Trifunctional enzyme subunit beta Recombinant Protein | HADHB recombinant protein

Recombinant Human Trifunctional enzyme subunit beta, mitochondrial

Cat. Num. AAA717111

• Gene Names: HADHB; ECHB; MTPB; MSTP029; TP-BETA
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Trifunctional enzyme subunit beta; Recombinant Human Trifunctional enzyme subunit beta; mitochondrial; TP-beta 1 domains:3-ketoacyl-CoA thiolase (EC:2.3.1.16); Acetyl-CoA acyltrans ferase; Beta-ketothiolase; HADHB recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 35-283aa; Partial
• Sequence: APAVQTKTKKTLAKPNIRNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRKLMLDLNKAKSMGQRLSLISKFRFNFLAPELPAVSEFSTSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSDVVPFKVPGKDTVTKDNGIRP
• Sequence Length: 474

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Product Categories/Family for HADHB recombinant protein

Metabolism

References

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Genet. 36:40-45(2004) Generation and annotation of the DNA sequences of human chromosomes 2 and 4.Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.Nature 434:724-731(2005) Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.Nat. 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NCBI and Uniprot Product Information

• NCBI GI #: 4504327
• NCBI GeneID: 3032
• NCBI Accession #: NP_000174.1
• NCBI GenBank Nucleotide #: NM_000183.2
• UniProt Accession #: P55084; O14969; Q53TA6; Q96C77; Q9H3F5; Q9T2V8; B2RB16; B4E2W0
• Molecular Weight: 53.8 kDa
• NCBI Official Full Name: trifunctional enzyme subunit beta, mitochondrial isoform 1
• NCBI Official Synonym Full Names: hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional protein), beta subunit
• NCBI Official Symbol: HADHB
• NCBI Official Synonym Symbols: ECHB; MTPB; MSTP029; TP-BETA
• NCBI Protein Information: trifunctional enzyme subunit beta, mitochondrial
• UniProt Protein Name: Trifunctional enzyme subunit beta, mitochondrial
• Protein Family: Trifunctional enzyme
• UniProt Gene Name: HADHB
• UniProt Entry Name: ECHB_HUMAN

NCBI Description

This gene encodes the beta subunit of the mitochondrial trifunctional protein, which catalyzes the last three steps of mitochondrial beta-oxidation of long chain fatty acids. The mitochondrial membrane-bound heterocomplex is composed of four alpha and four beta subunits, with the beta subunit catalyzing the 3-ketoacyl-CoA thiolase activity. The encoded protein can also bind RNA and decreases the stability of some mRNAs. The genes of the alpha and beta subunits of the mitochondrial trifunctional protein are located adjacent to each other in the human genome in a head-to-head orientation. Mutations in this gene result in trifunctional protein deficiency. Alternatively spliced transcript variants encoding different isoforms have been described. [provided by RefSeq, Jul 2013]

Uniprot Description

HADHB: Defects in HADHB are a cause of trifunctional protein deficiency (TFP deficiency). The clinical manifestations are very variable and include hypoglycemia, cardiomyopathy and sudden death. Phenotypes with mainly hepatic and neuromyopathic involvement can also be distinguished. Biochemically, TFP deficiency is defined by the loss of all three enzyme activities of the TFP complex. Belongs to the thiolase family.

Protein type: Lipid Metabolism - fatty acid elongation in mitochondria; Transferase; Amino Acid Metabolism - valine, leucine and isoleucine degradation; EC 2.3.1.16; Lipid Metabolism - fatty acid

Chromosomal Location of Human Ortholog: 2p23

Cellular Component: endoplasmic reticulum; mitochondrial envelope; mitochondrial inner membrane; mitochondrial outer membrane; mitochondrion

Molecular Function: 3-hydroxyacyl-CoA dehydrogenase activity; acetyl-CoA C-acyltransferase activity; enoyl-CoA hydratase activity; long-chain-3-hydroxyacyl-CoA dehydrogenase activity; protein binding

Biological Process: cellular lipid metabolic process; fatty acid beta-oxidation; glycerophospholipid biosynthetic process; phospholipid metabolic process

Disease: Trifunctional Protein Deficiency