FMRD;HLRCC;LRCC;MCL;MCUL1

Active Protein: Active protein

Activity: A DNA sequence encoding the mature form of human FH (P07954-1) (Ala 45-Lys 510) was fused with a polyhistidine tag at the C-terminus and an initial Met at the N-terminus.

Protein Construction: A DNA sequence encoding the mature form of human FH (P07954-1) (Ala 45-Lys 510) was fused with a polyhistidine tag at the C-terminus and an initial Met at the N-terminus.

Fusion Tag: C-His

Species: Human

Expressed Host: E.coli

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 85 % as determined by reducing SDS-PAGE.

Endotoxin: Please contact us for more information.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 52 kDa

Formulation: Lyophilized from sterile 10mM Tris, 5mM EDTA, 1mM DTT, pH 7.5

Reconstitution: Please refer to the printed manual for detailed information.

Background: Fumarate Hydratase (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. Fumarate Hydratase 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. Individuals with hemizygous germline fumarate hydratase (FH) mutations are predisposed to renal cancer. These tumors predominantly exhibit functional inactivation of the remaining wild-type allele, implicating FH inactivation as a tumor-promoting event.

Research Area: N/A