Analytical Data
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Gene name
MLXIP
- Application
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Alternative Names
Class E basic helix-loop-helix protein 36 ;bHLHe36Transcriptional activator MondoA
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9HAP2
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Expression Region
1-217aa
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Molecular Weight
38.8 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
MLXIP, also known as Max-like protein X interacting protein, is a key transcription factor that plays a crucial role in various biological processes, including glucose metabolism, energy homeostasis, and cellular response to stress. Dysregulation of MLXIP has been linked to metabolic disorders, obesity, and type 2 diabetes, making it a significant target for research aimed at understanding these conditions. The study of recombinant MLXIP proteins involves the expression and purification of this protein in a heterologous system, enabling researchers to investigate its biochemical properties, interaction networks, and functional mechanisms. This research is essential for identifying potential therapeutic targets and developing new treatments for metabolic diseases. Advances in recombinant protein technology have facilitated the production of MLXIP in sufficient quantities, allowing for detailed structural and functional studies using techniques such as X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy. Furthermore, the investigation of MLXIP's post-translational modifications and interaction with other proteins is critical for elucidating its regulatory roles in cellular metabolism. Overall, the exploration of MLXIP recombinant proteins is a promising avenue in the quest to understand metabolic diseases and to propose innovative therapeutic strategies.
