Recombinant Mouse Ephrin-B3 (EFNB3) Protein (His)

Name: Recombinant Mouse Ephrin-B3 (EFNB3) Protein (His)
Brand: Beta LifeScience
SKU: BLC-10721P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse Ephrin-B3 (EFNB3) Protein (His) is produced by our E.coli expression system. This is a extracellular protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O35393
Target Symbol	EFNB3
Synonyms	Efnb3Ephrin-B3
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	LSLEPVYWNSANKRFQAEGGYVLYPQIGDRLDLLCPRARPPGPHSSPSYEFYKLYLVEGAQGRRCEAPPAPNLLLTCDRPDLDLRFTIKFQEYSPNLWGHEFRSHHDYYIIATSDGTREGLESLQGGVCLTRGMKVLLRVGQSPRGGAVPRKPVSEMPMERDRGAAHSAEPGRDTIPGDPSSNATSRGAEGPLPPPSMPA
Expression Range	28-227aa
Protein Length	Extracellular Domain
Mol. Weight	26.0kDa
Research Area	Others
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.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
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	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. Binds promiscuously Eph receptors 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. May play a pivotal role in forebrain function. Binds to, and induce the collapse of, commissural axons/growth cones in vitro. May play a role in constraining the orientation of longitudinally projecting axons.
Subcellular Location	Membrane; Single-pass type I membrane protein.
Protein Families	Ephrin family
Database References	KEGG: mmu:13643 STRING: 10090.ENSMUSP00000004036 UniGene: PMID: 29901151 Data suggest that molecules in the erythropoietin-producing hepatocellular receptor B family (EPHB) / ephrinB (EFNB) signalling pathways, specifically ephrin B3 and GRIP1, are involved blood pressure regulation. PMID: 27941904 ephrin B3/EphB2 are obvious candidates for driving the Syk-dependent repulsive response. PMID: 27122172 The Eph/ephrin-B3-mediated heterotypic or homotypic cell interactions between thymocytes and thymic epithelial cells (TECs), or between TECs and themselves, contribute to the early maturation of MTS20(+) TECs. PMID: 27060907 Findings suggest that EphrinB3 may be a relevant target for promoting remyelination in demyelinating disease PMID: 26687980 The morphological and behavioural abnormalities in ephrin-B3 mutant mice are rescued by conditional knock-in of wild-type ephrin-B3 during the critical period when axon targeting and fear responses are initiated. PMID: 27008987 Ephrin-B3 knockout mice had significantly reduced pre-pulse inhibition compared with controls. PMID: 24949848 Conclude that EphB3 mediates cell death in the adult cortex through a novel dependence receptor-mediated cell death mechanism in the injured adult cortex and is attenuated following ephrinB3 stimulation. PMID: 24810043 findings indicate that a single guidance system, ephrinB3/EphA4, controls the formation of ascending and descending longitudinal axons in the spinal cord. PMID: 24360544 these data introduce EphB3 as a new biomarker to identify beta-cells at a critical step during their step-wise differentiation and define the timeframe of endocrine differentiation. PMID: 22434763 Induction of experimental stroke results in enhanced cell proliferation and neuronal differentiation around the lesion site of ephrin-B3-deficient compared to ephrin-B3-expressing mice. PMID: 21779764 EphrinB3 contributes to myelin-derived axonal growth inhibition and limits recovery from adult central nervous system trauma. PMID: 22411787 cell contact-mediated bidirectional ephrinB3/EphA4 signaling mediates the sorting of medial ganglionic eminence- and preoptic area-derived interneurons in the deep and superficial migratory stream. PMID: 22171039 This study demonistrated tht ephrin-B reverse signaling into three distinct intracellular pathways and protein-protein interactions that mediate the maturation of postsynaptic neurons. PMID: 21964490 These studies support an anti-proliferative role for EphB3 in regulating neural stem/progenitor cell numbers in the developing subventricular zone. PMID: 20969945 found that ablation of ephrin-B3 results in an enhancement of the NMDA receptor component of synaptic transmission relative to the AMPA receptor component in CA1 synapses PMID: 20678574 Ephrinb3 is directly involved in the specificity of mesostriatal projection. PMID: 20719236 conclude that ephrinB3-induced EphA4 signaling repels some components of the mammalian spinal central pattern generators (CPG) and restricts their axonal projections to one side of the spinal cord PMID: 12649481 Organ of Corti and spiral ganglion showed strong expression of ephrin-A3, ephrin-B2 and ephrin-B3. PMID: 12684176 EFNB3-Fc in the presence of suboptimal anti-CD3 crosslinking enhanced T-cell responses in terms of proliferation, activation marker expression, interferon-gamma but not interleukin-2 production, and cytotoxic T-cell activity PMID: 13679370 Ephrin-B3 is a myelin-based inhibitor of neurite outgrowth. PMID: 16020529 May act like a receptor by transducing reverse signals in order to regulate the number of synapses formed in the hippocampus. May stimulate forward signaling to modulate a number of other proteins involved in synaptic activity, learning, and memory. PMID: 16466709 Data show that ephrinB3 contributes to the control of cell proliferation and survival in the adult subventricular zone. PMID: 16483793 Novel mechanism for independent modulation of shaft synapses through ephrinB3 reverse signaling. PMID: 17626212 Rac-GAP alpha-chimerin regulates motor-circuit formation as a key mediator of Efnb3 forward signaling. PMID: 17719550 A previously unknown pathway is revealed that controls axon pruning by which ephrin-B3 reverse signals regulate actin dynamics to bring about the retraction of growth cones. PMID: 19182796

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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.