Analytical Data
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Gene name
FLJ10618
- Application
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Alternative Names
SLC25A36; Solute carrier family 25 member 36
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96CQ1
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Expression Region
1-311aa
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AA Sequence
MSQRDTLVHLFAGGCGGTVGAILTCPLEVVKTRLQSSSVTLYISEVQLNTMAGASVNRVVSPGPLHCLKVILEKEGPRSLFRGLGPNLVGVAPSRAIYFAAYSNCKEKLNDVFDPDSTQVHMISAAMAGFTAITATNPIWLIKTRLQLDARNRGERRMGAFECVRKVYQTDGLKGFYRGMSASYAGISETVIHFVIYESIKQKLLEYKTASTMENDEESVKEASDFVGMMLAAATSKTCATTIAYPHEVVRTRLREEGTKYRSFFQTLSLLVQEEGYGSLYRGLTTHLVRQIPNTAIMMATYELVVYLLNG
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Molecular Weight
59.95 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
FLJ10618, identified as a recombinant protein, has garnered attention in the field of molecular biology and biotechnology due to its potential implications in various therapeutic applications. Initially, its gene was isolated and characterized from human cDNA libraries, providing insights into its unique structural and functional properties. The protein's expression patterns and functional roles remain under investigation, particularly in relation to its involvement in cell signaling pathways and disease mechanisms. Research suggests that FLJ10618 may play critical roles in cellular processes such as proliferation, differentiation, and apoptosis, potentially linking it to conditions like cancer and metabolic disorders. Its recombinant form allows for extensive study, enabling researchers to explore the protein's interactions with other biomolecules, assess its stability, and evaluate its efficacy as a therapeutic agent. Recent advancements in recombinant protein technologies have facilitated the production of FLJ10618 in various host systems, which further enhances its potential for biomedical applications. Ongoing studies are focused on elucidating its biological functions, determining its molecular interactions, and exploring its viability as a drug target or therapeutic conjugate, thereby expanding the understanding of its role in health and disease. As research progresses, FLJ10618 not only promises to contribute significantly to the current knowledge of protein function but also represents a potential frontier for innovative approaches in personalized medicine and targeted therapies.











