Analytical Data
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Gene name
NFIX
- Application
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Alternative Names
NFIX；Nuclear factor 1 X-type
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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
Q14938-3
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Expression Region
1-441aa
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AA Sequence
MYSPYCLTQDEFHPFIEALLPHVRAFSYTWFNLQARKRKYFKKHEKRMSK DEERAVKDELLGEKPEIKQKWASRLLAKLRKDIRPEFREDYVLTITGKKP PCCVLSNPDQKGKIRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERL YKSPQCSNPGLCVQPHHIGVTIKELDLYLAYFVHTPESGQSDSSNQQGDA DIKPLPNGHLSFQDCFVTSGVWNVTELVRVSQTPVATASGPNFSLADLES PSYYNINQVTLGRRSITSPPSTSTTKRPKSIDDSEMESPVDDVFYPGTGR SPAAGSSQSSGWPNDVDAGPASLKKSGKLDFCSALSSQGSSPRMAFTHHP LPVLAGVRPGSPRATASALHFPSTSIIQQSSPYFTHPTIRYHHHHGQDSL KEFVQFVCSDGSGQATGQHSQRQAPPLPTGLSASDPGTATF
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Molecular Weight
74 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
NFIX (Nuclear Factor I X) is a transcription factor belonging to the Nuclear Factor I (NFI) family, which plays a crucial role in various biological processes, including cell differentiation, proliferation, and development. Research on NFIX has garnered significant attention due to its involvement in essential cellular functions and its implications in various diseases, including cancer and neurological disorders. The study of NFIX recombinant proteins has been instrumental in elucidating its functional characteristics and regulatory mechanisms. By expressing NFIX in a recombinant form, researchers can investigate its interactions with other proteins, DNA, and various signaling pathways. The ability to produce NFIX as a fusion protein with tags has facilitated the purification and characterization of this protein, allowing for detailed studies on its structural and functional properties. Moreover, understanding the role of NFIX in gene expression regulation can provide insights into developmental processes and potential therapeutic targets for diseases associated with NFIX dysregulation. The ongoing research into NFIX recombination not only advances our knowledge of its biological roles but also opens avenues for developing novel therapeutic strategies in regenerative medicine and cancer treatment. As NFIX continues to be a focal point of investigation, the exploration of its recombinant variants may uncover new dimensions of its function and regulation in health and disease.
