Analytical Data
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Gene name
HTRA4
- Application
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Alternative Names
HtrA Serine Peptidase 4
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P83105
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Expression Region
Gly202~Leu362
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Molecular Weight
21kDa
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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
HTRA4, a member of the high-temperature requirement A (HTRA) family of serine proteases, has gained significant attention in recent years due to its critical roles in various physiological processes and diseases. Originally identified in human tissues, HTRA4 is primarily expressed in the placenta and has been implicated in placental development and function. Research indicates that HTRA4 plays a crucial role in the modulation of cell migration, apoptosis, and extracellular matrix remodeling, making it essential for proper embryonic development. Moreover, studies have shown that altered expression levels of HTRA4 are associated with several pathological conditions, including cancer, cardiovascular diseases, and neurodegenerative disorders. Its proteolytic activity and regulatory functions suggest that HTRA4 may contribute to tumor progression by influencing the tumor microenvironment and mediating stress responses. Consequently, understanding the molecular mechanisms underlying HTRA4's activity is critical for exploring its potential as a therapeutic target. Research efforts are currently focused on characterizing the biochemical properties of HTRA4, including its substrate specificity and regulation, which may lead to insights into its roles in health and disease. Additionally, the development of recombinant HTRA4 proteins could facilitate studies on its functions and interactions, paving the way for novel therapeutic strategies that harness its proteolytic capabilities. Overall, the study of HTRA4 represents a burgeoning field that merges basic biology with clinical relevance, holding promise for advancements in disease treatment and understanding of developmental biology.
