Recombinant Human HtrA2 / Omi Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-2468

Recombinant Human HtrA2 / Omi Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-2468
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Product Overview

Tag His
Host Species Human
Accession O43464
Synonym OMI, PARK13, PRSS25
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 which belongs to thepeptidase S1B family. HTRA2 contains onePDZ (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 2of 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.
Description A DNA sequence encoding the mature form of human HTRA2 (O43464-1) (Ala 134-Glu 458) was expressed, with a His tag at the C-terminus.
Source E.coli
Predicted N Terminal Met
AA Sequence Ala 134-Glu 458
Molecular Weight The recombinant human HTRA2 consisting of 336 a.a. 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
Endotoxin Please contact us for more information.
Bioactivity Protease activity demonstrated by HtrA2 cleavage of bovine beta-casein (Sigma, Catalog # C-6905). Incubation of beta-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°C in 50 mM Tris, pH 8.0, which results in >95% cleavage of beta-casein, as revealed by SDS-PAGE.
Formulation Lyophilized from sterile 50mM Tris, 0.3M NaCl, 1mM DTT, 20% Glycerol, pH 7.8.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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