Human EFNA1 (Ephrin-A1) - Recombinant Protein

Beta LifeScience SKU/CAT #: BLT-04215P
SDS-PAGE analysis of Human EFNA1 (Ephrin-A1) - Recombinant Protein, CAT
SDS-PAGE analysis of Human EFNA1 (Ephrin-A1) - Recombinant Protein, CAT# BLT-04215P, showing >90% purity under 15% SDS-PAGE (Reduced)

Human EFNA1 (Ephrin-A1) - Recombinant Protein

Beta LifeScience SKU/CAT #: BLT-04215P
Regular price $595.00 Sale price $445.00Save $150
/
Size

Quantity Pricing

Pack Size Price (USD)
500 µg $1,030 (Fall Promotion)
1 mg $1,870 (Fall Promotion)

For direct online orders, quantity pricing will be displayed in cart when you add 5x100ug or 10x100ug


Submit an inquiry or email inquiry@betalifesci.com for a customization request or bulk order quote.

Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Product Name Recombinant Human Ephrin-A1/EFNA1/LERK-1 Protein
Product Overview This recombinant human Ephrin-A1/EFNA1/LERK-1 protein includes amino acids 19-182aa of the target gene is expressed in HEK293 Cells.The protein is supplied in lyophilized form and formulated in phosphate buffered saline (pH7.4) containing 0.01% sarcosyl, 5% trehaloseprior to lyophilization.
Target Uniprot Id P20827
Recommended Name Ephrin-A1
Gene Name EFNA1
Synonyms Ephrin-A1; EPH-Related Receptor Tyrosine Kinase Ligand 1; LERK-1; Immediate Early Response Protein B
Species Human
Predicted Molecular Mass 20.4 kDa
Expression System Mammalian Cell
Expression Range 19-182aa
Tag C-6His
Purity >90%
Formulation Lyophilized
Buffer Phosphate buffered saline (pH7.4) containing 0.01% sarcosyl, 5%Trehalose
Storage Condition 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Reconstitution Instruction Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Applications Positive Control; Immunogen; SDS-PAGE; WB
Research Area Signal Transduction, Cardiovascular
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. Plays an important role in angiogenesis and tumor neovascularization. The recruitment of VAV2, VAV3 and PI3-kinase p85 subunit by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly. Exerts anti-oncogenic effects in tumor cells through activation and down-regulation of EPHA2. Activates EPHA2 by inducing tyrosine phosphorylation which leads to its internalization and degradation. Acts as a negative regulator in the tumorigenesis of gliomas by down-regulating EPHA2 and FAK. Can evoke collapse of embryonic neuronal growth cone and regulates dendritic spine morphogenesis.
Subcellular Location Cell membrane; Lipid-anchor, GPI-anchor.; [Ephrin-A1, secreted form]: Secreted.
Protein Family Ephrin family
Tissue Specificity Brain. Down-regulated in primary glioma tissues compared to the normal tissues. The soluble monomeric form is expressed in the glioblastoma multiforme (GBM) and breast cancer cells (at protein level).

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.

Recently viewed