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- Regulatory Status
- RUO
- Other Names
- Ephrin B1, EFNB1, Eph-Related Receptor Tyrosine Kinase Ligand 2, ELK ligand, EPLG2, LERK2, EFL3
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- Product Citations
- publications
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Immobilized recombinant human Ephrin-B1 binds recombinant human EphB2-Fc Chimera in a dose-dependent manner with an EC50 range of 50 - 200 ng/mL. -
Stability Testing for Recombinant Human Ephrin-B1. Recombinant human Ephrin-B1 was aliquoted in PBS at 0.2 mg/mL. One aliquot was frozen and thawed four times (4x Freeze/Thaw), and compared to a control kept at 4°C (Control). The samples were tested in a binding assay with recombinant human EphB2-Fc Chimera.
Ephrins are cell surface molecules with a wide variety of biological functions since they are expressed on nearly every tissue of a developing embryo while also persisting throughout adulthood. The Ephrin family of ligands consists of five GPI-linked members (Ephrin-A1 through A5) in addition to three transmembrane proteins (Ephrin-B1 through B3). The interaction between Ephrin ligands and their Eph receptors generates bidirectional signaling, affecting both receptor and ligand expressing cells, and contributes greatly to the regulation of neural crest migration, growth cone development, and cancer progression. Mature Ephrin-B1 consists of a 210 amino acid extracellular domain (EDC), a 21 amino acid transmembrane segment, and an 88 amino acid cytoplasmic domain. Ephrin-B1's involvement in the developing nervous system predominantly arises from modulating presynaptic development, axon guidance, and the migration of cells. It also plays a role in the developed nervous system by restricting new synapse formation in the adult hippocampus through Ephrin-B1 expressing astrocytes, thus influencing long-term contextual memory. It is overexpressed in atherosclerotic tissue in addition to T lymphocytes and macrophages in monocytes and plaques. As a substrate for presenilin-dependent gamma-secretase transmembrane cleavage, Ephrin-B1 regulates cytoskeletal dynamics via intramembrane proteolysis. Furthermore, it is required for proper cardiac tissue cohesion by interacting with the claudin-5/ZO-1 complex on the lateral membrane of cardiomyocytes. Ephrin-B1 also mediates cell-cell adhesion through an Eph receptor mechanism of not only epithelial but also cancer cells. Abnormal Ephrin-B1 expression has been characterized in the secretion and invasion of cancer cells, namely prostate, by regulating the activation of metalloproteinase-8 via increased GTP-bound ARF1 GTPase.
Product DetailsProduct Details
- Source
- Human Ephrin-B1, amino acid Leu28-Ser236 (Accession # P98172) with C-terminal 6His tag was expressed in 293E cells.
- Molecular Mass
- The 218 amino acid recombinant protein has a predicted molecular mass of approximately 23.9 kD. The DTT-reduced and the non-reduced protein migrates at approximately 31 kD by SDS-PAGE. The predicted N-terminal amino acid is Leu.
- Purity
- >95%, as determined by Coomassie stained SDS-PAGE.
- Formulation
- 0.22 µm filtered protein solution is in PBS, pH 7.4
- Endotoxin Level
- Less than 0.1 EU per µg protein as determined by the LAL method.
- Concentration
- 10 and 25 µg sizes are bottled at 200 µg/mL. 100 µg size and larger sizes are lot-specific and bottled at the concentration indicated on the vial. To obtain lot-specific concentration and expiration, please enter the lot number in our Certificate of Analysis online tool.
- Storage & Handling
- Unopened vial can be stored between 2°C and 8°C for up to 2 weeks, at -20°C for up to six months, or at -70°C or colder until the expiration date. For maximum results, quick spin vial prior to opening. The protein can be aliquoted and stored at -20°C or colder. Stock solutions can also be prepared at 50 - 100 µg/mL in appropriate sterile buffer, carrier protein such as 0.2 - 1% BSA or HSA can be added when preparing the stock solution. Aliquots can be stored between 2°C and 8°C for up to one week and stored at -20°C or colder for up to 3 months. Avoid repeated freeze/thaw cycles.
