Recombinant Human ASH2L Protein

Name: Recombinant Human ASH2L Protein
Brand: Beta LifeScience
SKU: BL-1260SG
Availability: InStock

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Product Overview

Tag	GST
Host Species	Human
Accession	BC015936
Synonym	ASH2L2
Background	Set1/Ash2 histone methyltransferase complex subunit ASH2 (ASH2L) is part of MLL complexes, consisting of one of seven Set/MLL proteins (SETA, SETB, MLL1 to 5), ASH2L, RBBP5, WDR5, HDPY-30, and others. Possesses histone methyltransferase activity. Specifically methylates 'Lys-4' of histone H3 when the neighboring 'Lys-9' residue is not methylated.
Description	Full-length recombinant human ASH2L was produced in E. coli system, fused with a GST tag at N-terminus. This protein is purified with our unique purification methods.
Source	E.coli
AA Sequence	Full Length
Molecular Weight	~94 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 ASH2L 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	Transcriptional regulator. Component or associated component of some histone methyltransferase complexes which regulates transcription through recruitment of those complexes to gene promoters. Component of the Set1/Ash2 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3, but not if the neighboring 'Lys-9' residue is already methylated. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. May play a role in hematopoiesis. In association with RBBP5 and WDR5, stimulates the histone methyltransferase activities of KMT2A, KMT2B, KMT2C, KMT2D, SETD1A and SETD1B.
Subcellular Location	Nucleus.
Database References	HGNC: 744 OMIM: 604782 KEGG: hsa:9070 STRING: 9606.ENSP00000340896 UniGene: Hs.521530
Tissue Specificity	Ubiquitously expressed. Predominantly expressed in adult heart and testis and fetal lung and liver, with barely detectable expression in adult lung, liver, kidney, prostate, and peripheral leukocytes.

Gene Functions References

our results suggest that ASH2L contributes to leukemogenesis by cooperating with other proteins that aberrantly upregulate cellular growth and proliferation pathways. PMID: 28185526
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
Overall, epigenetic modulation is a promising approach to evaluate the role of chromatin structure for the radioresponsiveness of glioma cell lines. PMID: 28044469
Data suggest an interplay between megakaryocytic leukemia 1 (MKL1) and ASH2 protein to promote tumor necrosis factor alpha (TNF-alpha) induced proinflammatory transcription in macrophages. PMID: 28218970
the histone methyltransferase core enzyme ASH2L was bound at EGFR in the germinal matrix and in gliomas where levels of H3K4me3 are high, and the histone acetyltransferase P300 was bound in samples with H3K27ac enrichment PMID: 25996283
Ash2L acts in concert with P53 promoter occupancy to activate RNA Polymerase II by aiding formation of a stable transcription pre-initiation complex required for its activation. PMID: 25023704
ASH2L enhances ERalpha expression as a coactivator of GATA3 in breast cancers PMID: 25258321
Non active site mutations in the MLL1 SET domain render the protein defective for H3K4 dimethylation by the MLL1 core complex, which is associated with a loss of the ability of MLL1 to interact with WRAD or with the RbBP5/Ash2L heterodimer. PMID: 24680668
H2B dependent regulation of MLL family histone methylatransferases depends on the N-terminal WH motif of ASH2L. PMID: 23453805
crystal structure of the C-terminal SPRY domain of human Ash2L PMID: 22231628
The structure shows that Ash2L contains an atypical PHD finger that does not have histone tail-binding activity. PMID: 21660059
ASH2L binds DNA using a forkhead-like helix-wing-helix (HWH) domain. PMID: 21642971
NF-Y acts upstream of H3K4me3 deposition by recruiting Ash2L PMID: 21445285
Protein-arginine methyltransferase 1 (PRMT1) methylates Ash2L, a shared component of mammalian histone H3K4 methyltransferase complexes. PMID: 21285357
Data suggest that both Ash2L/RbBP5 and the MLL1 SET domain make direct contacts with the substrates and contribute to the formation of a joint catalytic center. PMID: 21124902
Results show that Depletion of CHD8 enhances HOXA2 expression and a loss of the WDR5/Ash2L/RbBP5 subcomplex. PMID: 20085832
Ash2l and Saf-A are recruited to the inactive X chromosome at the onset of stable X inactivation. PMID: 20150277
high dimethylation of histone H3 at lysine 4 expression is rare in hepatocellular carcinoma compared with other carcinomas, possibly due to complex epigenetic regulation involving Ash2 PMID: 19896696
These findings offer insight into the molecular role of ASH2L, and by extension that of WDR5, in proper H3K4 trimethylation. PMID: 16892064
Although hASH2 expression at the mRNA level was not deregulated, hASH2 protein expression was increased in most human tumors and tumor cell lines. Knockdown of hASH2 inhibited tumor cell proliferation. These show hASH2 as a novel oncoprotein. PMID: 18245475
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

FAQs

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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.