Recombinant Human EphB1 Protein (His Tag)

Name: Recombinant Human EphB1 Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-1825
Availability: InStock

Collections: Enzymes, Kinase, Recombinant proteins

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Product Overview

Tag	His
Host Species	Human
Accession	P54762
Synonym	ELK, EPHT2, Hek6, NET
Background	Ephrin type-B receptor 1, also known as EphB1, belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family which 16 known receptors (14 found in mammals) are involved: EPHA1, EPHA2, EPHA3, EPHA4, EPHA5, EPHA6, EPHA7, EPHA8, EPHA9, EPHA1, EPHB1, EPHB2, EPHB3, EPHB4, EPHB5, EPHB6. EphB2 receptor tyrosine kinase phosphorylates syndecan-2 and that this phosphorylation event is crucial for syndecan-2 clustering and spine formation. The Eph family of receptor tyrosine kinases (comprising EphA and EphB receptors) has been implicated in synapse formation and the regulation of synaptic function and plasticity6. Ephrin receptors are components of cell signalling pathways involved in animal growth and development, forming the largest sub-family of receptor tyrosine kinases (RTKs). Ligand-mediated activation of Ephs induce various important downstream effects and Eph receptors have been studied for their potential roles in the development of cancer. EphB receptor tyrosine kinases are enriched at synapses, suggesting that these receptors play a role in synapse formation or function. We find that EphrinB binding to EphB induces a direct interaction of EphB with NMDA-type glutamate receptors. This interaction occurs at the cell surface and is mediated by the extracellular regions of the two receptors, but does not require the kinase activity of EphB.
Description	A DNA sequence encoding the human EPHB1 (P54762-1) extracellular domain (Met 1-Pro 540) was expressed, with a His tag at the C-terminus.
Source	HEK293
Predicted N Terminal	Met 18
AA Sequence	Met 1-Pro 540
Molecular Weight	The recombinant human EPHB1 consists of 534 a.a. and has a calculated molecular mass of 60 kDa as estimated in SDS-PAGE under reducing conditions.
Purity	>95% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Measured by its binding ability in a functional ELISA.1. Immobilized human EPHB1-His at 10 ug/ml (100 ul/well) can bind human EFNB1-Fc2h with a linear ranger of 3.125-200 ng/mL.2. Immobilized human EPHB1-His at 10 ug/ml (100 ul/well) can bind human EFNB2-Fch with a linear ranger of 0.3125-20 ng/mL.
Formulation	Lyophilized from sterile PBS, pH 7.4, 5% glycerol.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Cognate/functional ephrin ligands for this receptor include EFNB1, EFNB2 and EFNB3. During nervous system development, regulates retinal axon guidance redirecting ipsilaterally ventrotemporal retinal ganglion cells axons at the optic chiasm midline. This probably requires repulsive interaction with EFNB2. In the adult nervous system together with EFNB3, regulates chemotaxis, proliferation and polarity of the hippocampus neural progenitors. In addition to its role in axon guidance plays also an important redundant role with other ephrin-B receptors in development and maturation of dendritic spines and synapse formation. May also regulate angiogenesis. More generally, may play a role in targeted cell migration and adhesion. Upon activation by EFNB1 and probably other ephrin-B ligands activates the MAPK/ERK and the JNK signaling cascades to regulate cell migration and adhesion respectively. Involved in the maintenance of the pool of satellite cells (muscle stem cells) by promoting their self-renewal and reducing their activation and differentiation.
Subcellular Location	Cell membrane; Single-pass type I membrane protein. Early endosome membrane. Cell projection, dendrite.
Protein Families	Protein kinase superfamily, Tyr protein kinase family, Ephrin receptor subfamily
Database References	HGNC: 3392 OMIM: 600600 KEGG: hsa:2047 STRING: 9606.ENSP00000381097 UniGene: Hs.116092
Tissue Specificity	Preferentially expressed in brain.

Gene Functions References

SUMOylation of EphB1 repressed activation of its downstream signaling molecule PKC-gamma, and consequently inhibited neuroblastoma tumorigenesis. PMID: 29550816
investigate NET could modulate one's attention orientation to facial expressions, we categorized individuals according to the genotypes of the -182 T/C (rs2242446) polymorphism. Our results indicated that the -182 T/C polymorphism significantly modulated attention orientation to facial expressions, of which the CC genotype facilitated attention reorientation to the locations where cued faces were previously presented. PMID: 27541794
some of the mutations found in EPHB1 may contribute to an increased invasive capacity of cancers. PMID: 28108514
Association of EPHB1 rs11918092 with symptoms of schizophrenia in Chinese Zhuang and Han populations. PMID: 27028544
The tumor-suppressor function of EphB1 is clinically relevant across many malignancies, suggesting that EphB1 is an important regulator of common cancer cell transforming pathways. PMID: 25944917
In medulloblastoma cell lines, EphB1 downregulation or knockdown reduced cell growth, viability, cell-cycle regulator expression, and migration, but increased radiosensitivity and the percentage of cells in G1 phase of the cell cycle. PMID: 25879388
Our results indicate that EphB1 may be involved in carcinogenesis of renal cell carcinoma PMID: 25120806
The genes CD248, Ephb1 and P2RY2 were detected as the top overexpressed in GC biopsies. PMID: 24716914
The study presents the first structure of the EphB1 tyrosine kinase domain determined by X-ray crystallography to 2.5A. PMID: 24677421
EphB1 and Ephrin-B could be regarded as independent good prognostic factors and important biological markers for Squamous cell/adenosquamous carcinoma and adenocarcinoma of gallbladder. PMID: 24606480
Our data indicate that loss of EphB1 protein is associated with metastasis and poorer survival in patients with serous ovarian cancer PMID: 24427352
Low EphB1 expression is associated with glioma. PMID: 24121831
EphB1 stimulation triggered approximately 50% serine-threonine PTEN dephosphorylation and PTEN-Cbl complex disruption, a process requiring PTEN protein phosphatase activity. PMID: 23118026
No association is found for EPH receptor B1 and susceptibility to schizophrenia. PMID: 21041834
EPHB1 polymorphisms may be associated with susceptibility to hepatocellular carcinoma in the Korean population. PMID: 21763378
Data show that EphB receptors interact with E-cadherin and with the metalloproteinase ADAM10 at sites of adhesion. PMID: 21804545
analysis of EphB1, EphB2, and EphB4-binding peptides interaction with antagonists with ephrin-like affinity PMID: 15722342
The ubiquitin ligase Cbl induces the ubiquitination and lysosomal degradation of activated EphB1, a process requiring EphB1 and Src kinase activity. PMID: 18034775
Transgenic EphB1 and ephrin-B3 cooperatively regulate the proliferation and migration of neural progenitors in the hippocampus. PMID: 18057206
Loss of expression of EphB1 protein in gastric carcinoma is associated with invasion and metastasis PMID: 18424888
EphB1 may have roles in the pathogenesis and development of colorectal cancer. PMID: 18931529

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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.