- Activity
- When recombinant human Ephrin-B1 is immobilized at 2 µg/mL, recombinant human EphB2-Fc Chimera binds in a dose-dependent manner. The EC50 range for this effect is 50 - 200 ng/mL. HRP Protein A (Cat. No. 689202) was used to detect the binding.
- Application
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Bioassay
- Application Notes
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BioLegend carrier-free recombinant proteins provided in liquid format are shipped on blue ice. Our comparison testing data indicates that when handled and stored as recommended, the liquid format has equal or better stability and shelf-life compared to commercially available lyophilized proteins after reconstitution. Our liquid proteins are verified in-house to maintain activity after shipping on blue ice and are backed by our 100% satisfaction guarantee. If you have any concerns, contact us at tech@biolegend.com.
Antigen Details
- Structure
- Monomer
- Distribution
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Ephrin-B1 is expressed on glomerular podocyte slit diaphragms, developing thymocytes, peripheral T cells, monocytes, macrophages, vascular endothelial cells, cardiomyocytes, osteoclasts, and luteinizing granulosa cells in the ovary
- Function
- Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development.
- Interaction
- Neurons, Endothelial cells
- Ligand/Receptor
- EphB1, EphB2, EphB3
- Bioactivity
- Measured by its ability to bind recombinant human EphB2
- Biology Area
- Cell Biology, Neuroscience, Synaptic Biology
- Antigen References
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- Pasquale EB. 2008. Cell. 133:38-52.
- Tanaka M, et al. 2005. EMBO J. 24:3700-11.
- Wilkinson DG. 2001. Nat Rev Neurosci. 2:155-64.
- Wang Y, et al. 2010. Nature. 465:483-6.
- Tomita T, et al. 2006. Mol. Neurodegener. 1:2.
- Genet G, et al. 2012. Circ. Res. 110: 688-700.
- Sakamoto A, et al. 2008. Clin. Sci. 114:643-50.
- Iwasaki K, et al. 2018. Cancer Sci. 109:3159-3170.
- Koeppen J, et al. 2018. J Neurosci. 38:5710.
- Gene ID
- 1947 View all products for this Gene ID
- UniProt
- View information about Ephrin-B1 on UniProt.org
Related FAQs
- Why choose BioLegend recombinant proteins?
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• Each lot of product is quality-tested for bioactivity as indicated on the data sheet.
• Greater than 95% Purity or higher, tested on every lot of product.
• 100% Satisfaction Guarantee for quality performance, stability, and consistency.
• Ready-to-use liquid format saves time and reduces challenges associated with reconstitution.
• Bulk and customization available. Contact us.
• Learn more about our Recombinant Proteins. - How does the activity of your recombinant proteins compare to competitors?
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We quality control each and every lot of recombinant protein. Not only do we check its bioactivity, but we also compare it against other commercially available recombinant proteins. We make sure each recombinant protein’s activity is at least as good as or better than the competition’s. In order to provide you with the best possible product, we ensure that our testing process is rigorous and thorough. If you’re curious and eager to make the switch to BioLegend recombinants, contact your sales representative today!
- What is the specific activity or ED50 of my recombinant protein?
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The specific activity range of the protein is indicated on the product datasheets. Because the exact activity values on a per unit basis can largely fluctuate depending on a number of factors, including the nature of the assay, cell density, age of cells/passage number, culture media used, and end user technique, the specific activity is best defined as a range and we guarantee the specific activity of all our lots will be within the range indicated on the datasheet. Please note this only applies to recombinants labeled for use in bioassays. ELISA standard recombinant proteins are not recommended for bioassay usage as they are not tested for these applications.
- Have your recombinants been tested for stability?
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Our testing shows that the recombinant proteins are able to withstand room temperature for a week without losing activity. In addition the recombinant proteins were also found to withstand four cycles of freeze and thaw without losing activity.
- Does specific activity of a recombinant protein vary between lots?
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Specific activity will vary for each lot and for the type of experiment that is done to validate it, but all passed lots will have activity within the established ED50 range for the product and we guarantee that our products will have lot-to-lot consistency. Please conduct an experiment-specific validation to find the optimal ED50 for your system.
- How do you convert activity as an ED50 in ng/ml to a specific activity in Units/mg?
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Use formula Specific activity (Units/mg) = 10^6/ ED50 (ng/mL)
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