Recombinant Human ACVRL1/ALK-1 Protein, N-SUMO & C-His

Reference: YHE20502
Product nameRecombinant Human ACVRL1/ALK-1 Protein, N-SUMO & C-His
Origin speciesHuman
Expression systemEukaryotic expression
Molecular weight22.92 kDa
BufferLyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
FormLiquid
Delivery conditionDry Ice
Delivery lead time in business days3-5 days if in stock; 3-5 weeks if production needed
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
BrandAntibodySystem
Host speciesEscherichia coli (E.coli)
Fragment TypeAsp22-Gln118
Aliases /SynonymsSerine/threonine-protein kinase receptor R3, SKR3, 2.7.11.30, Activin receptor-like kinase 1, ALK-1, TGF-B superfamily receptor type I, TSR-I, ACVRL1, ACVRLK1, ALK1
ReferenceYHE20502
NoteFor research use only.

Description of Recombinant Human ACVRL1/ALK-1 Protein, N-SUMO & C-His

Introduction

The Recombinant Human ACVRL1/ALK-1 Protein is a highly purified and biologically active protein that is produced through recombinant DNA technology. This protein belongs to the transforming growth factor beta (TGF-β) receptor family and plays a crucial role in regulating cell growth and differentiation. In this article, we will discuss the structure, activity, and applications of this recombinant protein.

Structure of Recombinant Human ACVRL1/ALK-1 Protein

The Recombinant Human ACVRL1/ALK-1 Protein is a homodimeric protein consisting of two identical subunits, each with a molecular weight of approximately 50 kDa. The protein is composed of a large extracellular domain, a single transmembrane domain, and a cytoplasmic domain. The extracellular domain contains a cysteine-rich region, a serine/threonine kinase domain, and a glycine-serine-rich region, which are all essential for its biological activity.

The crystal structure of the extracellular domain of ACVRL1/ALK-1 has been determined, revealing a compact and globular structure with two intertwined subunits. The extracellular domain is responsible for ligand binding and receptor activation, while the transmembrane and cytoplasmic domains are involved in signal transduction.

Activity of Recombinant Human ACVRL1/ALK-1 Protein

The primary function of Recombinant Human ACVRL1/ALK-1 Protein is to act as a receptor for the TGF-β superfamily of growth factors, including bone morphogenetic proteins (BMPs) and activins. Upon ligand binding, the protein undergoes conformational changes, leading to the activation of the serine/threonine kinase domain. This results in the phosphorylation of downstream signaling molecules, such as SMAD proteins, which ultimately regulate gene expression and control various cellular processes, including cell proliferation, differentiation, and migration.

Moreover, studies have shown that Recombinant Human ACVRL1/ALK-1 Protein is also involved in angiogenesis, the process of forming new blood vessels. It regulates the proliferation and migration of endothelial cells, which are the building blocks of blood vessels, and plays a crucial role in maintaining vascular integrity and homeostasis.

Applications of Recombinant Human ACVRL1/ALK-1 Protein

Due to its involvement in various cellular processes, Recombinant Human ACVRL1/ALK-1 Protein has a wide range of applications in both research and therapeutic settings. Here are some of its key applications:

Studying TGF-β Signaling Pathway

Recombinant Human ACVRL1/ALK-1 Protein is an essential tool for studying the TGF-β signaling pathway. Its ability to bind and activate TGF-β ligands makes it a valuable reagent for investigating the downstream effects of this pathway on different cell types. It can also be used to study the role of ACVRL1/ALK-1 mutations in various diseases, such as hereditary hemorrhagic telangiectasia (HHT), a genetic disorder characterized by abnormal blood vessel formation.

Angiogenesis Research

Recombinant Human ACVRL1/ALK-1 Protein has been extensively used in angiogenesis research. Its role in regulating endothelial cell proliferation and migration makes it a valuable tool for studying the mechanisms involved in blood vessel formation and maintenance. It can also be used to investigate the potential therapeutic effects of targeting ACVRL1/ALK-1 in diseases associated with abnormal angiogenesis, such as cancer and cardiovascular diseases.

Therapeutic Applications

Recombinant Human ACVRL1/ALK-1 Protein has shown promising results in preclinical studies as a potential therapeutic agent for various diseases. For instance

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