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Merck

H7290

Sigma-Aldrich

Anti-HtrA2 antibody produced in rabbit

enhanced validation

~1.5 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonim(y):

Anti-High Temperature Requirement protein A2, Anti-HtrA serine peptidase 2, Anti-Omi, Anti-PARK13, Anti-PRSS25, Anti-Protease, Serine, 25

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About This Item

Kod UNSPSC:
12352203

pochodzenie biologiczne

rabbit

białko sprzężone

unconjugated

forma przeciwciała

affinity isolated antibody

rodzaj przeciwciała

primary antibodies

klon

polyclonal

Postać

buffered aqueous solution

masa cząsteczkowa

antigen ~36 kDa (also 50 kDa band corresponding to HtrA2 precursor)

reaktywność gatunkowa

human, rat

opakowanie

antibody small pack of 25 μL

rozszerzona walidacja

recombinant expression
Learn more about Antibody Enhanced Validation

stężenie

~1.5 mg/mL

metody

western blot: 2-4 μg/mL using rat liver microsomal fraction and HEK-293 cells expressing human HTRA2

numer dostępu UniProt

Warunki transportu

dry ice

temp. przechowywania

−20°C

docelowa modyfikacja potranslacyjna

unmodified

informacje o genach

human ... HTRA2(27429)
rat ... Htra2(297376)

Opis ogólny

High-temperature requirement protein A2 (HtrA2) belongs to the HtrA family of serine proteases. This protein is located in the mitochondria and is made up of N-terminal mitochondrial localization sequence (MLS), an inhibitor of apoptosis protein (IAP) binding domain (IBM), a single C-terminal PDZ domain that mediates protein-protein interaction, and a conserved catalytic domain of serine proteases. The HTRA2 gene is located on the human chromosome at 2p13.1.

Specyficzność

Anti-HtrA2 specifically recognizes human and rat HtrA2.

Zastosowanie

Anti-HtrA2 antibody produced in rabbit may be used in immunoblotting.

Działania biochem./fizjol.

High-temperature requirement A2 (HtrA2) exhibits endoproteolytic activity by cleaving misfolded proteins and other cellular proteins. This protein possesses protease activity, which is required for mitochondrial homeostasis. HtrA2 is released from the mitochondria as a mature form in response to apoptotic stimuli and is involved in regulating apoptosis through multiple pathways, including caspase-dependent and caspase-independent cell death. Mature HtrA2 promotes cytochrome c-dependent caspase activation by neutralizing inhibitors of apoptosis proteins (IAPs). Mutations that inactivate HtrA2 are associated with neurodegenerative diseases such as Parkinson′s disease and Alzheimer′s disease.

Postać fizyczna

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Przechowywanie i stabilność

For continuous use, store at 2–8 °C for up to one month. For extended storage, freeze in working aliquots at –20 °C. Repeated freezing and thawing, or storage in “frost-free” freezers, is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilutions should be discarded if not used within 12 hours.

Oświadczenie o zrzeczeniu się odpowiedzialności

Unless otherwise stated in our catalog, our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Kod klasy składowania

12 - Non Combustible Liquids

Temperatura zapłonu (°C)

Not applicable

Środki ochrony indywidualnej

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Certyfikaty analizy (CoA)

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Masz już ten produkt?

Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

Generation of a human iPSC line CIBi007-A from a patient with young-onset Parkinson?s disease carrying variants in PRKN and HTRA2
Yan Y, et al.
Stem Cell Research, 47, 101905-101905 (2020)
Autocatalytic processing of HtrA2/Omi is essential for induction of caspase-dependent cell death through antagonizing XIAP
Seong Y M, et al.
The Journal of Biological Chemistry, 279(36), 37588-37596 (2004)

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