Recombinant Proteins

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EFNB3 Human

Ephrin- B3 Human Recombinant

Recombinant human EFNB3, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 224 amino acids (residues 28-226). With a molecular weight of 24.6 kDa, EFNB3 is fused to a 25 amino acid His-tag at the N-terminus and purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT3247
Source
E.coli.
Appearance
Clear, colorless, and sterile-filtered solution.

EFNB3 Human, Sf9

Ephrin- B3 Human Recombinant, Sf9

Produced in Sf9 Baculovirus cells, EFNB3 is a single, glycosylated polypeptide chain with a molecular weight of 23.0 kDa (208 amino acids, 28-226a.a.). On SDS-PAGE, its molecular size appears approximately between 28-40 kDa. The protein is expressed with a 6-amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3311
Source
Sf9, Baculovirus cells.
Appearance
Clear, colorless solution, sterile-filtered.

EFNA5 Human, Active

Ephrin A5 Human Recombinant, Active

EFNA5 Human Recombinant is a single, glycosylated polypeptide chain consisting of amino acids 21-203. With a 239 amino acid hIgG-His-Tag fused to the C-terminus, it totals 422 amino acids and has a molecular mass of 48.1 kDa. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT2937
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered colorless solution.

EFNB1 Human

Ephrin-B1 Human Recombinant

Recombinant human EFNB1, expressed in E.coli, is a single, non-glycosylated polypeptide chain. It consists of 231 amino acids (residues 28-237), resulting in a molecular weight of 25.3 kDa. The protein is engineered with a 21 amino acid His-Tag at the N-terminus to facilitate purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3002
Source
E.coli.
Appearance
The product is a clear and colorless solution that has been sterilized by filtration.

EFNB1 Human, Sf9

Ephrin-B1 Human Recombinant, Sf9

Produced in Sf9 Baculovirus cells, EFNB1 is a single, glycosylated polypeptide chain with a molecular weight of 50.3 kDa (28-237 a.a.). It appears as a band around 50-70 kDa on SDS-PAGE. EFNB1 is expressed with a 242 amino acid hIgG-His-tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3062
Source

Sf9, Baculovirus cells.

Appearance
Sterile Filtered colorless solution

EFNB2 Human

Ephrin- B2 Human Recombinant

Recombinant human EFNB2, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 227 amino acids (residues 28-229). It has a molecular weight of 24.9 kDa. The protein features a 25 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3138
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

EFNB2 Mouse

Ephrin- B2 Mouse Recombinant

Recombinant Mouse EFNB2, expressed in Sf9 Baculovirus cells, is a single polypeptide chain with a molecular weight of 23.4 kDa. This protein comprises 212 amino acids (residues 29-232). It features an 8 amino acid His-tag fused at the C-terminus. Purification is achieved using proprietary chromatographic techniques. Note: The molecular size observed on SDS-PAGE may range from approximately 28-40 kDa.
Shipped with Ice Packs
Cat. No.
BT3196
Source
Sf9, Baculovirus cells.
Appearance
A clear, sterile-filtered solution.

EFNA1 Human, HEK

Ephrin A1 Human Recombinant, HEK

Recombinant EFNA1 Human, produced in HEK293 cells, is a single, glycosylated polypeptide chain with a molecular weight of 20.2kDa (calculated). It comprises 170 amino acids, including a 6 a.a C-terminal His tag, spanning from amino acid positions 19 to 182.

Shipped with Ice Packs
Cat. No.
BT2624
Source

HEK293 cells.

Appearance
White lyophilized powder, filtered for purity.

EFNA1 Human, Sf9

Ephrin A1 Human Recombinant, Sf9

Produced in Sf9 Baculovirus cells, EFNA1 is a single, glycosylated polypeptide chain. It comprises 406 amino acids (specifically, amino acids 19-182a.a.) and has a molecular mass of 46.6kDa. On SDS-PAGE, the molecular size will appear within the range of 40-57kDa. This EFNA1 protein is expressed with a 242 amino acid hIgG-His-tag located at the C-Terminus. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT2677
Source
Sf9, Baculovirus cells.
Appearance
A colorless solution that has undergone sterile filtration.

EFNA3 Human

Ephrin A3 Human Recombinant

Recombinant human EFNA3, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 217 amino acids (residues 23-214). This protein has a molecular weight of 24 kDa. A 25 amino acid His-tag is fused to the N-terminus of EFNA3. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT2749
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.
Definition and Classification

Ephrins, also known as Eph receptor-interacting proteins, are a family of proteins that serve as ligands for the Eph receptor, the largest known subfamily of receptor protein-tyrosine kinases (RTKs) . Ephrins are divided into two subclasses based on their structure and linkage to the cell membrane: ephrin-A and ephrin-B. Ephrin-As are anchored to the membrane by a glycosylphosphatidylinositol (GPI) linkage and lack a cytoplasmic domain, while ephrin-Bs are attached to the membrane by a single transmembrane domain containing a short cytoplasmic PDZ-binding motif .

Biological Properties

Ephrins exhibit a variety of biological properties, including their expression patterns and tissue distribution. They are membrane-bound proteins, meaning their signaling can only occur through direct cell-cell interaction . Ephrin ligands and their receptors are expressed in various tissues, playing crucial roles in embryonic development and adult tissue homeostasis . For instance, ephrin-B2 and EphB4 are essential in determining the arterial and venous fate of endothelial cells .

Biological Functions

Ephrin-Eph signaling regulates numerous biological processes. During embryonic development, they guide axon growth cones, form tissue boundaries, and facilitate cell migration and segmentation . In adults, they are involved in long-term potentiation, angiogenesis, and stem cell differentiation . Additionally, Eph receptors and ephrins play significant roles in immune responses and pathogen recognition .

Modes of Action

Ephrin-Eph interactions follow a bidirectional signaling mechanism. Upon cell-cell contact, high-affinity binding between Eph receptors and ephrin ligands occurs, initiating intracellular signaling events . These events can lead to changes in cell shape, motility, and adhesion . Ephrin-As typically bind EphAs with high affinity through a “lock-and-key” mechanism, while EphBs bind ephrin-Bs with lower affinity via an “induced fit” mechanism .

Regulatory Mechanisms

The expression and activity of ephrins and Eph receptors are tightly regulated through various mechanisms. Transcriptional regulation and post-translational modifications play critical roles in controlling their functions . For example, the Src family kinases and JAK-STAT pathways are involved in the reverse signaling of Eph and ephrins .

Applications

Ephrin-Eph signaling has broad applications in biomedical research, diagnostic tools, and therapeutic strategies. They are being explored as potential targets for cancer treatment, particularly in breast cancer, where targeting specific Eph receptors and ephrins can induce apoptosis and tumor regression . Additionally, their roles in angiogenesis and immune responses make them valuable in developing therapies for various diseases .

Role in the Life Cycle

Ephrins play crucial roles throughout the life cycle, from development to aging and disease. During embryonic development, they guide cell migration and tissue formation . In adulthood, they maintain tissue homeostasis and contribute to processes like neuronal plasticity and vascular remodeling . Dysregulation of ephrin-Eph signaling is associated with various diseases, including cancer and neurodegenerative disorders .

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