Ephrin B2 Protein (EFNB2) (Soluble) (His tag)
-
- Target See all Ephrin B2 (EFNB2) Proteins
- Ephrin B2 (EFNB2)
- Protein Type
- Recombinant
- Protein Characteristics
- Soluble
-
Origin
- Human
-
Source
- Escherichia coli (E. coli)
- Purification tag / Conjugate
- This Ephrin B2 protein is labelled with His tag.
- Purpose
- Ephrin-B2, soluble
- Sequence
- MIVLEPIYWN SSNSKFLPGQ GLVLYPQIGD KLDIICPKVD SKTVGQYEYY KVYMVDKDQA DRCTIKKENT PLLNCAKPDQ DIKFTIKFQE FSPNLWGLEF QKNKDYYIIS TSNGSLEGLD NQEGGVCQTR AMKILMKVGQ DASSAGSTRN KDPTRRPELE AGTNGRSSTT SPFVKPNPGS STDGNSAGHS GNNILGSEVA LFALEHHHHH H
- Characteristics
- Length (aa):211
- Purity
- > 95 % by SDS-PAGE
- Top Product
- Discover our top product EFNB2 Protein
-
Ephrin B2 (EFNB2) (AA 28-229) protein (Fc Tag)
EFNB2 Origin: Human Host: HEK-293 Cells Recombinant > 95 % as determined by Tris-Bis PAGE,> 95 % as determined by HPLC
Ephrin B2 (EFNB2) (AA 28-127) protein (GST tag)EFNB2 Origin: Human Host: Wheat germ Recombinant WB, ELISA, AA, AP
Ephrin B2 (EFNB2) protein (His tag,Fc Tag)EFNB2 Origin: Mouse Host: Human Cells Recombinant > 95 % as determined by SDS-PAGE
Ephrin B2 (EFNB2) (AA 1-333) protein (GST tag)EFNB2 Origin: Human Host: Wheat germ Recombinant WB, ELISA, AA, AP
-
- Restrictions
- For Research Use only
-
- Format
- Lyophilized
-
- Target
- Ephrin B2 (EFNB2)
- Alternative Name
- Ephrin-B2 (EFNB2 Products)
- Synonyms
- EFNB2 Protein, efnb2 Protein, ephrin-B2 Protein, htkl Protein, eplg5 Protein, htk-l Protein, lerk5 Protein, ephrinB2 Protein, efnb2a Protein, MGC68890 Protein, efnb2b Protein, ELF-2 Protein, Epl5 Protein, Eplg5 Protein, Htk-L Protein, LERK-5 Protein, Lerk5 Protein, NLERK-1 Protein, EPLG5 Protein, HTKL Protein, LERK5 Protein, ephrin B2 Protein, ephrin-B2 precursor Protein, ephrin B2 L homeolog Protein, ephrin B2 S homeolog Protein, EFNB2 Protein, efnb2 Protein, efnb2.L Protein, efnb2.S Protein, Efnb2 Protein
- Background
- EPH-related receptor tyrosine kinase ligand 5, HTK ligand,The large families of Eph receptor tyrosine kinases and their Ephrin ligands transduce signals in a cell-cell contact-dependent fashion. They thereby coordinate the growth, differentiation, and patterning of almost every organ and tissue. Eph/Ephrin interactions can trigger a wide array of cellular responses, including cell adhesion, boundary formation, and repulsion. The exact mechanisms leading to this diversity of responses are unclear but appear to involve differential signaling, proteolytic cleavage of Ephrins, and endocytosis of the ligand-receptor complex. In the developing cardiovascular system, Eph and Ephrin molecules control the angiogenic remodeling of blood vessels and lymphatic vessels and play essential roles in endothelial cells as well as in supporting pericytes and vascular smooth muscle cells. Recent evidence suggests that Ephs and Ephrins may also be involved in pathological angiogenesis, in particular, the neovascularization of tumors. Consequently, the expression, interactions, or signaling of Eph/Ephrin molecules might be targets for future therapeutic approaches. Ephrins are naturally divided into two structural groups. All ligands 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 B-class ligands are transmembrane proteins, which can be tyrosine phosphorylated upon receptor ligation. Class B ephrins show 33 % amino acid sequence identity in their extracellular segments and 44 % amino acid sequence identity in their cytoplasmic regions.
- Molecular Weight
- 23.4 kDa
- Gene ID
- 1948
- NCBI Accession
- NM_004093, NP_004084
- UniProt
- P52799
- Pathways
- RTK Signaling, Regulation of Muscle Cell Differentiation
-
