Analytical Data
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Gene name
OLFM1
- Application
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Alternative Names
AMY; NOE1; NOELIN1; OlfA
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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
Q99784
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Expression Region
Ala153~Gly420
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Molecular Weight
33kDa
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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
OLFM1, or olfactomedin 1, is a protein that has emerged as an intriguing subject of research due to its significant roles in various biological processes, particularly in neural development and function. It is a member of the olfactomedin domain-containing protein family and is known to interact with glycosaminoglycans and proteins, influencing cell adhesion and signaling. Studies have shown that OLFM1 is involved in regulating neural stem cell proliferation and differentiation, suggesting its potential role in neurogenesis and brain development. Furthermore, dysregulation of OLFM1 expression has been associated with several pathological conditions, including brain tumors and neurodegenerative diseases, highlighting its clinical relevance. The production of recombinant OLFM1 protein is essential for elucidating its structural and functional properties, enabling researchers to investigate its specific mechanisms of action in cellular contexts. By generating a concentrated supply of this protein through recombinant techniques, scientists can conduct extensive biochemical assays and functional studies, paving the way for potential therapeutic applications aimed at modulating OLFM1 activity in disease models. Understanding the detailed interactions and roles of OLFM1 in cellular pathways may provide insights into novel strategies for treating neurological disorders and improving regenerative medicine approaches. Hence, OLFM1 research holds promise not only for advancing basic biology but also for contributing to the development of innovative clinical interventions.
