Analytical Data
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Gene name
OLFML1
- Application
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Alternative Names
OLFML1；Olfactomedin-like Protein 1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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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AA Sequence
PAMVHYIYQRFRVLEQGLEKCTQATRAYIQEFQEFSKNISVMLGRCQTYTSEYKSAVGNLALRVERAQREIDYIQYLREADECIESEDKTLAEMLLQEAEEEKKIRTLLNASCDNMLMGIKSLKIVKKMMDTHGSWMKDAVYNSPKVYLLIGSRNNTVWEFANIRAFMEDNTKPAPRKQILTLSWQGTGQVIYKGFLFFHNQATSNEIIKYNLQKRTVEDRMLLPGGVGRALVYQHSPSTYIDLAVDEHGLWAIHSGPGTHSHLVLTKIEPGTLGVEHSWDTPCRSQDAEASFLLCGVLYVVYSTGGQGPHRITCIYDPLGTISEEDLPNLFFPKRPRSHSMIHYNPRDKQLYAWNEGNQIIYKLQTKRKLPLK
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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 (Olfactory Lamine Cell Adhesion Molecule 1) is a member of the olfactomedin-like protein family, which is characterized by its unique structure and role in cell adhesion and signaling. Emerging research has indicated its involvement in various biological processes, including neuronal development, tissue regeneration, and disease mechanisms. Recent studies suggest that OLFML1 may play a pivotal role in tumor progression and metastasis, as its expression levels are often altered in cancer tissues. Additionally, it has been associated with nervous system functions, particularly in olfactory sensory neurons, hinting at its potential roles in sensory perception and neurodevelopment. The recombinant production of OLFML1 protein is crucial for understanding its functional properties and interactions. By creating a standardized and purified version of this protein, researchers aim to elucidate its biochemical characteristics and cellular functions, paving the way for potential therapeutic applications. Investigating OLFML1 through recombinant protein studies can provide insights into its mechanistic roles and could ultimately contribute to the development of novel strategies for targeting related pathologies, particularly in oncology and neurobiology. As the understanding of OLFML1 continues to evolve, it may reveal significant implications for both basic research and clinical applications.
