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SDHA recombinant protein :: Succinate dehydrogenase [ubiquinone] flavoprotein subunit Recombinant Protein

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Catalog # MBS717214 (PROMOTIONAL PRICING: 10% OFF web price. Discount is not applicable for bulk pricing such as 5x96T or 10x96T. Discount will be applied after order has been placed)
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SDS-PAGE
Product Name

Succinate dehydrogenase [ubiquinone] flavoprotein subunit (SDHA), Recombinant Protein

Popular Item
Full Product Name

Recombinant Human Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial

Product Synonym Names
Flavoprotein subunit of complex II; Fp
Product Synonym Gene Name
SDH2; SDHF[Similar Products]
Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
MBS717214 COA
Sequence Positions
44-293aa; Partial
Sequence
SAKVSDSISA QYPVVDHEFD AVVVGAGGAG LRAAFGLSEA GFNTACVTKL FPTRSHTVAA QGGINAALGN MEEDNWRWHF YDTVKGSDWL GDQDAIHYMT EQAPAAVVEL ENYGMPFSRT EDGKIYQRAF GGQSLKFGKG GQAHRCCCVA DRTGHSLLHT LYGRSLRYDT SYFVEYFALD LLMENGECRG VIALCIEDGS IHRIRAKNTV VATGGYGRTY FSCTSAHTST GDGTAMITRA GLPCQDLEFV
OMIM
252011
3D Structure
ModBase 3D Structure for P31040
Host
E Coli
Purity/Purification
Greater than 90% as determined by SDS-PAGE. (lot specific)
Form/Format
Liquid containing glycerol
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
Production Note
Special Offer: The E. coli host-expressed protein is manufactured from a stock plasmid containing the protein gene. E. coli host-expressed protein is stocked in different unit sizes ranging from as small as 10 ug to as large as 1 mg. Bulk inventory is also available. The E. coli host-expressed protein has been ordered over and over again by researchers and has stood the test of time as both a robust protein and important target for the research community. It is part of our new program to make our most popular protein targets and corresponding hosts available in expanded unit sizes and with a quick processing time. Select E. coli host-expressed protein for the fastest delivery among all hosts. Please contact us or email to support@mybiosource.com for more details.
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
ISO Certification
Manufactured in an ISO 9001:2008 Certified Laboratory.
Other Notes
Small volumes of SDHA recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
Related Product Information for
SDHA recombinant protein
Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). Can act as a tumor suppressor.
Product Categories/Family for SDHA recombinant protein

SDHA recombinant protein SDS-PAGE image
(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)
NCBI/Uniprot data below describe general gene information for SDHA. It may not necessarily be applicable to this product.
NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
54.4kD
NCBI Official Full Name
succinate dehydrogenase
NCBI Official Synonym Full Names
succinate dehydrogenase complex flavoprotein subunit A
NCBI Official Symbol
NCBI Official Synonym Symbols
FP; PGL5; SDH1; SDH2; SDHF; CMD1GG
  [Similar Products]
NCBI Protein Information
succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
UniProt Protein Name
Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
UniProt Synonym Protein Names
Flavoprotein subunit of complex II; Fp
Protein Family
UniProt Gene Name
UniProt Synonym Gene Names
SDH2; SDHF; Fp  [Similar Products]
UniProt Entry Name
SDHA_HUMAN
NCBI Summary for SDHA
This gene encodes a major catalytic subunit of succinate-ubiquinone oxidoreductase, a complex of the mitochondrial respiratory chain. The complex is composed of four nuclear-encoded subunits and is localized in the mitochondrial inner membrane. Mutations in this gene have been associated with a form of mitochondrial respiratory chain deficiency known as Leigh Syndrome. A pseudogene has been identified on chromosome 3q29. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jun 2014]
UniProt Comments for SDHA
SDHA: is the catalytic subunit of succinate dehydrogenase (SDH) complex II of the mitochondrial electron transport chain. Complex II contains four subunits: the flavoprotein catalytic subunit SDHA, iron-sulfur protein SDHB, and a cytochrome b560 composed of SDHC and SDHD. Interaction with SDH5 is required for FAD attachment. Responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). Defects in SDHA cause defective mitochondrial oxidative phosphorylation, giving rise to heterogeneous clinical symptoms ranging from isolated organ dysfunction to multisystem disorder. Acetylation of SDHA may control entry of the substrate into the active site, thus regulating its enzymatic activity. Acetylated SDHA may be a SIRT3 substrate SIRT3 is a mitochondrial NAD(+)-dependent deacetylase. Increased succinate levels as a consequence of SDH deficiency inhibit hypoxia inducible factor-1alpha (HIF-1alpha) prolyl hydroxylases leading to sustained HIF-1alpha expression in tumours. Defects in SDHA cause of Leigh syndrome, a severe disorder characterized by bilaterally symmetrical necrotic lesions in subcortical brain regions.

Protein type: Oxidoreductase; Mitochondrial; Tumor suppressor; EC 1.3.5.1; Carbohydrate Metabolism - citrate (TCA) cycle; Energy Metabolism - oxidative phosphorylation

Chromosomal Location of Human Ortholog: 5p15

Cellular Component: mitochondrial inner membrane; mitochondrial respiratory chain complex II; mitochondrion; myelin sheath

Molecular Function: FAD binding; protein binding; succinate dehydrogenase (ubiquinone) activity; succinate dehydrogenase activity

Biological Process: cellular metabolic process; nervous system development; succinate metabolic process; tricarboxylic acid cycle

Disease: Cardiomyopathy, Dilated, 1gg; Leigh Syndrome; Mitochondrial Complex Ii Deficiency; Paragangliomas 5
Product References and Citations for SDHA recombinant protein
Human complex II (succinate-ubiquinone oxidoreductase) cDNA cloning of the flavoprotein (Fp) subunit of liver mitochondria.Hirawake H., Wang H., Kuramochi T., Kojima S., Kita K.J. Biochem. 116:221-227(1994) The cDNA sequence of the flavoprotein subunit of human heart succinate dehydrogenase.Morris A.A.M., Farnsworth L., Ackrell B.A.C., Turnbull D.M., Birch-MacHin M.A.Biochim. Biophys. Acta 1185:125-128(1994) Compound heterozygous mutations in the flavoprotein gene of the respiratory chain complex II in a patient with Leigh syndrome.Parfait B., Chretien D., Roetig A., Marsac C., Munnich A., Rustin P.Hum. Genet. 106:236-243(2000) Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) Homo sapiens protein coding cDNA.Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. The DNA sequence and comparative analysis of human chromosome 5.Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.Nature 431:268-274(2004)

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