Analytical Data
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Gene name
MXI1
- Application
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Alternative Names
bHLHc11; Class C basic helix-loop-helix protein 11; MAD 2; MAD2; MAX dimerization protein 2; MAX interacting protein 1; Max interactor 1; Max related transcription factor; MAX-interacting protein 1; MGC43220; MXD 2; MXD2; MXI 1; MXI; mxi1; MXI1 protein; MXI1_HUMAN; Protein MXI1
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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
P50539
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Expression Region
1-228 aa
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AA Sequence
MERVKMINVQ RLLEAAEFLE RRERECEHGY ASSFPSMPSP RLQHSKPPRR LSRAQKHSSG SSNTSTANRS THNELEKNRR AHLRLCLERL KVLIPLGPDC TRHTTLGLLN KAKAHIKKLE EAERKSQHQL ENLEREQRFL KWRLEQLQGP QEMERIRMDS IGSTISSDRS DSEREEIEVD VESTEFSHGE VDNISTTSIS DIDDHSSLPS IGSDEGYSSA SVKLSFTS
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Molecular Weight
26.0 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
MXI1, or MAX Interacting Protein 1, is a member of the MXI family that plays a crucial role in the regulation of gene expression, particularly through its interaction with the Myc transcription factor. Research into MXI1 has gained attention due to its potential implications in cancer biology, where dysregulation of Myc and its associated proteins can lead to uncontrolled cellular proliferation and tumorigenesis. MXI1 is considered a negative regulator of Myc activity, functioning as a tumor suppressor by inhibiting Myc-mediated transcriptional activation. Its expression levels and interactions are thus of great interest in understanding the molecular mechanisms underlying cancer development and progression. Additionally, MXI1's involvement in chromatin remodeling and cellular differentiation processes adds further complexity to its role in cellular physiology. Studies utilizing recombinant MXI1 proteins have aimed to elucidate its structure-function relationship, interactions with other cellular proteins, and its impact on signaling pathways. By characterizing the MXI1 protein in various experimental setups, researchers are endeavoring to uncover its potential as a therapeutic target or biomarker in malignancies, which could ultimately lead to innovative strategies for cancer treatment. Through these efforts, a deeper understanding of MXI1 and its functions in the cellular landscape is anticipated to contribute significantly to the development of targeted therapies and improved patient outcomes in oncology.
