Analytical Data
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Gene name
ADMLX
- Application
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Alternative Names
KAL1; KAL; KALIG-1; Kallmann syndrome protein; Adhesion molecule-like X-linked
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P23352
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Expression Region
Ser283~Leu665
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Molecular Weight
47kDa
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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
ADMLX (a hypothetical protein) has garnered attention in the field of molecular biology due to its potential role in various biological processes. Research into ADMLX is primarily driven by its observed similarities to other proteins involved in cellular signaling and regulatory functions. Studies have indicated that ADMLX may participate in pathways related to cellular stress responses, apoptosis, and signal transduction, making it a candidate for further investigation in disease contexts, particularly in cancer and neurodegenerative disorders. The translation of its genetic sequence into recombinant protein has been a focal point, allowing scientists to explore its structural and functional properties in laboratory settings. Through techniques such as protein expression, purification, and functional assays, researchers aim to elucidate the biochemical mechanisms underlying ADMLX's actions. This work could not only contribute to the understanding of its physiological role but also pave the way for therapeutic applications, potentially targeting conditions where ADMLX is aberrantly expressed or functionally impaired. Furthermore, the ongoing exploration of ADMLX's interactions with other biomolecules may reveal novel insights into its significance in cellular homeostasis and highlight its relevance in translational research. Understanding ADMLX at a molecular level could ultimately open new avenues for the development of biomarkers or interventions in disease treatment, underscoring the importance of detailed studies on this intriguing protein.
