Analytical Data
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Gene name
OLFML3
- Application
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Alternative Names
Olfactomedin-like protein 3,HNOEL-iso,Holf44,OLFML3,PSEC0035, PSEC0173, PSEC0244, UNQ663,PRO1294
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Species
Human
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Source
HEK293
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Tag
C-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NRN5-1
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Expression Region
K120-V406
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AA Sequence
KGKGRRNEKYDMVTDCGYTISQVRSMKILKRFGGPAGLWTKDPLGQTEKIYVLDGTQNDTAFVFPRLRDFTLAMAARKASRVRVPFPWVGTGQLVYGGFLYFARRPPGRPGGGGEMENTLQLIKFHLANRTVVDSSVFPAEGLIPPYGLTADTYIDLAADEEGLWAVYATREDDRHLCLAKLDPQTLDTEQQWDTPCPRENAEAAFVICGTLYVVYNTRPASRARIQCSFDASGTLTPERAALPYFPRRYGAHASLRYNPRERQLYAWDDGYQIVYKLEMRKKEEEV
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Protein Length
Partial
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Molecular Weight
38-45 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
OLFML3 (Olfactomedin-like protein 3) is a member of the olfactomedin-like protein family, which is involved in various biological processes, including cell adhesion, signaling, and the regulation of cellular functions. Recent studies suggest that OLFML3 plays a significant role in the development and progression of certain cancers, as well as in the modulation of immune responses. Understanding the structure and function of OLFML3 is crucial for elucidating its role in these physiological and pathological contexts. Researchers have focused on the recombinant production of OLFML3 protein to explore its biochemical properties and functional mechanisms. By using advanced techniques such as molecular cloning and protein expression systems, scientists aim to obtain pure, functional OLFML3 for in-depth studies, including binding assays, structural analysis, and cellular experiments. These investigations are pivotal for identifying potential therapeutic targets and developing strategies for cancer intervention and immune modulation. As the field of biomedical research continues to advance, the study of OLFML3 will contribute significantly to our understanding of its role in human health and disease, providing a foundation for future therapeutic innovations.
