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S100A4
Protein S100-A4 (S100A4) is a protein that in humans is encoded by the ''S100A4'' gene. Function The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21. This protein may function in motility, invasion, and tubulin polymerization. Chromosomal rearrangements and altered expression of this gene have been implicated in tumor metastasis. Multiple alternatively spliced variants, encoding the same protein, have been identified. Interactions S100A4 has been shown to interact with S100 calcium binding protein A1. Therapeutic targeting for cancer S100A4, a member of the S100 calcium-binding protein family secreted by tumor and stro ...
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S100 Calcium Binding Protein A1
Protein S100-A1, also known as S100 calcium-binding protein A1 is a protein which in humans is encoded by the ''S100A1'' gene. S100A1 is highly expressed in cardiac and skeletal muscle, and localizes to Z-discs and sarcoplasmic reticulum. S100A1 has shown promise as an effective candidate for gene therapy to treat post- myocardially infarcted cardiac tissue. Structure S100A1 is a member of the S100 family of proteins expressed in cardiac muscle, skeletal muscle and brain, with highest density at Z-lines and sarcoplasmic reticulum. S100A1 contains 4 EF-hand calcium-binding motifs in its dimerized form, and can exist as either a hetero or homodimer. The S100A1 homodimer is high affinity (nanomolar range or tighter), and is formed through hydrophobic packing of an X-type 4-helix bundle created between helices 1, 1', 4, and 4'. Protein nuclear magnetic resonance spectroscopy structural information on the homodimeric form of this protein shows that each monomer is helical and cont ...
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Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residue ...
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Gene
In biology, the word gene (from , ; "...Wilhelm Johannsen coined the word gene to describe the Mendelian units of heredity..." meaning ''generation'' or ''birth'' or ''gender'') can have several different meanings. The Mendelian gene is a basic unit of heredity and the molecular gene is a sequence of nucleotides in DNA that is transcribed to produce a functional RNA. There are two types of molecular genes: protein-coding genes and noncoding genes. During gene expression, the DNA is first copied into RNA. The RNA can be directly functional or be the intermediate template for a protein that performs a function. The transmission of genes to an organism's offspring is the basis of the inheritance of phenotypic traits. These genes make up different DNA sequences called genotypes. Genotypes along with environmental and developmental factors determine what the phenotypes will be. Most biological traits are under the influence of polygenes (many different genes) as well as gen ...
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EF-hand
The EF hand is a helix–loop–helix structural domain or ''motif'' found in a large family of calcium-binding proteins. The EF-hand motif contains a helix–loop–helix topology, much like the spread thumb and forefinger of the human hand, in which the Ca2+ ions are coordinated by ligands within the loop. The motif takes its name from traditional nomenclature used in describing the protein parvalbumin, which contains three such motifs and is probably involved in muscle relaxation via its calcium-binding activity. The EF-hand consists of two alpha helices linked by a short loop region (usually about 12 amino acids) that usually binds calcium ions. EF-hands also appear in each structural domain of the signaling protein calmodulin and in the muscle protein troponin-C. Calcium ion binding site The calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by ...
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MIA PaCa-2
MIA PaCa-2 is a human pancreatic cancer cell line used extensively in pancreatic cancer research and therapy development. In 1977, MIA PaCa-2 cells were derived from the carcinoma of a 65-year-old male. The cells exhibit CK5.6, AE1/AE3, E-cadherin, vimentin, chromogranin A, synaptophysin, SSTR2, and Neurotensin receptor 1, NTR1, but not CD56. The cells have a round, epithelial morphology, and are adherent in cell culture. MIA PaCa-2 has served for decades as a model of pancreatic cancer, and studies of MIA PaCa-2 physiology have helped clarify the mechanisms of carcinogenesis in pancreatic cancer, aid the development of cancer cell lysate, lysates targeting Immunoglobulin G, IgG production, and augmented drug-delivery methods relying on quantum dot, quantum dots. See also *DU145 *PANC-1 *BxPC-3 References {{Reflist External links Cellosaurus entry for MIA-Paca-2
Human cell lines ...
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