摘要:
A method for differentiation of osteoarthritis from rheumatoid arthritis and non-disease conditions in a sample, comprising measuring in the sample the concentration of human cartilage intermediate layer protein 2 (CILP-2) in body fluids and more specifically, measuring in the sample the concentration of the N-terminal part of CILP-2 (2C1) or fragments thereof.
摘要:
A method for differentiation of osteoarthritis from rheumatoid arthritis and non-disease conditions in a sample, comprising measuring in the sample the concentration of human cartilage intermediate layer protein 2(CILP-2) in body fluids and more specifically, measuring in the sample the concentration of the N-terminal part of CILP-2 (2C1) or fragments thereof.
摘要:
A method for differentiation of osteoarthritis from rheumatoid arthritis and non-disease conditions in a sample, comprising measuring in the sample the concentration of human cartilage intermediate layer protein 2 (CILP-2) in body fluids and more specifically, measuring in the sample the concentration of the N-terminal part of CILP-2 (2C1) or fragments thereof.
摘要:
A method for differentiation of osteoarthritis from rheumatoid arthritis and non-disease conditions in a sample, comprising measuring in the sample the concentration of human cartilage intermediate layer protein 2(CILP-2) in body fluids and more specifically, measuring in the sample the concentration of the N-terminal part of CILP-2 (2C1) or fragments thereof.
摘要:
A method for differentiation of osteoarthritis from rheumatoid arthritis and non-disease conditions in a sample, comprising measuring in the sample the concentration of a peptide comprising the 15 amino acid sequence (SEQ ID NO: 1) of the human cartilage intermediate layer protein 2.
摘要翻译:一种用于在样品中分化骨关节炎与类风湿性关节炎和非疾病状况的方法,包括在样品中测量包含人软骨中间层蛋白2的15个氨基酸序列(SEQ ID NO:1)的肽的浓度。
摘要:
A novel, N-oligosaccharide-substituted-specific protein of approximately 91.5 kDa was purified from extracts of human articular cartilage and designated Cartilage Intermediate Layer Protein (CILP). The protein is a chondrocyte product which is deposited in the interterritorial matrix. The gene encoding CILP, as well as its mRNA, were isolated and characterized. A single 4.2 kb mRNA detected in human articular cartilage encodes a polypeptide of 1184 amino acids with a calculated molecular weight of 132.5 kDa. The protein has a putative signal peptide of 21 amino acids, and is a proform of two polypeptides. The amino-terminal half corresponds to CILP (molecular weight of 78.5 kDa, not including post-translational modifications) and the carboxy-terminal half corresponds to a protein homologous to a porcine nucleotide pyrophosphohydrolase, NTPPHase (molecular weight of 51.8 kDa, not including post-translational modifications).