Recombinant Human RCL protein is a Human Full Length protein, in the 1 to 174 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, MS.
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Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application MS | Reactivity Reacts | Dilution info - | Notes - |
Part of a nucleotide salvage pathway that eliminates epigenetically modified 5-hydroxymethyl-dCMP (hmdCMP) in a two-step process entailing deamination to cytotoxic 5-hydroxymethyl-dUMP (hmdUMP), followed by its hydrolysis into 5-hydroxymethyluracil (hmU) and 2-deoxy-D-ribose 5-phosphate (deoxyribosephosphate) (PubMed:33833118). Catalyzes the second step in that pathway, the hydrolysis of the N-glycosidic bond in hmdUMP, degrading this cytotoxic nucleotide to avoid its genomic integration (PubMed:33833118).
C6orf108, RCL, DNPH1, 5-hydroxymethyl-dUMP N-hydrolase, 2'-deoxynucleoside 5'-phosphate N-hydrolase 1, c-Myc-responsive protein RCL
Recombinant Human RCL protein is a Human Full Length protein, in the 1 to 174 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, MS.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.316% Tris HCl, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
ab100943 was purified using conventional chromatography techniques.
Part of a nucleotide salvage pathway that eliminates epigenetically modified 5-hydroxymethyl-dCMP (hmdCMP) in a two-step process entailing deamination to cytotoxic 5-hydroxymethyl-dUMP (hmdUMP), followed by its hydrolysis into 5-hydroxymethyluracil (hmU) and 2-deoxy-D-ribose 5-phosphate (deoxyribosephosphate) (PubMed:33833118). Catalyzes the second step in that pathway, the hydrolysis of the N-glycosidic bond in hmdUMP, degrading this cytotoxic nucleotide to avoid its genomic integration (PubMed:33833118).
Belongs to the 2'-deoxynucleoside 5'-phosphate N-hydrolase 1 family.
The reactive center loop (RCL) is an important structural element found in serpins including alpha-1 antitrypsin. It functions by acting as a bait for target proteases and then trapping them modifying their activity in proteolytic cascade reactions. The RCL's standard molecular mass is around 10 kDa but it is most often part of larger serpin proteins. RCLs are found in a variety of tissues prominently in the liver where they play a role in regulating enzymes in the blood.
The reactive center loop operates by temporarily interacting with proteases to regulate their activities. It often finds itself as a component of a serpin-protease complex where it changes the enzymatic activity. This precise control allows proper regulation of proteolytic pathways that manage diverse physiological processes including inflammation and coagulation.
Reactive center loops engage in the regulation of two main pathways: the coagulation cascade and the inflammatory response pathway. In these pathways RCLs work closely with proteins like thrombin and plasminogen to maintain a balance between enzyme activation and inhibition. Through these interactions RCLs help modulate the clot formation and dissolution as well as inflammatory response to injury.
Reactive center loops have ties to alpha-1 antitrypsin deficiency and emphysema. Aberrant RCL function can lead to inefficient enzyme inhibition contributing to these conditions. The protein alpha-1 antitrypsin which includes the RCL when mutated or deficient can result in unregulated neutrophil elastase activity causing tissue damage and related respiratory conditions.
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15% SDS-PAGE showing ab100943 at approximately 21.2kDa (3µg).
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