Analytical Data
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Gene name
FLAG
- Application
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Alternative Names
FLAG;FBG3;FBX30;FBX44;F-box only Protein 44
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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
Q9H4M3
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Expression Region
1-255aa
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AA Sequence
MAVGNINELP ENILLELFTH VPARQLLLNC RLVCSLWRDL IDLVTLWKRK CLREGFITED WDQPVADWKI FYFLRSLHRN LLHNPCAEEG FEFWSLDVNG GDEWKVEDLS RDQRKEFPND QVKKYFVTSY YTCLKSQVVD LKAEGYWEEL MDTTRPDIEV KDWFAARPDC GSKYQLCVQL LSSAHAPLGT FQPDPATIQQ KSDAKWREVS HTFSNYPPGV RYIWFQHGGV DTHYWAGWYG PRVTNSSITI GPPLP
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Molecular Weight
29.7 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
FLAG-tagged proteins, commonly referred to as FLAG fusion proteins, are widely used in molecular biology for the purification, detection, and characterization of proteins of interest. The FLAG tag, a short amino acid sequence derived from the DYKDDDDK peptide, offers several advantages, including high specificity for commercially available anti-FLAG antibodies, which allow for efficient protein purification via affinity chromatography, enabling the study of protein interactions, localization, and function. Originally introduced in the 1990s, FLAG tags revolutionized the way researchers investigate protein expression and purification. This technique has facilitated various applications, from studying protein dynamics in living cells to developing therapeutic proteins. Furthermore, FLAG tags can be used in combination with other peptides or tags to enable multi-step purification processes or to allow for the detection of post-translational modifications. Recent advancements in synthetic biology and protein engineering have expanded the utility of FLAG-tagged proteins, making them indispensable tools for researchers across diverse fields, including biochemistry, cell biology, and drug development. Overall, the FLAG tag represents a significant contribution to our ability to analyze proteins and their functions in a variety of biological contexts.











