Recombinant Proteins

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LBP
CEA
HLA
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EPHA2 Human

EPH Receptor A2 Human Recombinant

Recombinant Human EPHA2, produced in HEK cells, is a single-chain glycoprotein. It consists of 515 amino acids (Ala24-Glu530) with a 2-amino acid C-terminal linker and a 6-amino acid C-terminal His tag. This results in a calculated molecular weight of 56.9 kDa.
Shipped with Ice Packs
Cat. No.
BT1964
Source
HEK 293.
Appearance
The product appears as a white powder following lyophilization (freeze-drying) and filtration.

EPHA2 Human, sf9

EPH Receptor A2 Human Recombinant, sf9

Recombinant Human EPHA2, expressed in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain. It consists of 520 amino acids (residues 27-537) with a molecular weight of 57.3 kDa. Note that on SDS-PAGE, the apparent molecular size may appear between 50-70 kDa. This EPHA2 protein is engineered with a 6-amino acid His-tag fused at the C-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT2021
Source
Sf9, Baculovirus cells.
Appearance
A clear, sterile-filtered solution.

EPHA3 Mouse

EPH Receptor A3 Mouse Recombinant

Recombinant EPHA3 protein, produced in HEK293 cells, is a single polypeptide chain comprising 527 amino acids (21-541 a.a.). It has a molecular weight of 59.5 kDa. The protein includes a 6-amino acid His tag at the C-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT2064
Source

HEK293 Cells.

Appearance
A colorless, sterile-filtered solution.

EPHA4 Mouse

EPH Receptor A4 Mouse Recombinant

Recombinant Mouse EPHA4, produced in Sf9 Baculovirus cells, is a single polypeptide chain comprising 536 amino acids (residues 20-547). This protein has a molecular weight of 59.3 kDa. When analyzed by SDS-PAGE, its apparent molecular size ranges from 50 to 70 kDa. The recombinant EPHA4 protein contains an 8-amino acid His-tag fused to its C-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT2184
Source
Sf9, Baculovirus cells.
Appearance
The product is a sterile and clear solution that has been filtered for purity.

EPHB1 Human

EPH Receptor B1 Human Recombinant

Recombinantly produced in HEK293 cells, EPHB1 Human Recombinant is a single, glycosylated polypeptide chain. This protein consists of 529 amino acids (amino acids 18-540), resulting in a molecular weight of 59.2 kDa. It features a 6-amino acid His tag at the C-terminus and undergoes purification using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT2231
Source

HEK293 Cells.

Appearance

Sterile filtered, colorless solution.

EPHB2 Human

EPH Receptor B2 Human Recombinant

Recombinant EPHB2 Human, expressed in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain. It comprises 533 amino acids (19-543a.a) and has a molecular mass of 59.1 kDa. However, on SDS-PAGE, the apparent molecular size will be approximately 50-70 kDa. This EPHB2 protein is fused to an 8 amino acid His-tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT2297
Source
Sf9, Baculovirus cells.
Appearance
A clear, sterile solution.

EPHB4 Mouse

EPH Receptor B4 Mouse Recombinant

Recombinant Mouse EPHB4, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain comprising 532 amino acids (16-539 a.a.). It has a molecular weight of 58.7kDa and exhibits a migration pattern of 50-70kDa on SDS-PAGE under reducing conditions. EPHB4 is expressed with an 8 amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT2395
Source
Sf9, Baculovirus cells.
Appearance
A clear solution, sterile filtered.
Definition and Classification

Eph receptors, named after their expression in an erythropoietin-producing human hepatocellular carcinoma cell line, represent the largest family of receptor tyrosine kinases (RTKs) in the animal kingdom . They are divided into two subclasses, EphA and EphB, based on sequence similarity and their binding affinity for either the glycosylphosphatidylinositol (GPI)-linked ephrin-A ligands or the transmembrane-bound ephrin-B ligands . Humans express nine EphA receptors (EphA1-8 and EphA10) and five EphB receptors (EphB1-4 and EphB6) .

Biological Properties

Eph receptors are widely expressed in various tissues and play crucial roles in numerous biological processes. They are involved in cell positioning, tissue patterning, and organ development . Eph receptors are expressed in most, if not all, cell types and are essential for cell contact-dependent communication . Their expression patterns and tissue distribution are highly regulated, with specific receptors being predominant in certain tissues .

Biological Functions

Eph receptors are pivotal in regulating cell migration, adhesion, differentiation, and proliferation . They play significant roles in the development of the nervous system, cardiovascular system, and other organs . Eph/ephrin signaling is crucial for immune responses and pathogen recognition, influencing cell-cell communication and immune cell migration .

Modes of Action

Eph receptors interact with their ligands, ephrins, on neighboring cells, leading to bidirectional signaling . This interaction can result in either cell-cell adhesion or repulsion, depending on the relative expression and affinity of the ligand-receptor pairs . The signaling cascades initiated by Eph/ephrin interactions involve autophosphorylation of tyrosine residues and recruitment of downstream signaling molecules .

Regulatory Mechanisms

The expression and activity of Eph receptors are tightly regulated at multiple levels. Transcriptional regulation, post-translational modifications, and interactions with other signaling pathways all contribute to the precise control of Eph receptor functions . Proteolytic cleavage and alternative splicing further increase the diversity and complexity of Eph receptor signaling .

Applications

Eph receptors have significant applications in biomedical research, diagnostic tools, and therapeutic strategies. They are potential targets for cancer therapy due to their roles in tumor progression, angiogenesis, and metastasis . Eph receptors are also being explored as targets for immunotherapy and as biomarkers for various diseases .

Role in the Life Cycle

Eph receptors are involved in critical processes throughout the life cycle, from embryonic development to aging . During development, they regulate cell sorting, migration, and boundary formation . In adulthood, Eph receptors maintain tissue homeostasis and are implicated in neural plasticity and immune responses . Dysregulation of Eph signaling is associated with various diseases, including cancer and neurological disorders .

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