Analytical Data
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Gene name
OLFML3
- Application
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Alternative Names
HNOEL-iso; hOLF44; OLF44; Olfactomedin like 3; Olfactomedin-like protein 3; OLFL3_HUMAN; OLFML3
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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
Q9NRN5
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Expression Region
22-406 aa
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AA Sequence
QQHHLVEYM ERRLAALEER LAQCQDQSSR HAAELRDFKN KMLPLLEVAE KEREALRTEA DTISGRVDRL EREVDYLETQ NPALPCVEFD EKVTGGPGTK GKGRRNEKYD MVTDCGYTIS QVRSMKILKR FGGPAGLWTK DPLGQTEKIY VLDGTQNDTA FVFPRLRDFT LAMAARKASR VRVPFPWVGT GQLVYGGFLY FARRPPGRPG GGGEMENTLQ LIKFHLANRT VVDSSVFPAE GLIPPYGLTA DTYIDLAADE EGLWAVYATR EDDRHLCLAK LDPQTLDTEQ QWDTPCPREN AEAAFVICGT LYVVYNTRPA SRARIQCSFD ASGTLTPERA ALPYFPRRYG AHASLRYNPR ERQLYAWDDG YQIVYKLEMR KKEEEV
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Molecular Weight
46.0 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
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Protein Description
OLFML3, or Olfactomedin-like 3, is a member of the olfactomedin protein family that has garnered attention due to its potential roles in developmental processes and various diseases. This glycoprotein is predominantly expressed in the central nervous system and has been implicated in cell signaling pathways, particularly those related to neuronal growth and differentiation. Research indicates that OLFML3 may play a significant role in the regulation of neuroinflammation and the pathogenesis of neurodegenerative disorders, such as Alzheimer's disease. Given its involvement in critical biological functions, the study of OLFML3, particularly in its recombinant form, is vital for elucidating its precise mechanisms of action. The generation of recombinant OLFML3 proteins allows for detailed biochemical and biophysical analyses, enabling researchers to explore its structural properties and interactions with other biomolecules. Additionally, understanding the functional implications of OLFML3 in cellular contexts may lead to novel therapeutic strategies to target its pathways, particularly in the realm of neuroprotection and regeneration. Overall, the study of recombinant OLFML3 not only provides insights into its biological roles but also holds promise for advancing our knowledge in neurobiology and potential clinical applications.
