Analytical Data
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Gene name
OLFML2B
- Application
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Alternative Names
Photomedin-2
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Species
Human
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Source
HEK293
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q68BL8
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Expression Region
23-750aa
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Molecular Weight
86.6 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
OLFML2B, a member of the olfactomedin-like protein family, has garnered increasing attention in the field of biomedical research due to its potential roles in various physiological and pathological processes. Initially identified in neural tissues, OLFML2B is thought to be involved in the regulation of cellular activities such as neuronal development, cell adhesion, and extracellular matrix interactions. Its structure, characterized by the presence of olfactomedin-like domains, suggests functional properties that may influence cell signaling and tissue remodeling. Recent studies have implicated OLFML2B in the modulation of inflammatory responses and its association with certain diseases, including neurodegenerative disorders and cancers. Understanding the functional mechanisms of OLFML2B through recombinant protein studies could unveil its role in health and disease, paving the way for potential therapeutic applications. By producing OLFML2B as a recombinant protein, researchers aim to elucidate its biological functions and interactions at the molecular level, thereby contributing to the development of targeted interventions that leverage its properties. Consequently, the investigation of OLFML2B's structure and function remains a promising avenue for advancing our knowledge of its significance in various biological contexts.
