Recombinant Human ROCK1 Protein, N-His

Reference: YHG54301
Product nameRecombinant Human ROCK1 Protein, N-His
Origin speciesHuman
Expression systemProkaryotic expression
Molecular weight42.90 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 TypeMet1-Thr351
Aliases /SynonymsRenal carcinoma antigen NY-REN-35, p160 ROCK-1, p160ROCK, Rho-associated protein kinase 1, Rho-associated, coiled-coil-containing protein kinase I, Rho-associated, coiled-coil-containing protein kinase 1, ROCK-I, ROCK1
ReferenceYHG54301
NoteFor research use only.

Description of Recombinant Human ROCK1 Protein, N-His

Introduction

Recombinant Human ROCK1 Protein is a highly purified and biologically active protein that is produced through recombinant DNA technology. It is a key regulator of cellular functions such as cell adhesion, migration, and proliferation, making it an important protein in various biological processes. In this article, we will discuss the structure, activity, and application of this protein in detail.

Structure of Recombinant Human ROCK1 Protein

The ROCK1 protein is a member of the Rho-associated coiled-coil containing protein kinase (ROCK) family, which consists of two isoforms – ROCK1 and ROCK2. The human ROCK1 gene is located on chromosome 18 and encodes a 135 kDa protein with 1388 amino acids. The protein is composed of several domains, including a kinase domain, a coiled-coil domain, and a pleckstrin homology (PH) domain. The kinase domain is responsible for the catalytic activity of the protein, while the coiled-coil domain is involved in protein-protein interactions and the PH domain is involved in membrane binding.

Activity of Recombinant Human ROCK1 Protein

Recombinant Human ROCK1 Protein is a serine/threonine kinase that regulates various cellular processes by phosphorylating downstream targets. It is activated by binding to the small GTPase RhoA, which leads to a conformational change in the protein and exposure of the active site. ROCK1 then phosphorylates its substrates, including myosin light chain (MLC) and myosin phosphatase target subunit 1 (MYPT1), which results in the activation of actomyosin contractility and subsequent changes in cell shape, adhesion, and migration. Additionally, ROCK1 has been shown to play a role in cell proliferation, apoptosis, and gene expression through its interaction with other signaling pathways.

Application of Recombinant Human ROCK1 Protein

Recombinant Human ROCK1 Protein has a wide range of applications in both research and therapeutic fields. In research, it is commonly used as a tool to study the role of ROCK1 in various cellular processes. Its ability to regulate actomyosin contractility makes it a valuable tool in studying cell adhesion, migration, and invasion. Additionally, ROCK1 has been implicated in various diseases, including cancer, cardiovascular diseases, and neurological disorders, making it a potential therapeutic target.

In the therapeutic field, Recombinant Human ROCK1 Protein has been used in drug discovery and development. Inhibitors of ROCK1 have been developed and tested for their potential use in treating diseases such as hypertension, glaucoma, and cancer. Furthermore, the protein itself has been used in preclinical studies for the treatment of spinal cord injuries and neurodegenerative diseases.

Conclusion

In summary, Recombinant Human ROCK1 Protein is a crucial protein involved in regulating various cellular processes through its kinase activity. Its structure, activity, and application have been extensively studied and have provided valuable insights into its role in health and disease. With ongoing research and development, this protein holds great potential for future therapeutic interventions.

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