SBP-tag
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SBP-tag
The Streptavidin-Binding Peptide (SBP)-Tag is a 38-amino acid sequence that may be engineered into recombinant proteins. Recombinant proteins containing the SBP-Tag bind to streptavidin and this property may be utilized in specific purification, detection or immobilization strategies. The sequence of the SBP tag is MDEKTTGWRGGHVVEGLAGELEQLRARLEHHPQGQREP. Discovery The Streptavidin-Binding Peptide was discovered within a library of seven trillion stochastically-generated peptides using the in vitro selection technique of mRNA Display. Selection was performed by incubating with streptavidin-agarose followed by elution with biotin. The SBP-Tag has been shown to bind streptavidin with an equilibrium dissociation constant of 2.5nM and is readily eluted with biotin under native conditions. Applications Protein purification Because of the mild elution conditions (biotin plus wash buffer) SBP-Tagged proteins can be generated in a relatively pure state with a single purification step. ...
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Protein Tag
Protein tags are peptide sequences genetically grafted onto a recombinant protein. Tags are attached to proteins for various purposes. They can be added to either end of the target protein, so they are either C-terminus or N-terminus specific or are both C-terminus and N-terminus specific. Some tags are also inserted at sites within the protein of interest; they are known as internal tags. Affinity tags are appended to proteins so that they can be purified from their crude biological source using an affinity technique. Affinity tags include chitin binding protein (CBP), maltose binding protein (MBP), Strep-tag and glutathione-S-transferase (GST). The poly(His) tag is a widely used protein tag, which binds to matrices bearing immobilized metal ions. Solubilization tags are used, especially for recombinant proteins expressed in species such as '' E. coli'', to assist in the proper folding in proteins and keep them from aggregating in inclusion bodies. These tags include thiore ...
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Amino Acid
Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although hundreds of amino acids exist in nature, by far the most important are the alpha-amino acids, which comprise proteins. Only 22 alpha amino acids appear in the genetic code. Amino acids can be classified according to the locations of the core structural functional groups, as Alpha and beta carbon, alpha- , beta- , gamma- or delta- amino acids; other categories relate to Chemical polarity, polarity, ionization, and side chain group type (aliphatic, Open-chain compound, acyclic, aromatic, containing hydroxyl or sulfur, etc.). In the form of proteins, amino acid '' residues'' form the second-largest component (water being the largest) of human muscles and other tissues. Beyond their role as residues in proteins, amino acids participate in a number of processes such as neurotransmitter transport and biosynthesis. It is thought that they played a key role in enabling life ...
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Wnt Signaling Pathway
The Wnt signaling pathways are a group of signal transduction pathways which begin with proteins that pass signals into a cell through cell surface receptors. The name Wnt is a portmanteau created from the names Wingless and Int-1. Wnt signaling pathways use either nearby cell-cell communication (paracrine) or same-cell communication (autocrine). They are highly evolutionarily conserved in animals, which means they are similar across animal species from fruit flies to humans. Three Wnt signaling pathways have been characterized: the canonical Wnt pathway, the noncanonical planar cell polarity pathway, and the noncanonical Wnt/calcium pathway. All three pathways are activated by the binding of a Wnt-protein ligand to a Frizzled family receptor, which passes the biological signal to the Dishevelled protein inside the cell. The canonical Wnt pathway leads to regulation of gene transcription, and is thought to be negatively regulated in part by the SPATS1 gene. The noncanonical plana ...
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Biochemical Separation Processes
Biochemistry or biological chemistry is the study of chemical processes within and relating to living organisms. A sub-discipline of both chemistry and biology, biochemistry may be divided into three fields: structural biology, enzymology and metabolism. Over the last decades of the 20th century, biochemistry has become successful at explaining living processes through these three disciplines. Almost all areas of the life sciences are being uncovered and developed through biochemical methodology and research. Voet (2005), p. 3. Biochemistry focuses on understanding the chemical basis which allows biological molecules to give rise to the processes that occur within living cells and between cells,Karp (2009), p. 2. in turn relating greatly to the understanding of tissues and organs, as well as organism structure and function.Miller (2012). p. 62. Biochemistry is closely related to molecular biology, which is the study of the molecular mechanisms of biological phenomena.Astb ...
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Amino Acids
Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although hundreds of amino acids exist in nature, by far the most important are the alpha-amino acids, which comprise proteins. Only 22 alpha amino acids appear in the genetic code. Amino acids can be classified according to the locations of the core structural functional groups, as Alpha and beta carbon, alpha- , beta- , gamma- or delta- amino acids; other categories relate to Chemical polarity, polarity, ionization, and side chain group type (aliphatic, Open-chain compound, acyclic, aromatic, containing hydroxyl or sulfur, etc.). In the form of proteins, amino acid '' residues'' form the second-largest component (water being the largest) of human muscles and other tissues. Beyond their role as residues in proteins, amino acids participate in a number of processes such as neurotransmitter transport and biosynthesis. It is thought that they played a key role in enabling lif ...
