EFNB2 / EphrinB2 Protein (His Tag)

EFNB2 / EphrinB2 Protein

EFNB2 / EphrinB2 Protein Product Information

• Synonym: EFNB2,RP11-272L14.1, EPLG5, HTKL, Htk-L, LERK5, MGC126226, MGC126227, MGC126228
• Protein Construction: A DNA sequence encoding the human EFNB2 ( NP_004084.1 ) extracellular domain ( Met 1 - Ala 229) was expressed, fused with a C-terminal polyhistidine tag
• Source: Human
• Expression Host: Human Cells

EFNB2 / EphrinB2 Protein QC Testing

• Purity: > 97 % as determined by SDS-PAGE
• Bio-activity: Measured by its binding ability in a functional ELISA
  Immobilized human EFNB2 at 2 μg/ml ( 100 μl/well ) can bind human EphB4 with a linear ranger of 1.56 - 12.5 ng/ml
• 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: Ile 28
• Molecular Mass: The recombinant human EFNB2 consists of 213 amino acids after removal of the signal peptide and predicts a molecular mass of 23.6 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rh EFNB2 is approximately 35 - 40 kDa due to glycosylation
• Formulation: Lyophilized from sterile PBS , pH 7.4
  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: EphrinB2 protein

EFNB2 / EphrinB2 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.

EFNB2 / EphrinB2 Protein Description

The ephrins (Eph) and Eph receptors comprise the largest subfamily of receptor protein-tyrosine kinases and have been implicated in mediating developmental events, especially in the nervous system and in erythropoiesis. Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosyl- phosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. All ephrins share a conserved extracellular sequence, which most likely corresponds to the receptor-binding domain. This conserved sequence consists of approximately 125 amino acids and includes four invariant cysteines. The cytoplasmic domains are approximately 80 amino acids long and are highly conserved, especially the last 33 amino acids. In molecular biology, ephrins and Eph receptors are components of cell signaling pathways involved in animal development, and implicated in some cancers. Eph receptors are classified as receptor tyrosine kinases (RTKs), and form the largest sub-family of RTKs. Almost all Eph receptors are expressed during various well defined stages of development in assorted locations and concentrations. Ephrin-B2 is a member of the ephrin ligand family, which binds members of the Eph receptor family. It has been shown to bind EphA4, EphB1, EphB2, EphB3, and EphB4. Ephrin-B2 plays a role in a variety of developmental processes, including arterial-venous differentiation, neural crest cell migration, and axon guidance.

References

1. Cerretti, D.P. et al., 1995, Mol. Immunol. 32 (16): 1197-1205.
2. Gale, NW. et al.,1996, Neuron.17 (1): 9-19.
3. Flanagan, J. et al., 1998, Annual Review of Neuroscience. 21: 309-45.
4. Holder, N. et al., 1999,  Development. 126 (10): 2033-44.
5. Wilkinson, DG. et al., 2001, Nat. Rev. Neurosci. 2 (3): 155-64. 
6. Murai, KK. et al., 2003, Journal of Cell Science. 116: 2823-32.