Name :
Recombinant Human HtrA2/Omi Protein (His Tag)
Biological Activity :
Background :
Serine protease HTRA2, also known as high-temperature requirement protein A2, Omi stress-regulated endoprotease, Serine protease 25, Serine proteinase OMI and HTRA2, is a single-pass membrane protein that belongs to the peptidase S1B family. HTRA2 contains one PDZ (DHR) domain. HTRA2 is a serine protease that shows proteolytic activity against a non-specific substrate beta-casein. It promotes or induces cell death either by direct binding to and inhibition of BIRC proteins (also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity or by a BIRC inhibition-independent, caspase-independent, and serine protease activity-dependent mechanism. HTRA2 cleaves THAP5 and promotes its degradation during apoptosis. Isoform 2 of HTRA2 seems to be proteolytically inactive. Defects in HTRA2 are the cause of Parkinson disease type 13 (PARK13) which is a complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity, and postural instability, as well as by a clinically significant response to treatment with levodopa.
Biological Activity :
Protease activity demonstrated by HtrA2 cleavage of bovine β-casein (Sigma, Catalog # C-6905). Incubation of β-casein at 0.2 mg/mL with Recombinant Human HTRA-2 at 0.02 mg/mL (ratio of 10:1) for 60 minutes at 45℃ in 50 mM Tris, pH 8.0, which results in >95% cleavage of β-casein, as revealed by SDS-PAGE.
Expression Host :
Human
Source :
E. coli
Tag :
Protein Accession No. :
O43464-1
NCBI Gene ID :
Synonyms :
Synonyms :
HtrA serine peptidase 2
Amino Acid Sequence :
Molecular Weight :
The recombinant human HTRA2 consisting of 336 amino acids and has a calculated molecular mass of 36.5 kDa as estimated in SDS-PAGE under reducing conditions.
Purity :
> 87 % as determined by SDS-PAGE
State of Matter :
Product Concentration :
Storage and Stability :
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Endotoxin Level :
Please contact us for more information.
Protein Construction :
A DNA sequence encoding the mature form of human HTRA2 (O43464-1) (Ala 134-Glu 458) was expressed, with a polyhistide tag at the C-terminus.
Buffer Solution :
Supplied as sterile 50mM Tris, 0.3M NaCl, 1mM DTT, 20% Glycerol, pH 7.8Please contact us for any concerns or special requirements.Please refer to the specific buffer information in the hardcopy of datasheet.
Shipping :
Liquid. It is shipped out with blue ice.
Redissolution :
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
Synonyms :
OMI Protein, Human; PARK13 Protein, Human; PRSS25 Protein, Human HtrA2/Omi 背景信息 Serine protease HTRA2, also known as high-temperature requirement protein A2, Omi stress-regulated endoprotease, Serine protease 25, Serine proteinase OMI and HTRA2, is a single-pass membrane protein that belongs to the peptidase S1B family. HTRA2 contains one PDZ (DHR) domain. HTRA2 is a serine protease that shows proteolytic activity against a non-specific substrate beta-casein. It promotes or induces cell death either by direct binding to and inhibition of BIRC proteins (also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity or by a BIRC inhibition-independent, caspase-independent, and serine protease activity-dependent mechanism. HTRA2 cleaves THAP5 and promotes its degradation during apoptosis. Isoform 2 of HTRA2 seems to be proteolytically inactive. Defects in HTRA2 are the cause of Parkinson disease type 13 (PARK13) which is a complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity, and postural instability, as well as by a clinically significant response to treatment with levodopa.
References & Citations :
Faccio L., et al., 2000, J. Biol. Chem. 275:2581-2588. Gray C.W., et al., 2000, Eur. J. Biochem. 267:5699-5710. Suzuki Y., et al., 2001, Mol. Cell 8:613-621. Strauss K.M., et al., 2005, Hum. Mol. Genet. 14:2099-2111.
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