Analytical Data
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Gene name
Major urinary 蛋白 2
- Application
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Alternative Names
Mup2; Major urinary protein 2; MUP 2
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Species
Mouse
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Source
Yeast
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P11589
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Expression Region
19-180aa
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Molecular Weight
20.7 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
Major urinary protein (MUP) is a significant component of murine urine, playing critical roles in chemical signaling and social communication among mice. Research into MUPs has gained attention due to their involvement in various biological processes, including pheromone signaling and mate selection, which are vital for reproductive success. MUPs are known to form stable dimers and have distinct conformational variation, which contribute to their diverse biological functions. Recent advancements in recombinant protein technology have allowed scientists to produce MUPs in vitro, facilitating studies on their structure-function relationships and enabling exploration of their roles in complex behavioral and ecological contexts. This research has potential implications not only in understanding rodent behavior but also in broader fields such as evolutionary biology and pheromone research. The exploration of recombinant MUPs aids in elucidating their binding affinities, interaction with receptors, and potential applications in developing pheromone-based biotechnological innovations. By enhancing our knowledge of MUPs, these studies may pave the way for novel strategies in pest control and wildlife management, highlighting the intricate connections between protein structure, function, and behavioral ecology.
