Recombinant Human PSMC1, N-His

Reference: YHF48601
Product nameRecombinant Human PSMC1, N-His
Origin speciesHuman
Expression systemEukaryotic expression
Molecular weight51.49 kDa
Protein delivered with Tag?N-Terminal His Tag
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-Leu440
Aliases /SynonymsP26s4, 26S proteasome regulatory subunit 4, Proteasome 26S subunit ATPase 1, PSMC1, 26S proteasome AAA-ATPase subunit RPT2
ReferenceYHF48601
NoteFor research use only.

Description of Recombinant Human PSMC1, N-His

Introduction

Recombinant Human PSMC1 (proteasome 26S subunit ATPase 1) is a highly conserved protein that plays a crucial role in protein degradation and cellular homeostasis. It belongs to the AAA+ (ATPases associated with diverse cellular activities) family and is an essential component of the 26S proteasome complex, which is responsible for the degradation of misfolded or damaged proteins.

Structure of Recombinant Human PSMC1

Recombinant Human PSMC1 is a 97 kDa protein that consists of 853 amino acids. It is composed of two main domains: the N-terminal domain (NTD) and the C-terminal domain (CTD). The NTD contains the AAA+ ATPase domain, which is responsible for the ATPase activity of PSMC1. The CTD contains the coiled-coil domain, which is involved in the interaction with other subunits of the proteasome complex.

Activity of Recombinant Human PSMC1

The main activity of Recombinant Human PSMC1 is to act as an ATPase, which provides the energy for the degradation of proteins by the 26S proteasome complex. It uses ATP hydrolysis to unfold and translocate target proteins into the proteasome for degradation. PSMC1 also plays a crucial role in the assembly and stability of the 26S proteasome complex.

In addition to its ATPase activity, PSMC1 has been shown to have other functions. It has been reported to interact with various proteins involved in transcriptional regulation, DNA repair, and cell cycle control, suggesting its involvement in these cellular processes.

Application of Recombinant Human PSMC1

Recombinant Human PSMC1 has various applications in both research and therapeutic settings. Its crucial role in protein degradation makes it a valuable tool for studying protein turnover and cellular homeostasis. It can be used to investigate the mechanism of action of the 26S proteasome complex and its involvement in various cellular processes.

Moreover, Recombinant Human PSMC1 has been used in drug discovery and development. Dysregulation of the proteasome complex has been linked to various diseases, including cancer and neurodegenerative disorders. PSMC1 inhibitors have been developed as potential therapeutics for these diseases, and Recombinant Human PSMC1 can be used to screen and validate these inhibitors.

Furthermore, Recombinant Human PSMC1 has been used as an antigen in the development of diagnostic assays for autoimmune diseases. Autoantibodies against PSMC1 have been detected in patients with systemic lupus erythematosus (SLE) and rheumatoid arthritis (RA). Recombinant Human PSMC1 can be used as a substrate in enzyme-linked immunosorbent assays (ELISA) to detect these autoantibodies, aiding in the diagnosis and monitoring of these diseases.

Conclusion

In summary, Recombinant Human PSMC1 is a highly conserved protein that plays a crucial role in protein degradation and cellular homeostasis. Its structure, activity, and various applications make it a valuable tool in both research and therapeutic settings. Further studies on PSMC1 and its interactions with other proteins will provide a better understanding of its role in cellular processes and its potential as a therapeutic target for various diseases.

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