Analytical Data
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Gene name
FLJ32756
- Application
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Alternative Names
Putative uncharacterized protein FLJ32756
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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
Q96M85
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Expression Region
1-177aa
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AA Sequence
MSHSRRAAPT QDQCHTPGFP TSRETSGSIW QARICGSLQA LDTWRTHIPR KSPAPTQASQ ICLLLPESPW RNPTPRGFLK PLINWDAILY FKEKRNIQVT TQAHPQNQAS CSSQEVATPG LVPQAAAPKV YERSHDNLNA EAQGLAGAQV SKPQNPITRL CSLKEQSILK IFTKQSI
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Molecular Weight
19.6 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
The FLJ32756 recombinant protein, part of a broader investigation into novel therapeutic targets and biomarkers, has gained attention due to its potential roles in various cellular processes. Initially identified through genomic sequencing efforts, FLJ32756 appears to be involved in mechanisms related to cell signaling, metabolism, and potentially, disease pathology. Early studies indicate that variations in its expression levels may correlate with certain diseases, such as cancer and metabolic disorders, suggesting that it could serve as a valuable marker for disease progression or response to therapy. Further characterization of FLJ32756 at the structural and functional levels is crucial for understanding its biological significance. Techniques like recombinant DNA technology have enabled the production of this protein for functional assays, allowing researchers to explore its interactions with other biomolecules and identify potential pathways it influences. The insights gained from such studies could pave the way for developing targeted therapies and improving diagnostic approaches in clinical settings. Overall, the research on FLJ32756 represents a significant step in unraveling the complexities of cellular function and elucidating the molecular underpinnings of various health conditions.
