Recombinant Human WDR5 Protein

Name: Recombinant Human WDR5 Protein
Brand: Beta LifeScience
SKU: BL-1270SG
Availability: InStock

Collections: High-quality recombinant proteins, Other recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Tag	His
Host Species	Human
Accession	BC001635
Synonym	BIG3; BIG-3
Background	WD repeat-containing protein 5 (WDR5) is a conserved subunit of Trithorax (TRX) histone methyltransferase complexes. Selectively binds dimethylated Lys4 (K4me2) in histone H3 to promote K4 trimethylation by TRX.
Description	Full-length recombinant human WDR5 was produced in E. coli system, fused with a His tag at N-terminus.
Source	E.coli
AA Sequence	Full Length
Molecular Weight	~40 kDa
Purity	For specific purity information on a given lot, see related COA.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability	The recombinant protein is stable for up to 12 months at -70°C
Usage	For Research Use Only
Storage	Recombinant Human WDR5 Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Contributes to histone modification. May position the N-terminus of histone H3 for efficient trimethylation at 'Lys-4'. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. May regulate osteoblasts differentiation. In association with RBBP5 and ASH2L, stimulates the histone methyltransferase activities of KMT2A, KMT2B, KMT2C, KMT2D, SETD1A and SETD1B.
Subcellular Location	Nucleus.
Protein Families	WD repeat WDR5/wds family
Database References	HGNC: 12757 OMIM: 609012 KEGG: hsa:11091 STRING: 9606.ENSP00000351446 UniGene: Hs.397638

