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Ubiquitin D is a protein that in humans is encoded by the UBD gene, also known as FAT10. [ 5 ] [ 6 ] [ 7 ] UBD acts like ubiquitin , by covalently modifying proteins and tagging them for destruction in the proteasome.
In whole blood (g/cm 3) In plasma or serum (g/cm 3) Water: ... Blood plasma protein ... normal range 2-62 ...
Ubiquitin-binding domains (UBDs) are protein domains that recognise and bind non-covalently to ubiquitin through protein-protein interactions. As of 2019, a total of 29 types of UBDs had been identified in the human proteome. [2] [3] Most UBDs bind to ubiquitin only weakly, with binding affinities in the low to mid μM range.
Ubiquitin is a small protein that exists in all eukaryotic cells. It performs its myriad functions through conjugation to a large range of target proteins. A variety of different modifications can occur. The ubiquitin protein itself consists of 76 amino acids and has a molecular mass of about 8.6 kDa.
The reference range for total protein is typically 60-80g/L. (It is also sometimes reported as "6.0-8.0g/dl"), [ 2 ] but this may vary depending on the method of analysis. Concentrations below the reference range usually reflect low albumin concentration, for instance in liver disease or acute infection .
Reference ranges (reference intervals) for blood tests are sets of values used by a health professional to interpret a set of medical test results from blood samples. Reference ranges for blood tests are studied within the field of clinical chemistry (also known as "clinical biochemistry", "chemical pathology" or "pure blood chemistry"), the ...
Ubiquitin-like proteins (UBLs) are a family of small proteins involved in post-translational modification of other proteins in a cell, usually with a regulatory function. The UBL protein family derives its name from the first member of the class to be discovered, ubiquitin (Ub), best known for its role in regulating protein degradation through covalent modification of other proteins.
Protein degradation is a normal process that removes damaged or unnecessary proteins and helps maintain the normal functions of cells. Ubiquitin protein ligase E3A attaches a small marker protein called ubiquitin to proteins that should be degraded. Cellular structures called proteasomes recognize and digest proteins tagged with ubiquitin.