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Strep-tag
The Strep-tag system is a method which allows the purification and detection of proteins by affinity chromatography. The Strep-tag II is a synthetic peptide consisting of eight amino acids (Tryptophan, Trp-Serine, Ser-Histidine, His-Proline, Pro-Gln-Phenylalanine, Phe-Glutamic acid, Glu-Lysine, Lys). This peptide sequence exhibits intrinsic affinity towards Strep-Tactin, a specifically engineered streptavidin, and can be N- or C- terminally fused to recombinant proteins. By exploiting the highly specific interaction, ''Strep''-tagged proteins can be isolated in one step from crude cell lysates. Because the ''Strep''-tag elutes under gentle, physiological conditions, it is especially suited for generation of functional proteins. Development and biochemistry of the Strep-tag Streptavidin is a tetrameric protein expressed in ''Streptomyces avidinii''. Because of Streptavidin's high affinity for vitamin H (biotin), Streptavidin is commonly used in the fields of molecular biology a ...
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Surface Plasmon Resonance
Surface plasmon resonance (SPR) is the resonant oscillation of conduction electrons at the interface between negative and positive permittivity material in a particle stimulated by incident light. SPR is the basis of many standard tools for measuring adsorption of material onto planar metal (typically gold or silver) surfaces or onto the surface of metal nanoparticles. It is the fundamental principle behind many color-based biosensor applications and lab-on-a-chip sensors. It should be stressed that SPR is not a resonance on the planar surface and it is a polariton or surface-wave like phenomenon. Explanation The surface plasmon polariton is a non-radiative electromagnetic surface wave that propagates in a direction parallel to the negative permittivity/dielectric material interface. Since the wave is on the boundary of the conductor and the external medium (air, water or vacuum for example), these oscillations are very sensitive to any change of this boundary, such as the adso ...
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Endoplasmic Reticulum
The endoplasmic reticulum (ER) is, in essence, the transportation system of the eukaryotic cell, and has many other important functions such as protein folding. It is a type of organelle made up of two subunits – rough endoplasmic reticulum (RER), and smooth endoplasmic reticulum (SER). The endoplasmic reticulum is found in most eukaryotic cells and forms an interconnected network of flattened, membrane-enclosed sacs known as cisternae (in the RER), and tubular structures in the SER. The membranes of the ER are continuous with the outer nuclear membrane. The endoplasmic reticulum is not found in red blood cells, or spermatozoa. The two types of ER share many of the same proteins and engage in certain common activities such as the synthesis of certain lipids and cholesterol. Different types of cells contain different ratios of the two types of ER depending on the activities of the cell. RER is found mainly toward the nucleus of cell and SER towards the cell membrane or plasma ...
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Protein Phosphatase 2A
Protein phosphatase 2A may refer to: * Protein phosphatase 2 Protein phosphatase 2 (PP2), also known as PP2A, is an enzyme that in humans is encoded by the ''PPP2CA'' gene. The PP2A heterotrimeric protein phosphatase is ubiquitously expressed, accounting for a large fraction of phosphatase activity in eu ..., an enzyme * (myosin-light-chain) phosphatase, an enzyme {{Short pages monitor ...
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Dengue Virus
''Dengue virus'' (DENV) is the cause of dengue fever. It is a mosquito-borne, single positive-stranded RNA virus of the family ''Flaviviridae''; genus ''Flavivirus''. Four serotypes of the virus have been found, a reported fifth has yet to be confirmed,Dwivedi, V. D., Tripathi, I. P., Tripathi, R. C., Bharadwaj, S., & Mishra, S. K. (2017). Genomics, proteomics and evolution of ''Dengue virus''. Briefings in functional genomics.16(4): 217–227, https://doi.org/10.1093/bfgp/elw040 all of which can cause the full spectrum of disease. Nevertheless, scientists' understanding of dengue virus may be simplistic as, rather than distinct antigenic groups, a ''continuum'' appears to exist. This same study identified 47 strains of ''dengue virus''. Additionally, coinfection with and lack of rapid tests for ''zika virus'' and ''chikungunya'' complicate matters in real-world infections. ''Dengue virus'' has increased dramatically within the last 20 years, becoming one of the worst mosquito- ...
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Protein G
Protein G is an immunoglobulin-binding protein expressed in group C and G Streptococcal bacteria much like Protein A but with differing binding specificities. It is a ~60-kDA (65 kDA for strain G148 and 58 kDa for strain C40) cell surface protein that has found application in purifying antibodies through its binding to the Fab and Fc region. The native molecule also binds albumin, but because serum albumin is a major contaminant of antibody sources, the albumin binding site has been removed from recombinant forms of Protein G. This recombinant Protein G, either labeled with a fluorophore or a single-stranded DNA strand, was used as a replacement for secondary antibodies in immunofluorescence and super-resolution imaging. Other antibody binding proteins In addition to Protein G, other immunoglobulin-binding bacterial proteins such as Protein A, Protein A/G and Protein L are all commonly used to purify, immobilize or detect immunoglobulins. Each of these immunoglobulin-binding ...
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Protein A
Protein A is a 42 kDa surface protein originally found in the cell wall of the bacteria ''Staphylococcus aureus''. It is encoded by the ''spa'' gene and its regulation is controlled by DNA topology, cellular osmolarity, and a two-component system called ArlS-ArlR. It has found use in biochemical research because of its ability to bind immunoglobulins. It is composed of five homologous Ig-binding domains that fold into a three-helix bundle. Each domain is able to bind proteins from many mammalian species, most notably IgGs. It binds the heavy chain within the Fc region of most immunoglobulins and also within the Fab region in the case of the human VH3 family. Through these interactions in serum, where IgG molecules are bound in the wrong orientation (in relation to normal antibody function), the bacteria disrupts opsonization and phagocytosis. History As a by-product of his work on type-specific staphylococcus antigens, Verwey reported in 1940 that a protein fraction prepared from ...
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