Gene Functions References

WDR5 was identified as a substrate of SETD6 and it was revealed that the methylation of specific lysines (K207/K325) of WDR5 was critical for maintaining global histone H3K4me3 levels and promoting breast cancer cell proliferation and migration PMID: 30226578
WDR5 is aberrantly overexpressed in head neck squamouos cell carcinoma and associates with aggressiveness and unfavorable prognosis, thus representing a novel diagnostic and prognostic biomarker for the cancer. PMID: 29569374
This is the first demonstration of the mechanism of E2/ERalpha signalling activation via the BIG3-PKA-PP1Calpha tri-complex in breast cancer cells. PMID: 28555617
Data found that the expression of WDR5 increased in a majority of the human gastric cancer tissues. Its knockdown significantly inhibited the ability of cell proliferation, reversed cell cycle arrest as well as cell's tumorigenicity. Data reveal that WDR5 may have oncogenic effect and WDR5-mediated H3K4 methylation plays an important role in gastric cancer. PMID: 29125890
findings reveal a nongenomic function for WDR5 in regulating H3K4 methylation induced by 3D environments, physical properties of the nucleus, cell polarity, and cell migratory capacity. PMID: 29987046
HCMV infection increases protein levels of WD repeat-containing protein 5 (WDR5) during infection, overexpression of WDR5 enhances viral replication, and knockdown of WDR5 dramatically attenuates viral replication. The results indicate that WDR5 promotes the nuclear egress of viral capsids, the depletion of WDR5 resulting in a significant decrease in production of infectious virions. PMID: 29437978
our findings indicate that HOXD-AS1 promotes proliferation, castration resistance, and chemo-resistance in prostate cancer by recruiting WDR5. PMID: 28487115
Functional analysis implicates TNRC6A, NAT10, MED14, and WDR5 in RNA-mediated transcriptional activation. PMID: 28813667
The decrease in WDR5 expression was particularly evident in HD-hiPSCs compared to hESCs and control-hiPSCs from healthy subjects PMID: 28476540
we demonstrate for the first time that targeted expression of miR-31-5p using a nonviral minicircle vector can serve as a novel approach for tumor miRNA therapy. Moreover, WDR5 may be a promising therapeutic target for NPC treatment. PMID: 28042945
WDR5 may have oncogenic effect and WDR5-mediated H3K4 methylation plays an important role in leukemogenesis PMID: 27192115
WDR5 functions to sustain proper execution of DNA replication in pancreatic ductal adenocarcinoma cells, as previously suggested by replication stress studies involving MLL1, and c-Myc, also found to interact with WDR5. PMID: 27320920
This report documents a novel lncRNA, GClnc1, which may act as a scaffold to recruit the WDR5 and KAT2A complex and modify the transcription of target genes. This study reveals that GClnc1 is an oncogenic lncRNA in human gastric cancer. PMID: 27147598
different cancer mutations in MLL1 lead to a loss or increase in activity, illustrating the complex and tumor-specific role of MLL1 in carcinogenesis. PMID: 28182322
WDR5 shows a direct binding to the ZNF407 promoter. PMID: 28300833
Taken together, these data suggest that WDR5 is directly involved in p53 signaling pathway. Our studies provide a new insight into WDR5 functions in A549 cells. PMID: 28412363
Targeted Disruption of the Interaction between WD-40 Repeat Protein 5 (WDR5) and Mixed Lineage Leukemia (MLL)/SET1 Family Proteins Specifically Inhibits MLL1 and SETd1A Methyltransferase Complexes. PMID: 27563068
WDR5 over-expression is associated with poor breast cancer clinical outcome. PMID: 26355959
Results identify WDR5 as a key cofactor for N-Myc-regulated transcriptional activation and tumorigenesis and as a novel therapeutic target for MYCN-amplified neuroblastomas. PMID: 26471359
BIG3 may block the KPNAs (KPNA1, KPNA5, and KPNA6) binding region(s) of PHB2. PMID: 26052702
solution structures of the MLL3 core complex assembled with and without WDR5 by small angle x-ray scattering show similar overall topologies PMID: 26324722
Target gene recognition by MYC depends on its interaction with WDR5. This interaction could create an avidity-based chromatin recognition mechanism allowing MYC to select its target genes in response to both genetic and epigenetic determinants. Review. PMID: 26383167
we have discovered that WDR5 plays an important role in bladder cancer suggesting that WDR5 is a potential biomarker and a promising target in the treatment of bladder cancer. PMID: 25656485
Wdr5-MLL interaction in C/EBPA N-terminal leukemia is a promising pharmacological target. PMID: 26167872
findings prove that the TSP-1/CD47/SIRP-alpha signal axis is important to the evolution of tumor cells in the microenvironment of immunotherapy and identify thrombospondin-1 as a key signal PMID: 25666610
results identify WDR5 as a critical epigenomic integrator of histone phosphorylation and methylation and as a major driver of androgen-dependent prostate cancer cell proliferation PMID: 24793694
BIG3(WRD5)-PHB2 interaction is critical for the tamoxifen resistance of breast cancer cells; its targeting reverses the resistance. PMID: 24051437
Data indicate that MLL1 methylates Ash2L in the absence of histone H3, but only when assembled within a complex with WDR5 and RbBP5. PMID: 24235145
data are consistent with a model in which WDR5 binds the gamma-globin promoter in a PRMT5-dependent manner. PMID: 22689669
A small molecule antagonist binds to WDR5 in the peptide-binding pocket which inhibits the catalytic activity of mixed-lineage leukemia protein. PMID: 22989411
we defined a role for Trithorax proteins WDR5 and MLL2 in activating the differentiation gene program in epidermal progenitor cells PMID: 22829784
WDR5-Win motif interaction is important for the assembly of the MLL1 core complex in vivo. PMID: 22665483
findings show that WDR5 is a direct target of SRY; the interaction of WDR5 and SRY activates Sox9 expression; results suggest that, in conjunction with SRY, WDR5 plays an important role in sex determination PMID: 22523547
WDR5 as a critical substrate of CUL4B in regulating neuronal gene expression. PMID: 21816345
crystal structure of WDR5 in ternary complex with RbBP5 and MLL1 PMID: 21220120
the change of folding free energy by mutations mainly corresponds to the deletion of hydrogen bonds. PMID: 20939513
NSL is composed of nine subunits. Two of its subunits, WD repeat domain 5 (WDR5) and host cell factor 1 (HCF1), are shared with members of the MLL/SET family of histone H3 lysine 4 (H3K4) methyltransferase complexes. PMID: 20018852
Results show that Depletion of CHD8 enhances HOXA2 expression and a loss of the WDR5/Ash2L/RbBP5 subcomplex. PMID: 20085832
WDR5 is essential in assembling a virus-induced VISA-associated complex and plays an important role in virus-triggered induction of type I interferons. PMID: 20080758
The WDR5 is required for binding of the methyltransferase complex to the K4-dimethylated H3 tail as well as for global H3 K4 trimethylation and HOX gene activation in human cells. PMID: 15960974
Wdr5 has a funcitonal role in endocondral bone formation PMID: 16340128
the high-resolution X-ray structures of WDR5 in the unliganded form and complexed with histone H3 peptides having unmodified and mono-, di- and trimethylated K4 PMID: 16829959
the crystal structure of WDR5 bound to a histone H3 PMID: 16829960
WDR5 mediates interactions of the MLL1 catalytic unit both with the common structural platform and with the histone substrate. PMID: 16878130
involvement of WDR5 in binding and presenting histone H3K4 for further methylation PMID: 16946699
WDR5's recognition of arginine 3765 of MLL1 is essential for the assembly and enzymatic activity of the MLL1 core complex in vitro PMID: 18829457
WDR5 recognizes Arg-3765 of MLL1, which is essential for the assembly and enzymatic activity of the MLL1 core complex PMID: 18829459
analysis of interactions between WDR5, the catalytic subunit, MLL, and the substrate, histone H3, of the MLL complex PMID: 18840606
The identified components revealed factors involved in histone methylation and cell cycle control and include Ash2L, RbBP5, WDR5, HCF-1, DBC-1, and EMSY. PMID: 19131338
Activation of an estrogen/estrogen receptor signaling by BIG3 through its inhibitory effect on nuclear transport of PHB2/REA in breast cancer is reported. PMID: 19496786

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.