Rat EFNB1 / Ephrin-B1 Protein (His Tag)

Produkt-Information von EFNB1 / Ephrin-B1 Protein

QC Testing von EFNB1 / Ephrin-B1 Protein

Purity	> 95 % as determined by SDS-PAGE	SDS-PAGE: EFNB1 / Ephrin-B1 protein
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	Ala 25
Molecular Mass	The recombinant rat EFNB1 comprises 216 amino acids and predicts a molecular mass of 23.8 kDa. The apparent molecular mass of the ratEFNB1 is approximately 36 kDa in SDS-PAGE under reducing conditions due to glycosylation.
Formulation	Lyophilized from 0.2μm filtered solution of PBS, pH7.5 Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.

EFNB1 / Ephrin-B1 Protein Usage Guide

Verwandte Produkte & Themen von EFNB1 / Ephrin-B1 Protein

Neuroscience>>Axon Guidance>>Ephrin & Eph Receptor>>Ephrin-B1/EFNB1

Cancer>>Growth Factor & Receptor>>Ephrin & Eph Receptor>>Ephrin-B1/EFNB1

Beschreibung von EFNB1 / Ephrin-B1 Protein

The ephrins (Eph) and Eph receptors comprise the largest subfamily of receptor protein-tyrosine kinases and have been implicated in 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 glycosylphosphatidylinositol 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. In?molecular biology, ephrins and Eph receptors are components of cell signaling pathways involved in animal development, and implicated in some cancers. Mouse ephrin-B1, also known as LERK-2, ELK-L, EFL-3, Cek5-L, and STRA-1, is a member of the ephrin ligand family which binds members of the Eph receptor family. Ephrin-B1 has been shown to bind EphA3, EphB1, EphB2, EphB3, and EphB4. The extracellular domains of human and mouse ephrin-B1 share 94% amino acid identity.

References

1. Cerretti DP. et al., 1995, Mol Immunol. 32 (16): 1197-205.
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 (14): 2823-32.

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