SRP6120
Fumarase human
recombinant, expressed in E. coli, ≥95% (SDS-PAGE)
Synonym(s):
FH, Fumarate hydratase, LRCC, MCL, MCUL1
Sign In to View Organizational & Contract Pricing.
Select a Size
About This Item
Form:
liquid
Assay:
≥95% (SDS-PAGE)
Biological source:
human
Recombinant:
expressed in E. coli
Mol wt:
50.2 kDa (467 aa, 44-510 aa)
biological source
human
recombinant
expressed in E. coli
assay
≥95% (SDS-PAGE)
form
liquid
potency
>1.0 units/mg
mol wt
50.2 kDa (467 aa, 44-510 aa)
packaging
pkg of 100 μg
impurities
<1.0 EU/μg
NCBI accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... FH(2271)
General description
Fumarase (Fumarate hydratase) 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.
Physical form
1 mg/mL solution in 20 mM Tris-HCl buffer (pH 8.0).
Preparation Note
Centrifuge the vial prior to opening.
Other Notes
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
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
常规特殊物品
This item has
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Izanara C Pritsch et al.
BMC molecular and cell biology, 21(1), 90-90 (2020-12-09)
The zoonotic worm parasite Fasciola hepatica secretes an abundance of cathepsin L peptidases that are associated with virulence, invasiveness, feeding and migration. The peptidases are produced as inactive zymogens that activate at low pH by autocatalytic removal of their N-terminal
Carolina De Marco Verissimo et al.
PLoS neglected tropical diseases, 14(8), e0008510-e0008510 (2020-08-08)
Serine protease inhibitors (serpins) regulate proteolytic events within diverse biological processes, including digestion, coagulation, inflammation and immune responses. The presence of serpins in Fasciola hepatica excretory-secretory products indicates that the parasite exploits these to regulate proteases encountered during its development
I L Pacheco et al.
Veterinary parasitology, 238, 61-65 (2017-04-08)
The expression of IFNγ and IL4 was quantified using q-PCR in the liver and hepatic lymph nodes (HLN) of sheep during early stages of infection with Fasciola hepatica (1, 3, 9 and 18days post-infection, dpi). A group of animals (Group
Isabel L Pacheco et al.
Veterinary research, 49(1), 56-56 (2018-07-05)
The expression of T regulatory cells (Foxp3), regulatory (interleukin [IL]-10 and transforming growth factor beta [TGF-β]) and proinflammatory (tumor necrosis factor alpha [TNF-α] and interleukin [IL]-1β) cytokines was quantified using real time polymerase chain reaction (qRT-PCR) in the liver of
Mark W Robinson et al.
PLoS pathogens, 7(5), e1002042-e1002042 (2011-05-19)
Over the last decade a significant number of studies have highlighted the central role of host antimicrobial (or defence) peptides in modulating the response of innate immune cells to pathogen-associated ligands. In humans, the most widely studied antimicrobial peptide is
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service