protein

Fumarase, 44-510aa, Human, Recombinant, E Coli

MBS203208

0.1 mg

255 USD

Recombinant Protein

Fumarase, 44-510aa, Human, Recombinant, E Coli

Fumarase

FH; HLRCC; LRCC; MCL; MCuL1; Fumarate hydratase Fumarase; Fumarate hydratase mitochondrial; MCuL 1; Multiple hereditary cutaneous leiomyomata.

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

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

FUMH_HUMAN

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

> 95% by SDS - PAGE

Liquid. In 20 mM Tris-HCl buffer (pH 8.0)

1 mg/ml (determined by Bradford assay)

Can be stored at 4 degree C short term (1-2 weeks). For long term storage, aliquot and store at -20 degree C or -70 degree C. Avoid repeated freezing and thawing cycles.

SDS-PAGE

Antigen Species: Human

Expression System: E Coli. Bioactivity: 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. Endotoxin: < 1.0 Eu per 1 microgram of protein (determined by LAL method). Assay: Prepare a 1.45 m assay buffer (Assay buffer: 100 mM potassium phosphate, 50 mM L-malic acid). Add 50 ul of recombinant Fumarase protein with various concentrations (0.5 ug, 1ug, 2ug) in assay buffer. Record the increase in A260 nm for 10 minutes. - L-Malate (Sigma-Aldrich. Cat. No, M-1000).

Cell Cycle

Fumarase (Fumarate hytdratase) is an enzyme that catalyzes the reversible hydration/dehydration of fumarate to S-malate and is involved in the tricarboxylic acid (TCA), or Krebs cycle. This enzyme exists in both a cytosolic form and an N-terminal extended mitochondrial form. The N-terminal extended form is targeted to the mitochondrion, where the removal of the extension is the same form as in the cytoplasm. Fumarase deficiency can lead to progressive encephalopathy, cerebral atrophy and developmental delay and this enzyme also is thought to act as a tumor suppressor. Recombinant Fumarase was expressed in E.coli and was purified by conventional chromatography techniques.

Lehtonen R., et al. (2003) J. Med. Genet. 40 (3): e19. Toro JR., et al. (2003) Am. J. Hum. Genet. 73(1): 95-106.

19743875

NP_000134

NM_000143.3

50.2kDa (467aa), confirmed by MALDI-TOF.

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]

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: Carbohydrate Metabolism - citrate (TCA) cycle; Lyase; Tumor suppressor; 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; homeostasis of number of cells within a tissue; tricarboxylic acid cycle. Disease: Fumarase Deficiency

0.1 mg

255 USD

0.5 mg

535