Analytical Data
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Gene name
OLFM3
- Application
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Alternative Names
OLFM3;NOE3;Noelin-3
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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
Q96PB7
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Expression Region
24-478aa
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AA Sequence
QTLPSLV GLNTTRLSTP DTLTQISPKE GWQVYSSAQD PDGRCICTVV APEQNLCSRD AKSRQLRQLL EKVQNMSQSI EVLNLRTQRD FQYVLKMETQ MKGLKAKFRQ IEDDRKTLMT KHFQELKEKM DELLPLIPVL EQYKTDAKLI TQFKEEIRNL SAVLTGIQEE IGAYDYEELH QRVLSLETRL RDCMKKLTCG KLMKITGPVT VKTSGTRFGA WMTDPLASEK NNRVWYMDSY TNNKIVREYK SIADFVSGAE SRTYNLPFKW AGTNHVVYNG SLYFNKYQSN IIIKYSFDMG RVLAQRSLEY AGFHNVYPYT WGGFSDIDLM ADEIGLWAVY ATNQNAGNIV ISQLNQDTLE VMKSWSTGYP KRSAGESFMI CGTLYVTNSH LTGAKVYYSY STKTSTYEYT DIPFHNQYFH ISMLDYNARD RALYAWNNGH QVLFNVTLFH IIKTEDDT
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Molecular Weight
54.9 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
OLFM3, or Olfactomedin 3, is a glycoprotein primarily expressed in the brain and various reproductive tissues, playing a crucial role in cell signaling and development. Recent studies have highlighted its involvement in neurogenesis, neuronal differentiation, and synaptic plasticity, indicating its potential impact on cognitive functions and neurological disorders. Furthermore, OLFM3 has been implicated in tumor biology, particularly in the context of various cancers, where it exhibits both tumor-suppressive and oncogenic properties depending on the cellular context. The recombinant expression of OLFM3 has garnered interest for its applications in therapeutic strategies, providing insights into disease mechanisms and potential biomarkers. Understanding OLFM3's structure-function relationship through recombinant protein studies can elucidate its biological roles and therapeutic potential, making it a focal point of research in both neuroscience and oncology.











