Recombinant Human Eyes Absent Homolog 2 (EYA2) Protein (His-SUMO)

Name: Recombinant Human Eyes Absent Homolog 2 (EYA2) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-04307P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Eyes Absent Homolog 2 (EYA2) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O00167
Target Symbol	EYA2
Synonyms	EAB 1; EAB1; EYA 2; EYA transcriptional coactivator and phosphatase 2; EYA2; EYA2_HUMAN; eyes absent 2 homolog (Drosophila); Eyes absent homolog 2 (Drosophila); Eyes absent homolog 2; Translation of this uORF probably lowers the translation efficiency of EYA2
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MVELVISPSLTVNSDCLDKLKFNRADAAVWTLSDRQGITKSAPLRVSQLFSRSCPRVLPRQPSTAMAAYGQTQYSAGIQQATPYTAYPPPAQAYGIPSFSTSPTGQSPYTYQMHGTTGFYQGGNGLGNAAGFGSVHQDYPSYPGFPQSQYPQYYGSSYNPPYVPASSICPSPLSTSTYVLQEASHNVPNQSSESLAGEYNTHNGPSTPAKEGDTDRPHRASDGKLRGRSKRSSDPSPAGDNEIERVFVWDLDETIIIFHSLLTGTFASRYGKDTTTSVRIGLMMEEMIFNLADTHLFFNDLEDCDQIHVDDVSSDDNGQDLSTYNFSADGFHSSAPGANLCLGSGVHGGVDWMRKLAFRYRRVKEMYNTYKNNVGGLIGTPKRETWLQLRAELEALTDLWLTHSLKALNLINSRPNCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKTGKESCFERIMQRFGRKAVYVVIGDGVEEEQGAKKHNMPFWRISCHADLEALRHALELEYL
Expression Range	1-514aa
Protein Length	Full Length of Isoform 2
Mol. Weight	72.7kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Functions both as protein phosphatase and as transcriptional coactivator for SIX1, and probably also for SIX2, SIX4 and SIX5. Tyrosine phosphatase that dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph) and promotes efficient DNA repair via the recruitment of DNA repair complexes containing MDC1. 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Its function as histone phosphatase may contribute to its function in transcription regulation during organogenesis. Plays an important role in hypaxial muscle development together with SIX1 and DACH2; in this it is functionally redundant with EYA1.
Subcellular Location	Cytoplasm. Nucleus.
Protein Families	HAD-like hydrolase superfamily, EYA family
Database References	HGNC: 3520 OMIM: 601654 KEGG: hsa:2139 STRING: 9606.ENSP00000333640 UniGene: Hs.472877
Tissue Specificity	Highest expression in muscle with lower levels in kidney, placenta, pancreas, brain and heart.

Gene Functions References

our data indicate that Eya2 may serve as a potential oncoprotein in human astrocytoma. Eya2 regulates astrocytoma cell proliferation and invasion, possibly through the regulation of ERK signaling. PMID: 28901379
EYA2 knockdown led to decreased metastatic spread of breast cancer cells to the lung and greatly attenuated the ability of EGFR to regulate the epithelial-to-mesenchymal transition markers. PMID: 28703807
High EYA2 expression is associated with acute myeloid leukemia. PMID: 28416638
EYA2 functions as a stimulant in lung adenocarcinoma pathogenesis. PMID: 26329363
results demonstrate that overexpression of miR-30a in lung adenocarcinoma A549 cells can inhibit cell migration and invasion, which is partially attributed to the decrease of EYA2 expression PMID: 26837415
SIX1 and EYA are often co-overexpressed in tumors, and the SIX1-EYA2 interaction has been shown to be critical for metastasis in a breast cancer model. PMID: 25555392
Decreased expression of EYA2 is associated with pancreatic adenocarcinomas. PMID: 24810906
This interaction suggests that CDK6 regulates EYA2 activity, a mechanism that could be important in development and in cancer. PMID: 24196439
MIR30A represses Eya2 expression by binding to the 3'-untranslated region of Eya2.The MIR30A/EYA2 axis regulates breast cancer cell proliferation and migration. PMID: 24508260
Functional roles of candidate genes EYA2 (20q13) and hsa-miR-375 (2q35) were studied by siRNA-mediated knock-down and overexpression, respectively, in hrHPV-containing cell lines. PMID: 22987659
Given that SIX1 and EYA are overexpressed in many tumor types, our data indicate that targeting the SIX1-EYA complex may be a potent approach to inhibit tumor progression in multiple cancer types PMID: 23435380
Studies indicate that the RNA and protein levels of Eya2 is upregulated in ovarian cancer. PMID: 22607316
Data implicate Eya2 as a necessary co-factor for many of the metastasis promoting functions of Six1. PMID: 21706047
Expression of EYA2 in lung adenocarcinoma is augmented. PMID: 19950702
Based on observation that the dachshund-binding site is located between the catalytic core & Sine Oculis binding sites within ED-Eya2, we propose that catalytic activity can be translated to SO binding through DAC, which acts as a transcriptional switch. PMID: 19858093
EYA2 was found to function as transcriptional activator in ovarian cancer cells by Gal4 assay and to promote tumor growth in vivo in xenograft models. PMID: 15705892
EYA2 and EYA3 displayed specificity for Tyr-142 of H2A.X PMID: 19351884

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.