Analytical Data
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Gene name
MYLIP
- Application
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Alternative Names
MYLIP；BZF1；IDOL；E3 ubiquitin-Protein ligase MYLIP
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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
Q8WY64
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Expression Region
1-445aa
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AA Sequence
MLCYVTRPDAVLMEVEVEAKANGEDCLNQVCRRLGIIEVDYFGLQFTGSKGESLWLNLRNRISQQMDGLAPYRLKLRVKFFVEPHLILQEQTRHIFFLHIKEALLAGHLLCSPEQAVELSALLAQTKFGDYNQNTAKYNYEELCAKELSSATLNSIVAKHKELEGTSQASAEYQVLQIVSAMENYGIEWHSVRDSEGQKLLIGVGPEGISICKDDFSPINRIAYPVVQMATQSGKNVYLTVTKESGNSIVLLFKMISTRAASGLYRAITETHAFYRCDTVTSAVMMQYSRDLKGHLASLFLNENINLGKKYVFDIKRTSKEVYDHARRALYNAGVVDLVSRNNQSPSHSPLKSSESSMNCSSCEGLSCQQTRVLQEKLRKLKEAMLCMVCCEEEINSTFCPCGHTVCCESCAAQLQSCPVCRSRVEHVQHVYLPTHTSLLNLTVI
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Molecular Weight
51.9 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
MYLIP, or Myosin Light Chain-Interacting Protein, has emerged as a significant focus in the field of molecular biology and biochemistry due to its crucial role in various cellular processes, such as muscle contraction and cell signaling. MYLIP is known to interact with myosin light chains, which are essential components of the myosin motor complex, mediating muscle contraction in both cardiac and skeletal muscle tissues. Recent research has highlighted the involvement of MYLIP in regulating lipid metabolism and its implications in the pathogenesis of metabolic disorders, including obesity and diabetes. Given the increasing prevalence of these diseases worldwide, understanding the molecular mechanisms of MYLIP's function could offer novel therapeutic targets for intervention. Moreover, MYLIP has been implicated in the regulation of cellular processes beyond muscle contraction, such as cell division and motility, suggesting that its role might extend to other organ systems and diseases. This multifunctional nature makes MYLIP a compelling subject for further investigation, as elucidating its precise functions and regulatory mechanisms may provide valuable insights into its contribution to health and disease. Thus, the research into MYLIP and its recombinant proteins not only sheds light on fundamental biological processes but also holds promise for the development of innovative treatment strategies for a range of conditions linked to myosin dysfunction and metabolic imbalance.
