Analytical Data
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Gene name
MLN
- Application
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Alternative Names
MLN；CAB1；MLN64；StAR-related lipid transfer Protein 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
P12872
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Expression Region
26-115aa
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AA Sequence
FVPIFTYGELQRMQEKERNKGQKKSLSVWQRSGEEGPVDPAEPIREEENEMIKLTAPLEIGMRMNSRQLEKYPATLEGLLSEMLPQHAAK
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Molecular Weight
45.5 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
MLN (motilin-like peptide) is a peptide that plays a crucial role in gastrointestinal motility and has garnered attention for its potential therapeutic applications. The research surrounding MLN and its recombinant protein variants stems from its functional similarities to motilin, a well-known gastrointestinal hormone implicated in the regulation of gastric functions and the contraction of smooth muscle. Studies have shown that MLN can influence the secretion of digestive enzymes and promote gastric emptying, making it a significant target for understanding and treating gastrointestinal disorders such as gastroparesis and functional dyspepsia. Advancements in recombinant DNA technology have enabled the production of MLN in a laboratory setting, allowing for detailed studies of its structure, function, and biological effects. By elucidating the mechanisms through which MLN acts, researchers aim to develop novel therapeutic agents that can mimic its effects or enhance its potency. Furthermore, understanding the receptor interactions and signaling pathways involved in MLN’s function could lead to new strategies for modulating gastrointestinal activity. Given the increasing prevalence of gastrointestinal disorders globally, the exploration of MLN as a therapeutic agent is not only timely but could also significantly impact patient care and treatment outcomes. Overall, the investigation of MLN recombinant proteins stands at the intersection of molecular biology, pharmacology, and clinical research, highlighting its potential as a vital component in the future of gastrointestinal therapeutics.
