Analytical Data
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Gene name
HTRA2
- Application
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Alternative Names
arginine/serine-rich 10; Arginine/serine-rich splicing factor 10; hTRA2-beta; SFRS10; Splicing factor; Splicing factor arginine/serine rich 10; SRFS10; TRA-2 beta; TRA2-beta; Tra2b; TRA2B_HUMAN; TRAN2B
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P62995
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Expression Region
111-201aa
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AA Sequence
RANPDPNCCLGVFGLSLYTTERDLREVFSKYGPIADVSIVYDQQSRRSRGFAFVYFENVDDAKEAKERANGMELDGRRIRVDFSITKRPHT
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Molecular Weight
26.5 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
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.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
HTRA2, a member of the high-temperature requirement A (HTRA) serine protease family, has garnered significant attention in biomedical research due to its dual roles in protein quality control and apoptosis regulation. Discovered as a mitochondrial protein, HTRA2 is involved in the proteolytic degradation of misfolded proteins, thereby maintaining cellular homeostasis and mitochondrial function. Alterations in its expression and activity have been linked to various human diseases, including neurodegenerative disorders such as Parkinson's disease and certain cancers, where its protective functions can be compromised. Research has shown that HTRA2 is released from mitochondria during stress, where it can exert pro-apoptotic effects by inhibiting anti-apoptotic proteins. This dual functionality makes HTRA2 a critical target for understanding the mechanisms of diseases characterized by mitochondrial dysfunction and apoptosis dysregulation. Recombinant HTRA2 protein studies have enabled the exploration of its structural properties and enzymatic functions, thereby providing insights into its potential as a therapeutic target. Investigations utilizing recombinant techniques aim to elucidate the molecular pathways mediated by HTRA2 in cellular homeostasis and pathology, which could lead to novel strategies for disease intervention.
