Cynomolgus EFNA5 / Ephrin-A5 Protein (His Tag)

Ephrin A5 Protein Datasheet

EFNA5 / Ephrin-A5 Protein Product Information

• Synonym: EFNA5
• Protein Construction: A DNA sequence encoding the Cynomolgus EFNA5 (F7GZC7) (Met1-Asn203) was expressed, fused with a polyhistidine tag at the C-terminus.
• Source: Cynomolgus
• Expression Host: Human Cells

EFNA5 / Ephrin-A5 Protein QC Testing

• Purity: > 90 % as determined by SDS-PAGE
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: Ser 20
• Molecular Mass: The recombinant Cynomolgus EFNA5 is a disulfide-linked homodimer. The reduced monomer comprises 194 amino acids and has a calculated molecular mass of 22.6 KDa. The apparent molecular mass of it is approximately 28 KDa respectively in SDS-PAGE.
• Formulation: Lyophilized from sterile PBS, pH7.4.
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.
• SDS-PAGE: EFNA5 / Ephrin-A5 protein

EFNA5 / Ephrin-A5 Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

EFNA5 / Ephrin-A5 Protein Description

Ephrin-A5, also known as AL-1, RAGS, or LERK-7 ( ligand for eph-related kinases, 7 ), is a member of the ephrin ligand family which binds the members of Eph receptor subfamily of tyrosine kinases. Based on their structure and sequence relationships, ephrins are divided into ephrin-A and ephrin-B class, and ephrin-A members are anchored to the membrane by GPI linkage. Ephrin-A5 is expressed with the highest levels in human adult brain, heart, spleen, and ovary and human fetal brain, lung, and kidney. This ligand has been reported to bind Eph A2, Eph A3, Eph A4, Eph A5, Eph A6, Eph A7, Eph A8, and Eph B2 receptors. The interactions between Eph receptors and their ephrin ligands have been implicated in mediating developmental events, particularly in the nervous system through regulating cell migration and axon pathfinding. It has been reported that Ephrin-A5 prevents axon bundling in cocultures of cortical neurons with astrocytes, a model of late stage nervous system development and differentiation. The ephrins (EPH) and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases (RTKs), and have been involved in a variety of biological processes, especially in the nervous system and in erythropoiesis, such as axon guidance and topographic map formation, synaptic plasticity, angiogenesis, and meanwhile have possible contributions to tumor growth and metastasis. Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class which are anchored to the membrane by a GPI linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. 14 receptors and 8 ligands have been reported in mammals.

References

1. Stein E. et al., 1999, J Neurosci. 19: 8885-93.
2. Wilkinson DG. 2001, Nat Rev Neurosci. 2: 155-164.
3. Cheng N. et al., 2002, Cytokine Growth Factor Rev. 13: 75-85.
4. Himanen JP. et al., 2004, Nat Neurosci. 7: 501-9.
5. Eberhart J. et al., 2004, J Neurosci. 24: 1070-8.
6. Irie F. et al., 2008, Proc Nat Acad Sci. 105: 12307-12.