Recombinant Human EFNA4 Protein (C-Fc-6His)

Beta LifeScience SKU/CAT #: BL-0496NP
BL-0496NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
BL-0496NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Recombinant Human EFNA4 Protein (C-Fc-6His)

Beta LifeScience SKU/CAT #: BL-0496NP
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Product Overview

Description Recombinant Human Ephrin-A4 is produced by our Mammalian expression system and the target gene encoding Leu26-Gly171 is expressed with a human IgG1 Fc, 6His tag at the C-terminus.
Accession P52798
Synonym Ephrin-A4; EPH-Related Receptor Tyrosine Kinase Ligand 4; LERK-4; EFNA4; EPLG4; LERK4
Gene Background Ephrin-A4 is a member of the ephrin ligand family which binds members of the Eph receptor family. All ligands share a conserved extracellular sequence, which most likely corresponds to the receptor binding domain. Ephrin-A4 consists of approximately 125 amino acids and includes four invariant cysteines, It has been shown to bind EphA2, EphA3, EphA4, EphA5, EphA6, EphA7, and EphB1. Ephrin-A4 binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. It may play a role in the interaction between activated B-lymphocytes and dendritic cells in tonsils.
Molecular Mass 44.3 KDa
Apmol Mass 45 KDa, reducing conditions
Formulation Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
Endotoxin Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity Biologically active. Please contact us to obtain bioactivity data.
Reconstitution Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage For Research Use Only

Target Details

Target Function 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. May play a role in the interaction between activated B-lymphocytes and dendritic cells in tonsils.
Subcellular Location [Isoform 1]: Cell membrane; Lipid-anchor, GPI-anchor.; [Isoform 2]: Secreted.
Protein Families Ephrin family
Database References
Tissue Specificity Expressed in the adult spleen, lymph node, prostate, ovary, small intestine, and colon, and in fetal heart, lung, liver and kidney. Also detected in hematopoietic cell lines.

Gene Functions References

  1. Study present for the first time in vitro and in vivo evidence suggesting that the major role of two ephrin A4 isoforms in chronic lymphocytic leukemia could be related with a non-previously described mechanism of survival linked to extravasation strongly dependent on integrin signaling. PMID: 27374180
  2. The cytoplasmic pattern of ephrin A4 could identify a subgroup of primary osteosarcoma patients with a high liability for progression, poor prognosis, and inferior response to chemotherapy. PMID: 20071790
  3. Characterization of the promoter PMID: 12030849
  4. This provides genetic evidence that Twist1, Msx2 and Efna4 function together in boundary formation and the pathogenesis of coronal synostosis. PMID: 16540516
  5. CLL B-cells showed a more heterogeneous Eph/EFN profile, specially EFNA4, EphB6 and EphA10. EphB6 and EFNA4 were further related with the clinical course of CLL. PMID: 18819711
  6. EFNA4-EphA2 interactions are involved in Chronic lymphocytic leukemia cell trafficking between blood and the tissues PMID: 19828693

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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