Ephrin-A5 (Efna5) Recombinant Protein | Efna5 recombinant protein

Recombinant Mouse Ephrin-A5 (Efna5)

Cat. Num. AAA1147694

• Gene Names: Efna5; AL-1; Epl7; RAGS; EFL-5; LERK-7; AV158822; Ephrin-A5
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Ephrin-A5 (Efna5); Recombinant Mouse Ephrin-A5 (Efna5); Efna5 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 21-203, Full length protein
• Sequence: QDPGSKVVADRYAVYWNSSNPRFQRGDYHIDVCINDYLDVFCPHYEDSVPEDKTERYVLYMVNFDGYSACDHTSKGFKRWECNRPHSPNGPLKFSEKFQLFTPFSLGFEFRPGREYFYISSAIPDNGRRSCLKLKVFVRPTNSCMKTIGVHDRVFDVNDKVENSLEPADDTVHESAEPSRGEN
• Sequence Length: 183

• Species: Mouse
• Preparation and Storage: Store at -20 degrees C. For long-term storage, store at -20 degrees C or -80 degrees C. Store working aliquots at 4 degrees C for up to one week. Repeated freezing and thawing is not recommended.

Related Product Information for Efna5 recombinant protein

Ephrin-A5, a member of the ephrin gene family, prevents axon bundling in cocultures of cortical neurons with astrocytes, a model of late stage nervous system development and differentiation. The EPH and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and have been implicated in mediating developmental events, particularly in the nervous system. EPH receptors typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin ligands and receptors have been named by the Eph Nomenclature Committee (1997). 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. The Eph family of receptors are similarly divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands.

NCBI and Uniprot Product Information

• NCBI GI #: 6753724
• NCBI GeneID: 13640
• NCBI Accession #: NP_034239.1
• NCBI GenBank Nucleotide #: NM_010109.3
• UniProt Accession #: O08543; O08544
• Molecular Weight: 23,338 Da
• NCBI Official Full Name: ephrin-A5 isoform 2
• NCBI Official Synonym Full Names: ephrin A5
• NCBI Official Symbol: Efna5
• NCBI Official Synonym Symbols: AL-1; Epl7; RAGS; EFL-5; LERK-7; AV158822; Ephrin-A5
• NCBI Protein Information: ephrin-A5
• UniProt Protein Name: Ephrin-A5
• Protein Family: Ephrin
• UniProt Gene Name: Efna5
• UniProt Synonym Gene Names: Epl7; Eplg7; Lerk7; LERK-7

Uniprot Description

Cell surface GPI-bound 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. Induces compartmentalized signaling within a caveolae-like membrane microdomain when bound to the extracellular domain of its cognate receptor. This signaling event requires the activity of the Fyn tyrosine kinase. Activates the EPHA3 receptor to regulate cell-cell adhesion and cytoskeletal organization. With the receptor EPHA2 may regulate lens fiber cells shape and interactions and be important for lens transparency maintenance. May function actively to stimulate axon fasciculation. The interaction of EFNA5 with EPHA5 also mediates communication between pancreatic islet cells to regulate glucose-stimulated insulin secretion. Cognate/functional ligand for EPHA7, their interaction regulates brain development modulating cell-cell adhesion and repulsion.