CILP
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Official Full Name
cartilage intermediate layer protein, nucleotide pyrophosphohydrolase
- Recombinant Proteins
- Cell & Tissue Lysates
- Protein Pre-coupled Magnetic Beads
- Human
- Mouse
- Zebrafish
- E.coli
- HEK293
- Insect Cell
- Mammalian Cell
- Mammalian cells
- Wheat Germ
- Yeast
- GST
- His
- Fc
- Avi
- Myc
- T7
- Non
- Involved Pathway
- Protein Function
- Interacting Protein
- Other Resource
CILP involved in several pathways and played different roles in them. We selected most pathways CILP participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with CILP were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
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CILP has several biochemical functions, for example, NOT alkaline phosphatase activity, NOT nucleotide diphosphatase activity. Some of the functions are cooperated with other proteins, some of the functions could acted by CILP itself. We selected most functions CILP had, and list some proteins which have the same functions with CILP. You can find most of the proteins on our site.
Function | Related Protein |
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NOT alkaline phosphatase activity | CILP;CILP2 |
NOT nucleotide diphosphatase activity | CILP;CILP2 |
CILP has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with CILP here. Most of them are supplied by our site. Hope this information will be useful for your research of CILP.
TGFB1
Research Area
Related articles
- Reviews
- Q&As
Customer Reviews (3)
Write a reviewThe catalytic activity of this protein is amazing, it can promote chemical reactions in a short time with unmatched catalytic efficiency.
This reproducibility of CILP is unmatched, and its ability to maintain a high degree of consistency regardless of conditions makes it ideal for experiments or applications that require a high degree of reproducibility.
Their CILP activity retention time is very long, can maintain the activity for a long time, very stable and reliable.
Q&As (6)
Ask a questionDuring extracellular matrix formation and degradation, CILP proteins can interact with other extracellular matrix proteins, such as collagen, glycoproteins, etc., to form a more complex network structure. At the same time, it can also activate enzymes such as matrix metalloproteinases and promote the degradation of extracellular matrix.
Studies have shown that CILP protein plays an important role in a variety of human diseases, such as osteoarthritis and osteoporosis. The occurrence of these diseases is often related to abnormal expression and function of CILP proteins.
The activity of CILP protein is affected by a variety of regulators, including Ca2+, pH, phosphorylation modification, etc. These regulators can influence the structure and function of CILP proteins, thereby affecting their biological functions.
Expression of CILP protein can be affected by a variety of environmental factors. For example, hormone levels, oxidative stress, mechanical forces, nutritional factors, etc. can affect the expression of CILP protein.
Studying the biological function of CILP proteins requires a variety of experimental techniques and methods, such as cell biology, molecular biology, biochemistry and genomics. By observing gene expression, cell growth, differentiation and other indicators, the biological function of CILP protein in cells can be evaluated.
CILP proteins can interact with a variety of cell signaling pathways, including the MAPK pathway, PI3K/Akt pathway, etc. By interacting with these pathways, CILP proteins can regulate the biological behavior of cells.
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