Recombinant Human Ephrin A1/EFNA1 Protein (denatured)

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Host Species	Human
Accession	P20827
Synonym	B61 ECKLG EFL 1 EFL1 EFNA 1 Efna1 EFNA1_HUMAN EPH related receptor tyrosine kinase ligand 1 EPH-related receptor tyrosine kinase ligand 1 Ephrin-A1 Ephrin-A1, secreted form EphrinA1 EPLG 1 EPLG1 Immediate early response protein B61 LERK 1 LERK-1 LERK1 Ligand of eph related kinase 1 OTTHUMP00000033242 OTTHUMP00000033271 secreted form TNF alpha-induced protein 4 TNFAIP 4 TNFAIP4 Tumor necrosis factor alpha induced protein 4 Tumor necrosis factor alpha-induced protein 4
Description	Recombinant Human Ephrin A1/EFNA1 Protein (denatured) was expressed in E.coli. It is a Full length protein
Source	E.coli
AA Sequence	MGSSHHHHHHSSGLVPRGSHMDRHTVFWNSSNPKFRNEDYTIHVQLNDYV DIICPHYEDHSVADAAMEQYILYLVEHEEYQLCQPQSKDQVRWQCNRPSA KHGPEKLSEKFQRFTPFTLGKEFKEGHSYYYISKPIHQHEDRCLRLKVTV SGKITHSPQAHVNPQEKRLAADDPEVRVLHSIGHS
Molecular Weight	22 kDa including tags
Purity	>90% SDS-PAGE.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Liquid Solution
Stability	The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution	See related COA
Unit Definition	For Research Use Only
Storage Buffer	Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function	Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. Plays an important role in angiogenesis and tumor neovascularization. The recruitment of VAV2, VAV3 and PI3-kinase p85 subunit by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly. Exerts anti-oncogenic effects in tumor cells through activation and down-regulation of EPHA2. Activates EPHA2 by inducing tyrosine phosphorylation which leads to its internalization and degradation. Acts as a negative regulator in the tumorigenesis of gliomas by down-regulating EPHA2 and FAK. Can evoke collapse of embryonic neuronal growth cone and regulates dendritic spine morphogenesis.
Subcellular Location	Cell membrane; Lipid-anchor, GPI-anchor.; [Ephrin-A1, secreted form]: Secreted.
Protein Families	Ephrin family
Database References	HGNC: 3221 OMIM: 191164 KEGG: hsa:1942 STRING: 9606.ENSP00000357392 UniGene: Hs.516664
Tissue Specificity	Brain. Down-regulated in primary glioma tissues compared to the normal tissues. The soluble monomeric form is expressed in the glioblastoma multiforme (GBM) and breast cancer cells (at protein level).

