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Recombinant Biotinylated Human EphB4, ultra sensitivity (primary amine labeling), 25 µg  

Recombinant Biotinylated Human EphB4, ultra sensitivity (primary amine labeling), 25 µg

MABSol® Recombinant Biotinylated Human EphB4 Protein, expressed from human HEK293 cells, His Tag, ultra sensitivity (primary amine labeling)

Synonyms: recombinant, human, biotinylated, protein, EphB4, HTK, MYK1, TYRO11

More details

EP4-H8229-25

377,00 €

Background
Ephrin type-B receptor 4(EPHB4) is also known as HTK, MYK1 and TYRO11,is a member of Eph family. The Eph family of receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. Ephrin receptors make up the largest subgroup of the receptor tyrosine kinase (RTK) family. The protein encoded by EPHB4 binds to Ephrin-B2 and plays an essential role in vascular development. EPHB4 and its ligand ephrin-B2 are specifically expressed on venous and arterial endothelial cells, respectively, and play an essential role in vascular development via bidirectional signals. The forward EPHB4 signaling inhibits cell adhesion, chemotaxis, angiogenesis and tumor growth. Incontrast, the reverse Ephrin-B2 signaling exerts the opposite effect. It has been reported that aberrant expression of EPHB4 is associated with prostate cancer and highly malignant breast cancers, accordingly, EPHB4 has potential application as a therapeutic candidate.

The primary amine of rh EPHB4 was labeled by biotin without decreasing its bioactivity, and has been used successfully for easy detection in ELISA, dot blot or Western blot, immunohistochemistry applications using streptavidin or avidin-conjugated probes. Biotin and other reactive related chemicals have been removed thoroughly by desalting after reaction termination.

Source
Recombinant MABSol® Biotinylated Human EphB4, His Tag, primary amine labeling (EP4-H8229) is expressed from human HEK293 cells. It contains AA Leu 16 - Ala 539 (Accession # NP_004435.3). It is the biotinylated form of Human EphB4, His Tag (EP4-H5229).
Predicted N-terminus: Leu 16

Molecular Characterization
This protein carries a polyhistidine tag at the C-terminus.
The protein has a calculated MW of 57.9 kDa. The protein migrates as 62-75 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

Biotinylation
The primary amines in the side chains of lysine residues and the N-terminus of the protein are conjugated with biotins using standard chemical labeling method. A standard biotin reagent (13.5 angstroms) is used in this product.

Biotin:Protein Ratio

Passed as determined by the HABA assay / binding ELISA.

Endotoxin
Less than 1.0 EU per μg by the LAL method.

Purity
>97% as determined by SDS-PAGE.

Formulation
Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally trehalose is added as protectant before lyophilization.

Reconstitution
Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

Storage
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
-20°C to -70°C for 12 months in lyophilized state;
-70°C for 3 months under sterile conditions after reconstitution.

Clinical and Translational Updates

(1) "Capillary Malformation-Arteriovenous Malformation Syndrome Due to EPHB4 Gene Mutation: Clinical, Dermoscopic, Ecographic and Histopathological Features"
Setó-Torrent, Iglesias-Sancho, Altemir-Vidal et al
Indian J Dermatol (2022) 67 (3), 295-296
(2) "Adaptive activation of EFNB2/EPHB4 axis promotes post-metastatic growth of colorectal cancer liver metastases by LDLR-mediated cholesterol uptake"
Xu, Gu, Kuerbanjiang et al
Oncogene (2022)
(3) "Yi Shen Juan Bi Pill alleviates bone destruction in inflammatory arthritis under postmenopausal conditions by regulating ephrinB2 signaling"
Xu, Tao, Cao et al
Front Pharmacol (2022) 13, 1010640
Showing 1-3 of 799 papers.