Analytical Data
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Gene name
Mup11
- Application
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Alternative Names
Mup11;Mup9;Major urinary Protein 11
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Species
Mouse
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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
P04938
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Expression Region
32-181 aa
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AA Sequence
EKINGEWHTIILASDKREKIEDNGNFRLFLEQIHVLENSLVLKFHTVRDEECSELSMVADKTEKAGEYSVTYDGFNTFTIPKTDYDNFLMAHLINEKDGETFQLMGLYGREPDLSSDIKERFAQLCEEHGILRENIIDLSNANRCLQARE
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Molecular Weight
19.6 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
Mup11, or Major urinary protein 11, is a protein that plays a significant role in the chemical communication among mammals, particularly in the context of pheromonal signaling and territorial marking. These proteins are predominantly found in the urine of rodents, where they serve to convey various social and reproductive information. The study of Mup11 is particularly relevant in understanding the mechanisms of olfactory signaling and its influence on mating behavior and social interactions. In recent years, an increasing interest in the biochemical properties of Mup11 has emerged, driven by advancements in recombinant protein technology, which allows for the production and analysis of Mup11 at a molecular level. By utilizing recombinant DNA techniques, researchers can produce Mup11 in host systems such as bacteria or yeast, facilitating studies on its structure, function, and interaction with receptors. Understanding Mup11’s role can offer insights into the evolution of communication among species, as well as potential applications in pest control and wildlife management. Moreover, characterizing Mup11 provides a valuable model for examining the broader family of major urinary proteins, enriching our knowledge of non-verbal communication mechanisms in mammals. As researchers delve deeper into the functions and interactions of Mup11, the findings may contribute to new avenues in behavioral ecology and endocrinology, shedding light on the complex interplay between chemical signals and animal behaviors.