Gene Functions References

ephrin-A1 seems to be remarkably involved in elementary processes of endothelial migration like cellular polarization, migratory direction and speed. PMID: 27742560
Findings show that EFNA1 expression is a useful marker for predicting a high risk of recurrence in hepatocellular carcinoma patients but not EPHA2. PMID: 24969670
Results suggest that EFNA1 is involved in colorectal tumorigenesis, and rs12904 A>G polymorphism in the 3' UTR of EFNA1 is associated with CRC susceptibility in a Chinese population. PMID: 24175772
EphA2-ephrinA1 trans-endocytosis is sensitive to the mechanical properties of a cell's microenvironment PMID: 24853748
Ephrin-A1 is upregulated in tumor microenvironment and promotes angiogenesis through a coordinated cross-talk with PI3K/Akt-dependent eNOS activation. PMID: 24040255
The interaction between ephrin-As, Eph receptors and integrin alpha3 is plausibly important for the crosstalk between Eph and integrin signalling pathways at the membrane protrusions and in the migration of brain cancer cells. PMID: 23686814
Increased expression of EFNA1 mRNA is associated with gastric cancer. PMID: 23065816
Expression of EPHRIN-A1 tends to be associated with worse survival in head and neck cancer. PMID: 24330498
EFNA1 expression is a useful marker for predicting high risk of relapse and cancer-related death in patients who have undergone curative resection for CRC. PMID: 23258614
Findings suggest that the glycosylation on ephrin-A1 plays a critical role in the binding and activation of the EphA2 receptor. PMID: 23661698
present study showed a high expression of EphA2/ephrinA1 in adenoid cystic carcinoma. EphA2/ephrinA1 can serve as a novel therapy target for adenoid cystic carcinoma. PMID: 23298804
EphA2 activation by ephrin-A1 induces tumor suppressor gene cdx-2 expression which attenuates cell proliferation, tumor growth and thus may be a promising therapeutic target against NSCLC. PMID: 22824143
in p-stage I NSCLC patients, those in the higher EphA2 expression and higher ephrin-A1 expression groups shared almost the same clinicopathological backgrounds which are generally considered to be better prognostic factors. PMID: 22236865
The EphA2 ligand EphrinA1 induces EphA2 phosphorylation and intracellular internalization and degradation, thus inhibiting breast tumor progression. PMID: 22228563
Multiple oncogenic signalling pathways are affected by ephrin-A1, from the promotion of a specific pathway in one cell or cancer type to the inhibition of the same pathway in another type of cell or cancer. [Review] PMID: 22040911
Ovarian serous carcinomas and ovarian cancer cell lines overexpress EphA2 and EphrinA-1. Tumor patients with higher expression levels of both EphA2 and EphrinA-1 have a significantly poorer clinical outcome. PMID: 21500549
The Eph-ephrinA system can promote cell attachment along with intercellular dissociation. PMID: 21349856
This study demonstrated that the Eph-ephrin A system can promote intercellular dissociation in Ishikawa cells suggesting an important role in the initial step of embryo implantation by opening the endometrial epithelial cell barrier. PMID: 21138904
Osteosarcoma samples were characterized using genome-wide microarrays: increased expression of the EphA2 receptor and its ligand EFNA1 was detected. PMID: 21166698
up-regulation of EphA2 and down-regulation of Ephrina1 may correlate with poor prognosis for patients with high-grade glioma PMID: 20571968
EphA2 and EphrinA1 are highly expressed in renal cell carcinoma, and positively correlated with histological differentiation, clinical stage and angiogenesis. PMID: 19950554
EFNA1 may be a useful serum marker for the detection of hepatocellular carinoma development and progression. PMID: 19642143
The interaction between EphA2 and this ligand protein is necessary for induction of maximal neovascularization by VEGF. PMID: 12496364
This protein, an EphA ligand, stimulated protein degradation by EphA2. PMID: 12496371
Ephrin-A1 stimulation of Jurkat T cells induces tyrosine phosphorylation of EphA3 receptors and cytoplasmic proteins, including c-cbl proto-oncogene, and causes down-regulation of endogenous EphA3 receptors from the cell surface and their degradation. PMID: 12794130
A new ephrin-A1 isoform, ephrin-A1b, lacks a segment of 22 amino acids (residues 131-152). Exon 3 is spliced out in its transcript. It may regulate the function of its ephrin-A1a counterpart. PMID: 14692877
This study demonstrates for the first time significantly reduced ephrin-A1 expression in T cells of asthma patients. PMID: 14707054
found ephrin-A1 expressed exclusively in the invasive extravillous trophoblast in preeclampsia and normal placenta PMID: 15193868
ephrin-A1 is expressed by venule endothelial cells PMID: 15585656
EPHA2 and EFNA1 expression may influence the behavior of human gastric cancer. PMID: 15649254
low molecular weight protein-tyrosine phosphatase acts as terminator of EphA2 signaling causing efficient negative feedback loop on biological response mediated by ephrinA1; tyrosine phosphorylation main event orchestrating repulsive response PMID: 16051609
High expression of Ephrin A-1 is associated with urinary bladder carcinoma. PMID: 16428472
Activation of ERK-1/2 plays an essential role in ephrin-A1-mediated cell migration, whixh is inhibited by green tea catechin epigallocatechin gallate. PMID: 17049832
Ephrin-A1 serves as a critical negative regulator in the tumorigenesis of gliomas by down-regulating EphA2 and FAK. PMID: 17332925
Increasing ephrin-A expression enhances T-cell interactions not only with purified integrin ligands but also endothelial cells, while EphA activation down-regulates these interactions. PMID: 17980912
Soluble monmomeric EphrinA1 is released from tumor cells and is a functional ligand for the EphA2 receptor. PMID: 18794797
The function of EphA2 and ephrinA1 in tumorigenesis and tumor progression is complex and seems to be dependent on cell type and microenvironment PMID: 19074825
Increased expression of EphA2 and EphrinA-1 plays an important role in the progression human gastric adenocarcinoma. PMID: 19101799
The crystal structures of an A-class complex between EphA2 and ephrin-A1 and of unbound EphA2, are presented. PMID: 19525919

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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.

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