Editing Proteomics (section)

===Current research methodologies===
Fluorescence two-dimensional differential gel electrophoresis (2-D DIGE)<ref name=Tonge01/> may be used to quantify variation in the 2-D DIGE process and establish statistically valid thresholds for assigning quantitative changes between samples.<ref name=Tonge01>{{cite journal | vauthors = Tonge R, Shaw J, Middleton B, Rowlinson R, Rayner S, Young J, Pognan F, Hawkins E, Currie I, Davison M | display-authors = 6 | title = Validation and development of fluorescence two-dimensional differential gel electrophoresis proteomics technology | journal = Proteomics | volume = 1 | issue = 3 | pages = 377–396 | date = March 2001 | pmid = 11680884 | doi = 10.1002/1615-9861(200103)1:3<377::AID-PROT377>3.0.CO;2-6 | s2cid = 22432028 }}</ref>

Comparative proteomic analysis may reveal the role of proteins in complex biological systems, including reproduction. For example, treatment with the insecticide triazophos causes an increase in the content of brown planthopper (''Nilaparvata lugens'' (Stål)) male accessory gland proteins (Acps) that may be transferred to females via mating, causing an increase in fecundity (i.e. birth rate) of females.<ref>{{cite journal | vauthors = Wang LP, Shen J, Ge LQ, Wu JC, Yang GQ, Jahn GC |title=Insecticide-induced increase in the protein content of male accessory glands and its effect on the fecundity of females in the brown planthopper, ''Nilaparvata lugens'' Stål (Hemiptera: Delphacidae)  |journal=Crop Protection |volume=29 |issue=11 |pages=1280–5 |date=November 2010 |doi=10.1016/j.cropro.2010.07.009 |bibcode=2010CrPro..29.1280W }}</ref> To identify changes in the types of accessory gland proteins (Acps) and reproductive proteins that mated female planthoppers received from male planthoppers, researchers conducted a comparative proteomic analysis of mated ''N. lugens'' females.<ref name="Ge et al 2011">{{cite journal | vauthors = Ge LQ, Cheng Y, Wu JC, Jahn GC | title = Proteomic analysis of insecticide triazophos-induced mating-responsive proteins of Nilaparvata lugens Stål (Hemiptera: Delphacidae) | journal = Journal of Proteome Research | volume = 10 | issue = 10 | pages = 4597–4612 | date = October 2011 | pmid = 21800909 | doi = 10.1021/pr200414g }}</ref> The results indicated that these proteins participate in the reproductive process of ''N. lugens'' adult females and males.<ref name="Ge et al 2011" />

Proteome analysis of ''Arabidopsis peroxisomes''<ref name=Reumann11/> has been established as the major unbiased approach for identifying new peroxisomal proteins on a large scale.<ref name=Reumann11>{{cite journal | vauthors = Reumann S | title = Toward a definition of the complete proteome of plant peroxisomes: Where experimental proteomics must be complemented by bioinformatics | journal = Proteomics | volume = 11 | issue = 9 | pages = 1764–1779 | date = May 2011 | pmid = 21472859 | doi = 10.1002/pmic.201000681 | s2cid = 20337179 }}</ref>

There are many approaches to characterizing the human proteome, which is estimated to contain between 20,000 and 25,000 non-redundant proteins. The number of unique protein species likely will increase by between 50,000 and 500,000 due to RNA splicing and proteolysis events, and when post-translational modification also are considered, the total number of unique human proteins is estimated to range in the low millions.<ref>{{cite journal | vauthors = Uhlen M, Ponten F | title = Antibody-based proteomics for human tissue profiling | journal = Molecular & Cellular Proteomics | volume = 4 | issue = 4 | pages = 384–393 | date = April 2005 | pmid = 15695805 | doi = 10.1074/mcp.R500009-MCP200 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Jensen ON | title = Modification-specific proteomics: characterization of post-translational modifications by mass spectrometry | journal = Current Opinion in Chemical Biology | volume = 8 | issue = 1 | pages = 33–41 | date = February 2004 | pmid = 15036154 | doi = 10.1016/j.cbpa.2003.12.009 }}</ref>

In addition, the first promising attempts to decipher the proteome of animal tumors have recently been reported.<ref name="Klopfleisch1"/>
This method was used as a functional method in ''[[Macrobrachium rosenbergii]]'' protein profiling.<ref name="Alinejad_2015">{{cite journal | vauthors = Alinejad T, Bin KQ, Vejayan J, Othman RY, Bhassu S | title = Proteomic analysis of differentially expressed protein in hemocytes of wild giant freshwater prawn Macrobrachium rosenbergii infected with infectious hypodermal and hematopoietic necrosis virus (IHHNV) | journal = Meta Gene | volume = 5 | issue = | pages = 55–67 | date = September 2015 | pmid = 26106581 | pmc = 4473098 | doi = 10.1016/j.mgene.2015.05.004 }}</ref>