
Katalognummer: 209 - 101-M281
Produktkategori: Företag och industri > Vetenskap och laboratorium
Storlek: 100 µg
101-M281
CTGF belongs to the CCN (CYR61/CTGF/NOV) family of secreted proteins that share a common multimodular organization. Each protein contains an IGF-binding protein domain, a von Willebrand factor type C domain, a thrombospondin type I domain, and a cysteine knot domain. The multimodular CTGF has the ability to bind multiple ligands and has numerous effects on development, differentation, and disease. The C-terminal cysteine knot motif contains the heparin and low density lipoprotein receptor (LDLR) binding sites that contribute to the adhesive and mitogenic properties of CTGF.
102-P224
CTGF belongs to the CCN (CYR61/CTGF/NOV) family of secreted proteins that share a common multimodular organization. Each protein contains an IGF-binding protein domain, a von Willebrand factor type C domain, a thrombospondin type I domain, and a cysteine knot domain. The multimodular CTGF has the ability to bind multiple ligands and has numerous effects on development, differentation, and disease. The C-terminal cysteine knot motif contains the heparin and low density lipoprotein receptor (LDLR) binding sites that contribute to the adhesive and mitogenic properties of CTGF.
102-P245
NOV belongs to the CCN (CTGF/CYR61/NOV) family of secreted proteins that share a common multimodular organization. Each protein contains an IGFBP domain, a von Willebrand factor type C domain, a thrombospondin type I domain and a cysteine knot domain. NOV interacts with several proteins and is involved in both internal and external cell signaling.
102-P39
Erythropoietin (EPO) is a glycoprotein hormone that is principally known for its role in erythropoiesis, where it is responsible for stimulating proliferation and differentiation of erythroid progenitor cells. The differentiation of CFU-E (Colony Forming Unit-Erythroid) cells into erythrocytes can only be accomplished in the presence of EPO. Physiological levels of EPO in adult mammals are maintained primarily by the kidneys, whereas levels in fetal or neonatal mammals are maintained by the liver. EPO also can exert various non-hematopoietic activities, including vascularization and proliferation of smooth muscle, neural protection during hypoxia, and stimulation of certain B cells. EPO contains 166 amino acid residues and has a calculated molecular weight of approximately 18.4 kDa. As a result of glycosylation, Recombinant Human EPO migrates with an apparent molecular mass of 37.0 kDa by SDS-PAGE gel, under reducing and non-reducing conditions.
102-P61
MDC or CCL22, also named stimulated T cell chemotactic protein (STCP-1), is a CC chemokine initially isolated from clones of monocyte-derived macrophages. Human MDC cDNA encodes a precursor protein of 93 amino acid residues with a 24 amino acid residue predicted signal peptide that is cleaved to yield a 69 amino acid residue mature 8 kDa protein. At the amino acid sequence level, MDC shows less than 35% identity to other CC chemokine family members. Human MDC is expressed in dendritic cells, macrophages and activated monocytes. In addition, MDC expression is also detected in the tissues of thymus, lymph node and appendix. The gene for human MDC has been mapped to chromosome 16 rather than chromosome 17 where the genes for many human CC chemokines are clustered. Recombinant or chemically synthesized mature MDC has been shown to induce chemotaxis or Ca2+ mobilization in dendritic cells, IL2 activated NK cells, and activated T lymphocytes. A CD8+ T lymphocyte-derived secreted soluble activity that suppresses infection by primary non-syncytium-inducing and syncytium-inducing HIV1 isolates and the T cell line-adapted isolate HIV1 IIIB, has been identified as MDC. Based on aminoterminal sequence analysis, the major CD8 + T lymphocyte-derived MDC protein yielded an aminoterminal sequence of YGANM, which is two amino acid residues shorter than the predicted mature MDC. The difference in potency between the two mature MDC isoforms has not been determined.

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