Recombinant Human EphA7 Fc Chimera Protein, CF
Recombinant Human EphA7 Fc Chimera Protein, CF Summary
When Recombinant Human (rh) EphA7 Fc Chimera is coated at 2 μg/mL (100 μL/well), the concentration of biotinylayed rhEphrin-A4 Fc Chimera that produces 50% of the optimal binding response is found to be approximately 1.5 ‑ 6 ng/mL.
(Met1 - Val555)
Accession # NP_004431
(Pro100 - Lys330)
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 100 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
EphA7, also known as Mdk1, Hek11, Ehk3, Ebk, and Cek11, is a 115 ‑ 120 kDa glycosylated member of the Eph family of transmembrane receptor tyrosine kinases (1, 2). The A and B classes of Eph proteins are distinguished by Ephrin ligand binding preference but have a common structural organization. EphA7 preferentially binds to and is activated by Ephrin‑A1, ‑A2, ‑A3, ‑A4, and ‑A5 (3 ‑ 6). Eph‑Ephrin interactions are widely involved in the regulation of cell migration, tissue morphogenesis, and cancer progression. The 532 amino acid (aa) extracellular domain (ECD) of human EphA7 contains an N‑terminal Ephrin binding region, a cysteine‑rich region, and two fibronectin type III domains (FnIII). The 421 aa cytoplasmic domain contains the tyrosine kinase domain and a sterile alpha motif (SAM) (7). Within the ECD, human EphA7 shares 98% aa sequence identity with mouse and rat EphA7. Alternate splicing generates secreted isoforms of human EphA7 that are truncated either before or following the first FnIII domain (7, 8). In mouse, EphA7 is expressed in discrete regions of the developing and adult neocortex (4, 9 ‑ 12), Purkinje layer of the cerebellum (10), limbic system (4, 9, 11, 12), visual and auditory systems (10, 11, 13), and the peripheral sensory nervous system (10, 11). EphA7 functions as a repulsive guidance molecule during the targeting of retinal axons to the superior colliculus and of neocortical axons to the thalamus (4, 9, 13). EphA7 is also expressed in mesenchymal cells along routes of axon innervation during limb development (14). EphA7 ligands are expressed in a complementary pattern during embryogenesis (3, 9, 13, 14). EphA7 is selectively expressed in early stages of the B cell lineage, and a 50 kDa secreted form is produced by mature peripheral B and T cells (6, 15). This isoform is also expressed in human lung carcinoma (8). EphA7 can be up or down‑regulated in a variety of human cancers (6, 16, 17).
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Citation for Recombinant Human EphA7 Fc Chimera Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
Ephrin receptor A10 monoclonal antibodies and the derived chimeric antigen receptor T cells exert an antitumor response in mouse models of triple-negative breast cancer
Authors: JH Cha, LC Chan, YN Wang, YY Chu, CH Wang, HH Lee, W Xia, WC Shyu, SP Liu, J Yao, CW Chang, FR Cheng, J Liu, SO Lim, JL Hsu, WH Yang, GN Hortobagyi, C Lin, L Yang, D Yu, LB Jeng, MC Hung
The Journal of Biological Chemistry, 2022-03-10;0(0):101817.
Sample Types: Protein
Applications: ELISA Capture
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