Analytical Data
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Gene name
ID4
- Application
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Alternative Names
bHLHb27; Class B basic helix-loop-helix protein 27; DNA binding protein inhibitor ID 4; DNA binding protein inhibitor ID4; DNA-binding protein inhibitor ID-4; ID 4; Id4; ID4_HUMAN; IDB4
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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
P47928
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Expression Region
1-161aa
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AA Sequence
MKAVSPVRPS GRKAPSGCGG GELALRCLAE HGHSLGGSAA AAAAAAAARC KAAEAAADEP ALCLQCDMND CYSRLRRLVP TIPPNKKVSK VEILQHVIDY ILDLQLALET HPALLRQPPP PAPPHHPAGT CPAAPPRTPL TALNTDPAGA VNKQGDSILC R
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Molecular Weight
16.6 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
ID4 is a member of the inhibitor of differentiation (ID) family of proteins, which play crucial roles in regulating cell growth, differentiation, and proliferation. Initially identified for its involvement in the maintenance of multipotent progenitor cells, ID4 has garnered significant attention due to its implications in various biological processes, including embryonic development and tumorigenesis. Research has shown that ID4 functions as a dominant-negative regulator of basic helix-loop-helix (bHLH) transcription factors, thereby influencing cellular fate decisions. Its expression patterns are particularly prominent in certain cancers, suggesting a potential role in oncogenesis and serving as a biomarker for cancer diagnosis and progression. Moreover, studies have indicated that ID4 may contribute to stem cell-like properties in cancer cells, making it a target of interest for therapeutic interventions. Understanding the molecular mechanisms underlying ID4 activity could pave the way for novel approaches in regenerative medicine and cancer therapy. Thus, ongoing research into the recombinant production of ID4 protein aims to elucidate its structure-function relationships and further explore its potential as a clinical target.
