CCS Human
Superoxide dismutase copper chaperone, Copper chaperone for superoxide dismutase.
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Description
CCS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 294amino acids (1-274a.a.) and having a molecular wieght of 31.2kDa. The CCS is fused to a 20a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Product Specs
Superoxide dismutase copper chaperone, Copper chaperone for superoxide dismutase.
MGSSHHHHHH SSGLVPRGSH MASDSGNQGT LCTLEFAVQM TCQSCVDAVR KSLQGVAGVQ DVEVHLEDQM VLVHTTLPSQ EVQALLEGTG RQAVLKGMGS GQLQNLGAAV AILGGPGTVQ GVVRFLQLTP ERCLIEGTID GLEPGLHGLH VHQYGDLTNN CNSCGNHFNP DGASHGGPQD SDRHRGDLGN VRADADGRAI FRMEDEQLKV WDVIGRSLII DEGEDDLGRG GHPLSKITGN SGERLACGII ARSAGLFQNP KQICSCDGLT IWEERGRPIA GKGRKESAQP PAHL.
Product Science Overview
Copper Chaperone for Superoxide Dismutase (CCS) is a crucial protein involved in the activation of the enzyme superoxide dismutase (SOD). SOD plays a vital role in protecting cells from oxidative damage by catalyzing the dismutation of superoxide radicals into oxygen and hydrogen peroxide. The human recombinant form of CCS is a synthesized version of this protein, designed to mimic its natural counterpart in the human body.
CCS is a copper-binding protein that facilitates the delivery of copper ions to SOD1, the cytosolic form of superoxide dismutase. The protein is composed of three distinct domains:
- Domain I: This domain contains a copper-binding motif and is responsible for the initial binding of copper ions.
- Domain II: This domain is structurally similar to SOD1 and is involved in the transfer of copper ions from CCS to SOD1.
- Domain III: This domain contains a cysteine-rich motif that is essential for the release of copper ions to SOD1.
The interaction between CCS and SOD1 is critical for the proper functioning of SOD1. Without the assistance of CCS, SOD1 would remain in an inactive apo-form, unable to perform its antioxidant functions.
The primary role of CCS is to ensure the proper activation of SOD1, which is essential for maintaining cellular redox balance. SOD1 is a key component of the cellular defense mechanism against oxidative stress, which can cause significant damage to cellular components, including DNA, proteins, and lipids. By facilitating the activation of SOD1, CCS helps protect cells from oxidative damage and contributes to overall cellular health.
Mutations in the CCS gene or disruptions in its function can lead to various health issues. For instance, impaired CCS function has been linked to neurodegenerative diseases such as Amyotrophic Lateral Sclerosis (ALS). In ALS, the accumulation of misfolded SOD1 proteins can lead to motor neuron degeneration. Understanding the role of CCS in SOD1 activation has provided valuable insights into the pathogenesis of such diseases and has opened up potential avenues for therapeutic interventions.
Research on human recombinant CCS has been extensive, with studies focusing on its structure, function, and role in disease. The recombinant form of CCS is used in various experimental setups to study its interaction with SOD1 and to explore potential therapeutic applications. For example, recombinant CCS can be used to investigate the effects of specific mutations on its function and to screen for compounds that can enhance its activity.
In addition to its role in neurodegenerative diseases, CCS has also been studied in the context of cancer. Elevated levels of CCS have been observed in certain types of cancer, suggesting that it may play a role in tumor progression. Further research is needed to fully understand the implications of CCS in cancer biology and to explore its potential as a therapeutic target.
