Analytical Data
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Gene name
OLFML1
- Application
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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
Q6UWY5
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Expression Region
29-402aa
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Molecular Weight
49.0 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
OLFML1 (Olfactomedin-like protein 1) is a member of the olfactomedin-domain containing protein family, which is known for its roles in various biological processes, including cell adhesion, proliferation, and differentiation. Recent studies have indicated that OLFML1 may play a significant role in the regulation of developmental and pathological conditions, particularly in the context of cancer and neurological disorders. By mediating signaling pathways and interacting with specific receptors, OLFML1 is believed to influence cellular behavior and tissue homeostasis. Researchers have increasingly focused on the recombinant expression of OLFML1 to explore its functional roles and potential therapeutic applications. The generation of recombinant OLFML1 allows for the investigation of its biochemical properties, interaction with other proteins, and impact on cellular functions in vitro and in vivo. Understanding the molecular mechanisms underlying OLFML1 activity could provide valuable insights into its contributions to health and disease, potentially leading to the development of novel diagnostic and therapeutic strategies targeting this protein. As such, the study of OLFML1 recombinant protein is not only important for basic scientific knowledge but also holds promise for clinical advancements in treating diseases associated with its dysregulation.
