Recombinant Proteins

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NECTIN1 Human

Nectin Cell Adhesion Molecule 1 Human Recombinant

This product consists of the human NECTIN1 protein, recombinantly produced in Sf9 insect cells (using a baculovirus expression system). It is a single polypeptide chain, containing 334 amino acids (specifically, amino acids 31-355 of the full protein sequence), and has a molecular weight of 37.3 kDa. This NECTIN1 protein is glycosylated, meaning it has sugar molecules attached to it. A 9 amino acid Histidine tag (His-tag) has been added to the C-terminus of the protein to facilitate purification, which was carried out using specialized chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT17282
Source

Sf9, Baculovirus cells.

Appearance
This product appears as a colorless solution that has been sterilized by filtration.

NECTIN3 Human

Nectin Cell Adhesion Molecule 3 Human Recombinant

Produced in Sf9 Insect cells, NECTIN3 is a single, glycosylated polypeptide chain consisting of 355 amino acids (58-404 a.a.) and possessing a molecular mass of 39.1kDa. It's important to note that on SDS-PAGE, the molecular size will appear approximately between 40-57kDa. The protein 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.
BT17363
Source

Sf9, Insect cells.

Appearance

A colorless solution that has undergone sterile filtration.

NECTIN2 Human

Nectin Cell Adhesion Molecule 2 Human Recombinant

Recombinant human NECTIN2, produced in Sf9 insect cells, is a single glycosylated polypeptide chain containing 337 amino acids (residues 32-360). It has a molecular mass of 36.3 kDa, though it appears between 40-57 kDa on SDS-PAGE due to glycosylation. This protein 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.
BT17193
Source

Sf9, Insect cells.

Definition and Classification

Nectins are a family of cellular adhesion molecules that belong to the immunoglobulin superfamily. They are involved in calcium-independent cellular adhesion and play crucial roles in the formation of various cell-cell junctions . The nectin family consists of four members: nectin-1, nectin-2, nectin-3, and nectin-4 . These molecules are ubiquitously expressed and have adhesive roles in a wide range of tissues, including epithelial and neuronal tissues .

Biological Properties

Key Biological Properties: Nectins are characterized by their ability to form both homophilic (same type) and heterophilic (different types) interactions . They have three extracellular immunoglobulin domains, a single transmembrane helix, and an intracellular domain that can bind to the scaffold protein afadin .

Expression Patterns and Tissue Distribution: Nectins are ubiquitously expressed in various tissues. For example, nectin-1 is found in the brain, skin, and eyes, while nectin-2 is expressed in the spleen, liver, and lungs . Nectin-3 is primarily found in the testis and placenta, and nectin-4 is expressed in the placenta and embryonic tissues .

Biological Functions

Primary Biological Functions: Nectins play essential roles in cell-cell adhesion, which is critical for the formation and maintenance of tissue architecture . They are involved in the formation of adherens junctions in epithelial cells and synaptic junctions in neurons .

Role in Immune Responses and Pathogen Recognition: Nectins are involved in immune responses by mediating the adhesion of immune cells to target cells . They also play a role in pathogen recognition, as certain viruses, such as herpes simplex virus, use nectins as entry receptors .

Modes of Action

Mechanisms with Other Molecules and Cells: Nectins interact with other cell adhesion molecules, such as cadherins, to enhance cell-cell adhesion . They can form homo-cis dimers on the same cell membrane and trans-interact with nectins on adjacent cells .

Binding Partners and Downstream Signaling Cascades: Nectins bind to afadin, which links them to the actin cytoskeleton . This interaction activates small G proteins, such as Cdc42 and Rac, which are involved in various signaling pathways that regulate cell movement, proliferation, and survival .

Regulatory Mechanisms

Regulatory Mechanisms Controlling Expression and Activity: The expression and activity of nectins are regulated at multiple levels, including transcriptional regulation and post-translational modifications . Transcription factors and signaling molecules can modulate the expression of nectin genes, while post-translational modifications, such as phosphorylation, can affect their activity and interactions .

Applications

Biomedical Research: Nectins are used as markers in various biomedical research studies to understand cell adhesion and signaling mechanisms .

Diagnostic Tools: Nectin-4, in particular, has been identified as a biomarker for certain cancers, such as breast and urothelial cancers . Diagnostic tools targeting nectin-4 are being developed to detect and monitor these cancers .

Therapeutic Strategies: Nectins are being explored as therapeutic targets. For example, enfortumab vedotin, an antibody-drug conjugate targeting nectin-4, has been approved for the treatment of urothelial carcinoma .

Role in the Life Cycle

Role Throughout the Life Cycle: Nectins play vital roles throughout the life cycle, from development to aging and disease . During development, they are involved in the formation of tissues and organs by mediating cell-cell adhesion . In adulthood, they maintain tissue integrity and function . Dysregulation of nectin expression or function can lead to various diseases, including cancer and neurological disorders .

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