Analytical Data
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Gene name
NFIB
- Application
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Alternative Names
NFIB；Nuclear factor 1 B-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
O00712
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Expression Region
2-420aa
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AA Sequence
MYSPICLTQ DEFHPFIEAL LPHVRAIAYT WFNLQARKRK YFKKHEKRMS KDEERAVKDE LLSEKPEIKQ KWASRLLAKL RKDIRQEYRE DFVLTVTGKK HPCCVLSNPD QKGKIRRIDC LRQADKVWRL DLVMVILFKG IPLESTDGER LMKSPHCTNP ALCVQPHHIT VSVKELDLFL AYYVQEQDSG QSGSPSHNDP AKNPPGYLED SFVKSGVFNV SELVRVSRTP ITQGTGVNFP IGEIPSQPYY HDMNSGVNLQ RSLSSPPSSK RPKTISIDEN MEPSPTGDFY PSPSSPAAGS RTWHERDQDM SSPTTMKKPE KPLFSSASPQ DSSPRLSTFP QHHHPGIPGV AHSVISTRTP PPPSPLPFPT QAILPPAPSS YFSHPTIRYP PHLNPQDTLK NYVPSYDPSS PQTSQSWYLG
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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
The NFIB (Nuclear Factor I B) protein has garnered significant attention in molecular biology and cancer research due to its pivotal role in various cellular processes, including cell differentiation, proliferation, and survival. As a member of the Nuclear Factor I (NF-I) family, NFIB functions as a transcription factor that regulates gene expression by binding to specific DNA sequences. Research has shown that NFIB is involved in the oncogenic pathways of several cancers, particularly in breast and prostate tumors, where it tends to enhance the transcription of genes associated with tumor growth and metastasis. The dysregulation of NFIB has been linked to poor prognosis and aggressive tumor behavior, making it a potential biomarker for cancer progression. Moreover, NFIB's interaction with other signaling pathways, such as those involving the PI3K/Akt and MAPK/ERK cascades, further underscores its significance in cancer biology. Recent studies focusing on the characterization of NFIB's protein structure and its binding mechanisms have opened new avenues for therapeutic interventions, aiming to disrupt its oncogenic functions. Understanding NFIB's role in the cancer microenvironment and its potential as a target for novel therapies could lead to advancements in the treatment and management of malignancies, highlighting the need for continued research in this area.
