Analytical Data
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Gene name
VMO1
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简介
Vitelline membrane outer layer protein 1 homolog (VMO1) is first characterized in the outer layer of the vitelline membrane of hen鈥檚 eggs, where VMO1is present together with lysozyme, VMO2, and ovomucin. VMO1 is a secreted protein and exerts important functions in inner ear and tear film, VMO1 may also interact with glycosylated proteins. VMO1 Protein, Human (HEK293, His) is the recombinant human-derived VMO1 protein, expressed by HEK293 , with C-6*His labeled tag.
- Application
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Alternative Names
Vitelline Membrane Outer Layer Protein 1 Homolog; VMO1
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Species
Human
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Source
HEK293
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Tag
C-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q7Z5L0-1
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Expression Region
Q25-S202
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Protein Length
Full Length of Isoform-1 Mature Protein
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Molecular Weight
18-22 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
VMO1 (Vesicular Monoamine Transporter 1) is a protein that plays a crucial role in the transport of monoamines, including neurotransmitters like serotonin, dopamine, and norepinephrine, into vesicles within neurons. The study of VMO1 and its recombinant protein form has gained attention due to its potential implications in understanding various neurological disorders and psychiatric conditions associated with monoamine dysregulation. Research has shown that alterations in monoamine systems can lead to conditions such as depression, anxiety, and schizophrenia. By creating recombinant VMO1 proteins, scientists aim to elucidate its structure-function relationship and its role in vesicular transport mechanisms. This research is critical not only for understanding the basic biology of neurotransmitter storage and release but also for developing therapeutic targets for drug design. Additionally, studying VMO1 in a recombinant form can help investigate its interactions with other proteins and its involvement in cellular signaling pathways, further shedding light on its contribution to neural function and pathology. Overall, the investigation of VMO1 and its recombinant variants presents significant opportunities for advancing neuroscience and developing novel treatments for mental health disorders.
