Analytical Data
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Gene name
WDR5
- Application
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Alternative Names
BIG3
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Species
Human
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P61964
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Expression Region
S22-C334
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Protein Length
Partial
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Molecular Weight
34.4 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
WDR5 (WD repeat domain 5) is a crucial protein that plays a significant role in various biological processes, including gene regulation, chromatin remodeling, and cell differentiation. It is a key component of the MLL (Mixed Lineage Leukemia) complex, which is essential for the methylation of histone H3 at lysine 4 (H3K4me), a modification associated with active gene transcription. Aberrant regulation of WDR5 and its associated complexes has been implicated in several diseases, most notably in hematological malignancies such as leukemia. Given its pivotal role in gene expression and potential as a therapeutic target, researchers have turned their focus towards the structural and functional characterization of WDR5. Recombinant WDR5 proteins are often generated for biochemical studies to unravel the mechanisms of its interaction with various partners, including the MLL complex and other chromatin-associated proteins. This research is not only crucial for understanding the fundamental biology of gene regulation but also holds promise for developing targeted therapies in cancer treatment. Investigating the structure-function relationship of WDR5 and its interactions can lead to the identification of small molecules that inhibit its activity, providing a potential strategy for combating WDR5-related pathologies. Overall, the study of WDR5 and its recombinant forms is a burgeoning field with significant implications for cancer biology and therapeutic innovation.
