Recombinant Proteins
Product List
CAPS Human
Calcyphosine Human Recombinant
CAPS Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 209 amino acids (1-189 a.a.) and having a molecular mass of 23.1kDa. The CAPS is purified by proprietary chromatographic techniques.
CAPSL Human
Calcyphosine-Like Human Recombinant
The CAPSL is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Introduction
Calcyphosine, also known as CAPS, is a cytoplasmic EF-hand calcium-binding protein. It is also referred to as thyroid protein p24. This protein is involved in both Ca²⁺-phosphatidylinositol and cAMP signal cascades . Calcyphosine-2 (CAPS2) and calcyphosine-like protein (CAPSL) are similar proteins expressed in various tissues .
Key Biological Properties: Calcyphosine is a highly conserved calcium-binding protein. It shows elevated expression in many forms of human cancer .
Expression Patterns: Calcyphosine is expressed in various tissues, including the thyroid, where it was initially identified . It is also found in other tissues such as the epididymis .
Tissue Distribution: Calcyphosine is widely distributed across different tissues, with significant expression in the thyroid and other tissues .
Primary Biological Functions: Calcyphosine plays a role in cellular signaling events, particularly in the regulation of ion transport . It is also involved in spindle formation during mitosis, helping create the kinetochore fibers that bind and segregate chromosomes .
Role in Immune Responses and Pathogen Recognition: While specific roles in immune responses and pathogen recognition are not well-documented, its involvement in cellular signaling suggests potential indirect roles in these processes.
Mechanisms with Other Molecules and Cells: Calcyphosine interacts with other proteins and molecules through its calcium-binding properties. It undergoes a structural shift when bound to calcium, regulating its binding to other proteins .
Binding Partners: Calcyphosine binds to hydrophobic phenyl-Sepharose when bound to calcium . It also shows similarities to calmodulin, a calcium-binding protein that interacts with enzymes such as myosin light-chain kinase, calcineurin, and CaM-kinase II .
Downstream Signaling Cascades: Calcyphosine is involved in both Ca²⁺-phosphatidylinositol and cAMP signal cascades .
Transcriptional Regulation: The expression of calcyphosine is regulated at the transcriptional level, with alternative splicing generating two transcript variants .
Post-Translational Modifications: Calcyphosine is a target for phosphorylation by protein kinase A downstream of TSH signaling . This modification regulates its activity and interactions with other proteins.
Biomedical Research: Calcyphosine is studied for its role in cancer, particularly its elevated expression in various forms of human cancer . It is also used in research on cellular signaling and spindle formation during mitosis .
Diagnostic Tools: Calcyphosine antibodies are used in diagnostic tools such as Western blotting, immunofluorescence, and ELISA to detect its presence in various tissues .
Therapeutic Strategies: While specific therapeutic strategies targeting calcyphosine are not well-documented, its role in cancer and cellular signaling suggests potential therapeutic applications.
Development: Calcyphosine is involved in spindle formation during mitosis, playing a crucial role in cell division and development .
Aging and Disease: Elevated expression of calcyphosine is observed in many forms of human cancer, suggesting a role in disease progression . Its involvement in cellular signaling and ion transport may also impact aging processes.
