Recombinant Proteins

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ITGB1 Human

Integrin Beta 1 Human Recombinant

Recombinant human ITGB1, produced in E. coli, is a single polypeptide chain of 462 amino acids (residues 21-461) with a molecular weight of 51.2 kDa. It includes a 20 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24519
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

ITGB1 Human, Sf9

Integrin Beta 1 Human Recombinant, Sf9

Recombinant human ITGB1, expressed in Sf9 insect cells using a baculovirus system, is a single, glycosylated polypeptide chain. It consists of 716 amino acids (residues 1-728) and has a molecular mass of 79.4 kDa. However, on SDS-PAGE, it appears at a size of approximately 70-100 kDa. This discrepancy is attributed to glycosylation. The protein is tagged at the C-terminus with an 8-amino acid His-tag and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24598
Source
Sf9, Baculovirus cells.
Appearance
A clear, colorless solution that has been sterilized by filtration.

ITGB1BP3 Human

Integrin Beta 1 Binding Protein 3 Human Recombinant

Recombinant human ITGB1BP3, expressed in E. coli, is available as a single polypeptide chain. It consists of 253 amino acids, with a molecular weight of 28.4 kDa. The protein comprises amino acids 1-230 of ITGB1BP3, along with a 23 amino acid His-tag fused at the N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24654
Source
E.coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

ITGB3BP Human

Integrin Beta 3 Binding Protein Human Recombinant

Recombinant human ITGB3BP, produced in E. coli bacteria, is a single chain of 239 amino acids (specifically amino acids 1 to 216), with a molecular weight of 27.1 kDa. It has a 23 amino acid His-tag attached to its N-terminus and is purified using specialized chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT24731
Source
E.coli.
Appearance
A clear, sterile solution.

ITGB4 Human

Integrin Beta 4 Human Recombinant

Produced in Sf9 Baculovirus cells, ITGB4 is a single, glycosylated polypeptide chain consisting of 691 amino acids (28-710a.a.). It has a molecular mass of 77.5kDa, although its size on SDS-PAGE may appear between 70-100kDa. 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.
BT24827
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered colorless solution.
Definition and Classification

Integrins are a large family of transmembrane receptors that facilitate cell-cell and cell-extracellular matrix (ECM) adhesion. They are heterodimeric proteins composed of alpha (α) and beta (β) subunits. In humans, there are 18 α and 8 β subunits, which combine to form at least 24 distinct integrin heterodimers . These receptors play crucial roles in various cellular processes, including signal transduction, cell migration, and the maintenance of cell structure .

Biological Properties

Key Biological Properties: Integrins are involved in bidirectional signaling, meaning they can transmit signals from the ECM to the cell interior and vice versa . This signaling is essential for cellular responses to the external environment.

Expression Patterns and Tissue Distribution: Integrins are ubiquitously expressed across various tissues. Different integrin subunits are expressed in specific patterns, contributing to the unique functions of each integrin heterodimer. For example, integrin α5β1 is predominantly found in fibroblasts and endothelial cells, while integrin αIIbβ3 is primarily expressed in platelets .

Biological Functions

Primary Biological Functions: Integrins mediate cell adhesion, migration, and proliferation. They are essential for the formation of stable cell-ECM interactions, which are critical for tissue integrity and repair .

Role in Immune Responses and Pathogen Recognition: Integrins play a significant role in the immune system by facilitating the migration of leukocytes to sites of infection or injury. They also participate in the recognition and binding of pathogens, aiding in the immune response .

Modes of Action

Mechanisms with Other Molecules and Cells: Integrins interact with various ECM proteins such as fibronectin, collagen, and laminin. These interactions are crucial for the activation of intracellular signaling pathways .

Binding Partners and Downstream Signaling Cascades: Upon binding to their ligands, integrins cluster and recruit cytoplasmic proteins like talin and kindlin, which link integrins to the actin cytoskeleton. This clustering activates signaling pathways such as the MAPK, PI3K/Akt, and Rho GTPase pathways, which regulate cell survival, proliferation, and migration .

Regulatory Mechanisms

Expression and Activity Control: Integrin expression is tightly regulated at the transcriptional level by various transcription factors. Post-translational modifications, such as phosphorylation and glycosylation, also modulate integrin activity and affinity for ligands .

Transcriptional Regulation and Post-Translational Modifications: Specific transcription factors, including NF-κB and AP-1, regulate the expression of integrin genes. Post-translational modifications, such as phosphorylation by kinases, can alter integrin conformation and function .

Applications

Biomedical Research: Integrins are extensively studied in cancer research due to their role in tumor cell migration and invasion. They are also investigated in cardiovascular diseases and wound healing .

Diagnostic Tools and Therapeutic Strategies: Integrins serve as biomarkers for various diseases and are targets for therapeutic interventions. Integrin inhibitors and antibodies are being developed for the treatment of conditions like thrombosis, cancer, and inflammatory diseases .

Role in the Life Cycle

Development to Aging and Disease: Integrins are vital throughout the life cycle, from embryonic development to aging. During development, they regulate cell migration and tissue formation. In adults, they maintain tissue homeostasis and repair. Dysregulation of integrin function is associated with various diseases, including cancer, fibrosis, and autoimmune disorders .

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