Recombinant Human EphB1 Protein (aa 565-984, His & GST Tag)

Beta LifeScience SKU/CAT #: BLPSN-1824

Recombinant Human EphB1 Protein (aa 565-984, His & GST Tag)

Beta LifeScience SKU/CAT #: BLPSN-1824
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Product Overview

Tag His&GST
Host Species Human
Accession AAI11745.1
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 (AAI11745.1) (Arg565-Ala984) was fused with the N-terminal His-tagged GST tag at the N-terminus.
Source Baculovirus-Insect Cells
Predicted N Terminal Met
AA Sequence Arg565-Ala984
Molecular Weight The recombinant human EPHB1 /GST chimera consists of 657 a.a. and has a calculated molecular mass of 75.3 kDa. The recombinant protein migrates as an approximately 66 kDa band 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 The specific activity was determined to be 140 nmol/min/mg using Poly(Glu:Tyr) 4:1 as substrate.
Formulation Supplied as sterile 20mM Tris, 500mM NaCl, 3mM DTT, pH 8.0, 10% gly.
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
Tissue Specificity Preferentially expressed in brain.

Gene Functions References

  1. SUMOylation of EphB1 repressed activation of its downstream signaling molecule PKC-gamma, and consequently inhibited neuroblastoma tumorigenesis. PMID: 29550816
  2. 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
  3. some of the mutations found in EPHB1 may contribute to an increased invasive capacity of cancers. PMID: 28108514
  4. Association of EPHB1 rs11918092 with symptoms of schizophrenia in Chinese Zhuang and Han populations. PMID: 27028544
  5. 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
  6. 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
  7. Our results indicate that EphB1 may be involved in carcinogenesis of renal cell carcinoma PMID: 25120806
  8. The genes CD248, Ephb1 and P2RY2 were detected as the top overexpressed in GC biopsies. PMID: 24716914
  9. The study presents the first structure of the EphB1 tyrosine kinase domain determined by X-ray crystallography to 2.5A. PMID: 24677421
  10. 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
  11. Our data indicate that loss of EphB1 protein is associated with metastasis and poorer survival in patients with serous ovarian cancer PMID: 24427352
  12. Low EphB1 expression is associated with glioma. PMID: 24121831
  13. EphB1 stimulation triggered approximately 50% serine-threonine PTEN dephosphorylation and PTEN-Cbl complex disruption, a process requiring PTEN protein phosphatase activity. PMID: 23118026
  14. No association is found for EPH receptor B1 and susceptibility to schizophrenia. PMID: 21041834
  15. EPHB1 polymorphisms may be associated with susceptibility to hepatocellular carcinoma in the Korean population. PMID: 21763378
  16. Data show that EphB receptors interact with E-cadherin and with the metalloproteinase ADAM10 at sites of adhesion. PMID: 21804545
  17. analysis of EphB1, EphB2, and EphB4-binding peptides interaction with antagonists with ephrin-like affinity PMID: 15722342
  18. The ubiquitin ligase Cbl induces the ubiquitination and lysosomal degradation of activated EphB1, a process requiring EphB1 and Src kinase activity. PMID: 18034775
  19. Transgenic EphB1 and ephrin-B3 cooperatively regulate the proliferation and migration of neural progenitors in the hippocampus. PMID: 18057206
  20. Loss of expression of EphB1 protein in gastric carcinoma is associated with invasion and metastasis PMID: 18424888
  21. EphB1 may have roles in the pathogenesis and development of colorectal cancer. PMID: 18931529

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.

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