Analytical Data
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Gene name
ERH
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简介
ERH proteins are involved in regulating the cell cycle and have been shown to be involved in cell division and proliferation processes. Structurally forming homodimers, it suggests potential functional significance. ERH Protein, Human (N-His) is the recombinant human-derived ERH protein, expressed by E. coli , with N-His labeled tag.
- Application
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Alternative Names
Enhancer of rudimentary homolog; ERH
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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
P84090
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Expression Region
M1-K104
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Protein Length
Full Length
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Molecular Weight
15 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
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Protein Description
Decorin, a small leucine-rich proteoglycan, plays a crucial role in extracellular matrix organization and cellular signaling. It is known to bind collagen and modulate cell behavior, which makes it a significant component in various physiological and pathological processes, including tissue development, wound healing, and tumor progression. PGS2 (Prostaglandin-endoperoxide synthase 2), an enzyme involved in inflammation and the synthesis of prostaglandins, has drawn attention for its role in cancer and other diseases. Recent studies have highlighted the interplay between decorin and PGS2, suggesting that decorin may influence PGS2 expression and activity, thereby affecting inflammatory responses and cancer progression. The recombinant protein forms of Decorin and PGS2 offer a valuable tool for investigating their interactions and biological functions in a controlled environment. These proteins can be produced in sufficient quantities for functional assays, providing insights into the therapeutic potential of targeting these molecules in various diseases. Understanding the mechanisms of action of Decorin and PGS2, particularly in their combined effects on cell signaling pathways, could lead to novel strategies for managing inflammation-related disorders and enhancing tissue regeneration. This research not only enhances our fundamental understanding of extracellular matrix dynamics but also opens avenues for developing innovative treatments that exploit the regulatory roles of these proteins in health and disease.
