protein

HtrA2/Omi 134-458 Human, Recombinant, His- tag, E Coli

MBS203109

0.1 mg

255 USD

Recombinant Protein

HtrA2/Omi 134-458 Human, Recombinant, His- tag, E Coli

HtrA2/Omi

HTRA2; OMI; PRSS25; HtrA2/Omi; EC 3.4.21.108; High temperature requirement protein A2; HtrA2; Omi stress-regulated endoprotease; Serine proteinase OMI; Serine protease 25; Serine protease HTRA2; mitochondrial; High temperature requirement protein A2

serine protease HTRA2, mitochondrial isoform 1 preproprotein; Serine protease HTRA2, mitochondrial; serine protease HTRA2, mitochondrial; HtrA-like serine protease; Omi stress-regulated endoprotease; high temperature requirement protein A2; protease, serine, 25; serine protease 25; serine proteinase OMI; HtrA serine peptidase 2; High temperature requirement protein A2; HtrA2; Omi stress-regulated endoprotease; Serine protease 25; Serine proteinase OMI

HtrA2/Omi

HTRA2; HTRA2; OMI; PARK13; PRSS25; OMI; PRSS25; HtrA2

HTRA2_HUMAN

458

MAVPSPPPAS PPSQYNFIAD VVEKTAPAVV YIEILDRHPF LGREVPISNG SGFVVAADGL IVTNAHVVAD RRRVRVRLLS GDTYEAVVTA VDPVADIATL RIQTKEPLPT LPLGRSADVR QGEFVVAMGS PFALQNTITS GIVSSAQRPA RDLGLPQTNV EYIQTDAAID FGNAGGPLVN LDGEVIGVNT MKVTAGISFA IPSDRLREFL HRGEKKNSSS GISGSQRRYI GVMMLTLSPS ILAELQLREP SFPDVQHGVL IHKVILGSPA HRAGLRPGDV ILAIGEQMVQ NAEDVYEAVR TQSQLAVQIR RGRETLTLYV TPEVTEGSHH HHHH

> 95% by SDS - PAGE

Liquid. In 20 mM Tris-HCl buffer (pH 8.0), 50 mM NaCl, 1 mM DTT, 20% Glycerol

0.5 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. Tag: His-tag

Expression System: E Coli

Enzymes & Proteases

HtrA2/Omi is a mammalian serine protease at high temperatures and has a chaperone activity at low temperature. The full-length HtrA2 is synthesized as a precursor protein and then targeted to the mitochondria where it is matured by the removal of N-terminal 133 residues. Mature HtrA2 consists of a putative transmembrane domain; an inhibitor of apoptosis protein (IAP)-binding motif; a single C-terminal PDZ domain that mediates protein-protein interactions. Recently, HtrA2 has known to contribute both to caspase-dependent and caspase-independent cell death. Mature form of HtrA2/Omi(residues 134-458) was overexpressed in E.coli, and purified by conventional column chromatography techniques.

Savopoulos JW., et al., (2000) Protein Expr. Purif. 19, 227-34. Gray CW, et al., (2000) Eur. J. Biochem. 267, 5699-710 . Martins LM, et al., (2002) J. Biol. Chem. 277, 439-44. Van Loo G, et al., (2002) Cell Death Differ. 9, 20-60.

7019477

NP_037379

NM_013247.4

36kDa (334aa), confirmed by MALDI-TOF.

Apoptosis Modulation And Signaling Pathway (198822); Parkinson's Disease Pathway (83098); Parkinsons Disease Pathway (705377)

This gene encodes a serine protease. The protein has been localized in the endoplasmic reticulum and interacts with an alternatively spliced form of mitogen-activated protein kinase 14. The protein has also been localized to the mitochondria with release to the cytosol following apoptotic stimulus. The protein is thought to induce apoptosis by binding the apoptosis inhibitory protein baculoviral IAP repeat-containing 4. Nuclear localization of this protein has also been observed. Alternate splicing of this gene results in two transcript variants encoding different isoforms. Additional transcript variants have been described, but their full-length sequences have not been determined. [provided by RefSeq, Jul 2008]

HTRA2: a serine proteinase that normally resides in mitochondrial membranes. It exists in two populations in mitochondria: as an unprocessed form probably attached to the inner mitochondrial membrane through a N-terminal transmembrane domain, and as a processed form containing a reaper motif at its N-terminus. Following apoptotic stimuli it is autoproteolytically activated and released into the cytosol, where it promotes programmed cell death in caspase-dependent and -independent manners. The amino-terminal reaper motif binds to the IAP (inhibitor of apoptosis) proteins cIAP1, cIAP2, and and XIAP, disrupting IAP-caspase complexes in a manner similar to Smac/DIABLO. Phosphorylation by the protein kinase Akt attenuates its serine protease and pro-apoptotic activities. The PDZ domain mediates interaction with Mxi2, an alternatively spliced form of the p38 stress-activated kinase. In contrast to its pro-apoptotic effects, targeted deletion in mice indicates that it is involved in protection against cell stress in striatial neurons. Defects in HTRA2 are the cause of Parkinson disease 13 (PARK13). Four alternatively spliced human isoforms have been described. Protein type: Mitochondrial; Membrane protein, integral; Protease; EC 3.4.21.108. Chromosomal Location of Human Ortholog: 2p12. Cellular Component: endoplasmic reticulum membrane; internal side of plasma membrane; cytoskeleton; membrane; mitochondrion; endoplasmic reticulum; mitochondrial membrane; mitochondrial intermembrane space; cytosol; nucleus; chromatin. Molecular Function: peptidase activity; protein binding; serine-type peptidase activity; serine-type endopeptidase activity; unfolded protein binding. Biological Process: mitochondrion organization and biogenesis; positive regulation of apoptosis; regulation of multicellular organism growth; positive regulation of caspase activity; response to herbicide; proteolysis; adult walking behavior; negative regulation of cell cycle; protein autoprocessing; DNA damage response, signal transduction resulting in induction of apoptosis; pentacyclic triterpenoid metabolic process; cellular protein catabolic process; forebrain development; neuron development; ceramide metabolic process. Disease: Parkinson Disease 13, Autosomal Dominant, Susceptibility To

0.1 mg

255 USD

0.5 mg

535