protein

Recombinant Human Fumarate Hydratase

MBS143875

0.01 mg

140 USD

Recombinant Protein

Recombinant Human Fumarate Hydratase

Fumarate Hydratase

Fumarase Human; Fumarate Hydratase Human Recombinant; MCL; LRCC; HLRCC; MCUL1; FH; Fumarate hydratase; Fumarase; Fumarase

fumarate hydratase, mitochondrial; Fumarate hydratase, mitochondrial; fumarate hydratase, mitochondrial; fumarase; fumarate hydratase

FH; FH; MCL; LRCC; HLRCC; MCUL1; Fumarase

FUMH_HUMAN

E Coli

510

MASQNSFRIE YDTFGELKVP NDKYYGAQTV RSTMNFKIGG VTERMPTPVI KAFGILKRAA AEVNQDYGLD PKIANAIMKA ADEVAEGKLN DHFPLVVWQT GSGTQTNMNV NEVISNRAIE MLGGELGSKI PVHPNDHVNK SQSSNDTFPT AMHIAAAIEV HEVLLPGLQK LHDALDAKSK EFAQIIKIGR THTQDAVPLT LGQEFSGYVQ QVKYAMTRIK AAMPRIYELA AGGTAVGTGL NTRIGFAEKV AAKVAALTGL PFVTAPNKFE ALAAHDALVE LSGAMNTTAC SLMKIANDIR FLGSGPRSGL GELILPENEP GSSIMPGKVN PTQCEAMTMV AAQVMGNHVA VTVGGSNGHF ELNVFKPMMI KNVLHSARLL GDASVSFTEN CVVGIQANTE RINKLMNESL MLVTALNPHI GYDKAAKIAK TAHKNGSTLK ETAIELGYLT AEQFDEWVKP KDMLGPK.

Greater than 95.0% as determined by SDS-PAGE.

The Fumarase protein solution (1mg/ml) contains 20mM Tris-HCl, pH-8. Sterile filtered colorless solution.

Store at 4 degree C if entire vial will be used within 2-4 weeks. Store, frozen at -20 degree C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

Biological Activity: Specific activity is > 1.0 unit/mg, and is defined as the amount of enzyme that cleaves 1umole of L-Malate to Fumarate per minute at pH 7.5 at 25 C.

ENZYMES; Enzymes; Hydratase

Description: Fumarase Human Recombinant produced in E Coli is a single, non-glycosylated polypeptide chain containing 467 amino acids (44-510) and having a molecular mass of 50.2 kDa. Fumarate Hydratase is purified by proprietary chromatographic techniques. Introduction: Fumarase is an enzymatic factor of Krebs cycle, which catalyzes the formation of L-malate from fumarate. Fumarase 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 aimed to the mitochondrion, where the removal of the extension results in the same form as in the cytoplasm. Fumarase is similar to a number of thermostable Class-2 fumarases and functions as a homotetramer. Mutations in the Fumarase gene causes fumarase deficiency and leads to progressive encephalopathy, cerebral atrophy and developmental delay. Fumarase enzyme is also thought to act as a tumor suppressor. Leydig cell tumors are caused by Fumarase mutations and represents one of the first reports of germline mutations in any type of adult testicular tumor.

19743875

NP_000134.2

NM_000143.3

P07954

50,213 Da

Carbon Metabolism Pathway 814926!!Carbon Metabolism Pathway 817567!!Citrate Cycle (TCA Cycle) Pathway 82927!!Citrate Cycle (TCA Cycle) Pathway 288!!Citrate Cycle (TCA Cycle, Krebs Cycle) Pathway 855811!!Citrate Cycle (TCA Cycle, Krebs Cycle) Pathway 468202!!Citrate Cycle, Second Carbon Oxidation, 2-oxoglutarate = Oxaloacetate Pathway 413348!!Citrate Cycle, Second Carbon Oxidation, 2-oxoglutarate = Oxaloacetate Pathway 468204!!Citric Acid Cycle (TCA Cycle) Pathway 105919!!Metabolic Pathways 132956

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]

0.01 mg

140 USD