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AB95193

Recombinant Mouse Mup1 protein

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(1 Publication)

Recombinant Mouse Mup1 protein is a Full Length protein, expressed in Escherichia coli, with 99%, suitable for ELISA, WB, FuncS.

View Alternative Names

Ltn 1, Lvtn 1, Mup 10, Mup 7, Mup a, NP, Nucleoprotein, Up 1, major urinary protein 1

Key facts

Purity

99% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

WB, ELISA, FuncS

applications

Biologically active

No

Animal free

No

Carrier free

No

Reconstitution

Reconstitute at 1 mg/mL in water

Storage buffer

Constituents: PBS

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p>Cell culture and/or animal studies</p>" } } }

Sequence info

[{"sequence":"MKMLLLLCVGLTLVCVHAEEASSTGRNFNVEKINGEWHTIILASDKREKIEDNGNFRLFLEQIHVLENSLVLKFHTVRDEECSELSMVADKTEKAGEYSVTYDGFNTFTIPKTDYDNFLMAHLINEKDGETFQLMGLYGREPDLSSDIKERFAQLCEKHGILRENIIDLSNANRCLQARE","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":null,"tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The Mup1 protein also known as Major Urinary Protein 1 has a molecular mass of approximately 19 kDa. It is expressed predominantly in the liver and secreted into the urine where it functions as a pheromone carrier. Mup1 is part of a large family of proteins called lipocalins known for their role in binding small hydrophobic molecules. In rodents Mup1 binds to volatile pheromones which are important for communication. Its expression pattern and functional role make Mup1 a significant protein for research concerning biochemical signaling mechanisms.
Biological function summary

Mup1 plays a substantial role in the modulation of pheromone signaling interacting with receptors in target organisms. It is not part of larger protein complexes but functions independently to facilitate chemical communication. Mup1's role extends beyond simple pheromone transport as it impacts mating behaviors and territorial marking in rodents. By carrying specific ligands Mup1 influences reproductive signaling and social interaction defining its importance in ecological studies.

Pathways

Mup1 influences pheromonal communication and social behavior pathways in mammals. It significantly interacts with the olfactory signaling pathway where it binds to receptors such as V1R and V2R on sensory neurons. The activity of Mup1 in these pathways highlights its connection to the neural circuits responsible for detecting social cues linking it to other proteins involved in olfactory signal transduction.

Mup1 has shown links to metabolic regulation disorders particularly obesity. Altered Mup1 expression affects glucose metabolism and energy homeostasis connecting it to proteins like leptin and adiponectin known for their roles in metabolic processes. Furthermore research indicates potential links between Mup1 and neurological disorders related to social behavior though the exact mechanisms remain under investigation. These associations highlight the significance of Mup1 in the context of both metabolic and neurobehavioral studies.

Specifications

Form

Lyophilized

Additional notes

purified by a single-step affinity chromatography using NINTA resin

General info

Product protocols

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Scientific reports 8:10723 PubMed30013070

2018

Quantitative proteomic characterization of cellular pathways associated with altered insulin sensitivity in skeletal muscle following high-fat diet feeding and exercise training.

Applications

Unspecified application

Species

Unspecified reactive species

Maximilian Kleinert,Benjamin L Parker,Thomas E Jensen,Steffen H Raun,Phung Pham,Xiuqing Han,David E James,Erik A Richter,Lykke Sylow
View all publications

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