Recombinant human EphA2 protein (EphA2-entrokinase-FC)
【No.】IRP010A | 【Protein name】 Recombinant human EphA2 protein |
【Gene Sequence Number/Expression Region】P29317/(24-537AA) | 【Label position】C-terminal Human-Fc Tag |
【Restriction sites】Enterokinase | 【Packing specification】100μg/tube |
EphA2 is a transmembrane tyrosine kinase receptor, a member of the tyrosine kinase receptor (RTKs) superfamily. Like other tyrosine kinases, the EphA2 molecule can be divided into three domains, the extracellular ligand binding domain, the intracellular tyrosine kinase active functional domain and the transmembrane domain. EphA2 is involved in the development of the nervous system and the development of the vascular system. Studies have shown that high expression of EphA2 can be found in breast cancer, colon cancer, prostate cancer, lung cancer, cervical cancer, ovarian cancer and other tissues. It is expected to be used as a treatment for malignant tumors. Targets and prognostic indicators. This product is EphA2-FC recombinant protein ( FC tag can be removed by enterokinase), which can be used for monoclonal antibody screening or antibody function verification.
Product name: Recombinant human EphA2 protein
Species: Human origin
Gene sequence number: P29317
Tags: Human-Fc Tag
Tag site : C terminal
Restriction site: enterokinase
Expression of region: extracellular domain ( 24 - 537 AA)
Host cell: CHO-S
Purity: > 90%
Purification method: Protein A column
Preservation system: PBS+20% glycerol
Storage conditions : -80℃
Illustration: Lane M on the left is the protein MW marker, Lane 1 is 10ug EphA2-Fc protein;
The right image shows the FACS detection of EphA2 protein binding to 293T overexpressing anti- EphA2- CAR.
Reference materials:
1. EphA2 Mediates Ligand-Dependent Inhibition and Ligand-Independent Promotion of Cell Migration and Invasion via a Reciprocal Regulatory Loop With Akt
2. EphA2 Is an Essential Mediator of UV Radiation-Induced Apoptosis
3. Activation of EphA2 Kinase Suppresses Integrin Function and Causes Focal-Adhesion-Kinase Dephosphorylation