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  2. Isoelectric point - Wikipedia

    en.wikipedia.org/wiki/Isoelectric_point

    In practice, a protein with an excess of basic aminoacids (arginine, lysine and/or histidine) will bear an isoelectric point roughly greater than 7 (basic), while a protein with an excess of acidic aminoacids (aspartic acid and/or glutamic acid) will often have an isoelectric point lower than 7 (acidic).

  3. Bovine serum albumin - Wikipedia

    en.wikipedia.org/wiki/Bovine_serum_albumin

    Bovine serum albumin (BSA or "Fraction V") is a serum albumin protein derived from cows. It is often used as a protein concentration standard in lab experiments. The nickname "Fraction V" refers to albumin being the fifth fraction of the original Edwin Cohn purification methodology that made use of differential solubility characteristics of plasma proteins.

  4. List of protein subcellular localization prediction tools

    en.wikipedia.org/wiki/List_of_protein_sub...

    BASys (Bacterial Annotation System) is a tool for automated annotation of bacterial genomic (chromosomal and plasmid) sequences including gene/protein names, GO functions, COG functions, possible paralogues and orthologues, molecular weights, isoelectric points, operon structures, subcellular localization, signal peptides, transmembrane regions ...

  5. Globulin - Wikipedia

    en.wikipedia.org/wiki/Globulin

    In the same study, it showed that Bg7S is the protein globulin that is soluble in certain high ionic strength of a salt solution that should have a high isoelectric point as well which should be around 9.05 to 9.26 pI. This type of globulin is found in many different plants such as tomatoes, corn, wheat, and carrots.

  6. Albumin - Wikipedia

    en.wikipedia.org/wiki/Albumin

    The isoelectric point of albumin is 4.7. [8] Alpha-fetoprotein is a fetal plasma protein that binds various cations, fatty acids and bilirubin. Vitamin D-binding protein binds to vitamin D and its metabolites, as well as to fatty acids. Not much is known about afamin. It seems to carry lipidated Wnt proteins and Vitamin E around. [9]

  7. Isoelectric focusing - Wikipedia

    en.wikipedia.org/wiki/Isoelectric_focusing

    Isoelectric focusing (IEF), also known as electrofocusing, is a technique for separating different charged molecules by differences in their isoelectric point (pI). [ 1 ] [ 2 ] It is a type of zone electrophoresis usually performed on proteins in a gel that takes advantage of the fact that overall charge on the molecule of interest is a ...

  8. Difference gel electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Difference_gel_electrophoresis

    The three samples are mixed and loaded onto IEF (isoelectric focusing chromatography) for first dimension and the strip is transferred to a SDS PAGE.After the gel electrophoresis, the gel is scanned with the excitation wavelength of each dye one after the other, so each sample can be seen separately (if we scan the gel at the excitation wavelength of the Cy3 dye, we will see in the gel only ...

  9. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    Knowing the structure of a similar homologous sequence (for example a member of the same protein family) allows highly accurate prediction of the tertiary structure by homology modeling. If the full-length protein sequence is available, it is possible to estimate its general biophysical properties, such as its isoelectric point.