Collaborator Elabscience
Recombinant ProteinsISO 9001:2015ISO 14001:2015ISO 45001:2018Collaborator Tested
ABM-16465

Recombinant Human HtrA2/Omi Protein (His Tag)

Protease activity demonstrated by HtrA2 cleavage of bovine β-casein (SigmaCatalog # 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 TrispH 8.0which results in > 95% cleavage of β-caseinas revealed by SDS-PAGE.E.coliPlease contact us for more information.

Recombinant Human HtrA2/Omi Protein (His Tag) supplied by Elabscience with collaborator-provided technical specifications. Read more ›

> 87 % as determined by reducing SDS-PAGE.
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> 87 % as determined by reducing SDS-PAGE.["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. ,36.5 kDa"]

Product Description

HtrA2/Omi is the stated recombinant protein target for this Elabscience product. The listing uses collaborator-supplied specifications to support research-use-only protein selection through ABMIUM.

Protein profile: reactive species/source: Human; expression system: E.coli; physical form: Lyophilized from sterile 50mM Tris, 0.3M NaCl, 1mM DTT, 20% Glycerol, pH 7.8<br/>Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.<br/>Please refer to the specific buffer information in the printed manual.; tag: Human ,HtrA2/Omi ,Recombinant Proteins; predicted molecular weight: 36.5 kDa.

Quality and formulation: purity: > 87 % as determined by reducing SDS-PAGE..

Functional evidence: 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.. In the ABMIUM matrix, collaborator-supplied functional evidence is marked C; unsupported application columns remain N.

Sequence coverage: 36.5 kDa.

Database references: UniProt: O43464-1 | NCBI Gene: 27429 | Gene symbol: HtrA2/Omi.

Research Use Only.

Key Facts

Product typeRecombinant Proteins Target: HtrA2/Omi
Collaborator Elabscience
Partner model PKSH031504_100ug
Target HtrA2/Omi
Research areasNeuroscience, Cell Biology, Cancer, Metabolism
Reactivity Human
Purity >87% by SDS-PAGE
Shelf life 12 months
AvailabilityIn stock - ships within 2 business days
Lead time2-3 business days
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Validation Matrix

1 category
ABMIUM Validated™ ABMIUM Verified™ Expected Performance Not suitable
CategoryBioactivityBindingCell-BasedIn VivoELISA Capture
Human

Specifications

Target
HtrA2/Omi
Also known as
HTRA2, High temperature requirement protein A2, HtrA2, OMI, Omi stress-regulated endoprotease, PRSS25, Serine protease 25, Serine protease HTRA2, Serine proteinase OMI, mitochondrial
Purity
>87% by SDS-PAGE
Form / buffer
Lyophilized

Storage & Stability

Shipped at
This product is provided as lyophilized powder which is shipped with ice packs.
Short-term storage
Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Aliquoting advice
Reconstitute entire vial immediately. Aliquot working stock; avoid repeated freeze-thaw.
Shelf life
12 months

Compliance & Certifications

ABMIUM
ABMIUM Verified

Collaborator meets ABMIUM quality standards and overall product performance standards have been met.

ISO
ISO 9001:2015

Quality management certification.

ISO
ISO 14001:2015

Environmental management certification.

ISO
ISO 45001:2018

Occupational health and safety management certification.

RUO
Research Use Only

For research applications. Not for diagnostic use.

REACH
REACH

REACH compliant.

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