Resources

ABRF Core Community

Collaborate with peers to share strategic advice, solve challenges and develop new approaches.

Contribute to dozens of topical discussions among your ABRF peers ranging from Core Administration and Proteomics and Animal Research and Bioinformatics. The ABRF Core Community is an exclusive home for ABRF members to learn from one another.

Leverage the collective experience and expertise of the entire membership through the All Member Community.

Use your existing ABRF member login credentials to access the Core Community.

The Core Marketplace

The CoreMarketplace (CM) is a searchable list of active core facilities. A Core, broadly defined, is a facility that performs scientific research. Research cores are often (but not always) part of a higher education institution.

The purpose of the CM is to provide this directory of research facilities to the scientific community. It also furthers research by highlighting citable resources within a listing for scientific publication.

Click Here to Search Core MarketPlace

Learn more about the Journal of Biomolecular Techniques.

View Journal

RRIDS

Source by Journal of Biomolecular Techniques

The Research Resource Identification (RRID) Initiative seeks to identify all of the different parts to research and label each one with a unique, citable identifier. This RRID, when published, links directly back to the research component cited making it easier to identify and replicate research findings.

In the partnership with the RRID Initiative, each core research facility can get its own RRID tag that can link a publication citation back to its CoreMarketplace listing. This makes it easier for your facility to get the credit you require to stay compliant with federal grants.

What do you need to get an RRID for your facility? We ask for three things:

A unique name. Choose a name for your core listing that applies specifically to your facility. Pre-pending the name or the initials of your institution to your facility is a good idea. "Genomics Core" is too generic a name. "UVM-Genomics Core" is much more specific.
An institution. Make sure your institution is selected in your listing. For those facilities that aren't part of an educational institution, choose "Private Company."
A current webpage. Make sure the URL to your facility webpage is current. We have seen a lot of old links that lead to error pages because web pages moved or were merged into organization. We need to see that the URL leads to a page that represents your facility.

When your facility page is updated, the data is sent over to the RRID database on your behalf. RRID tags are usually assigned within a couple of days and will automatically be added to your listing.

When your listing has an RRID assigned, you will see something like this added to your page.

Facility RRID, RRID: SCR_018206 CITE THIS

The RRID itself is cross-linked to the RRID Resource site (link below). The Cite This link creates a pop-up field containing the full citable link to your facility. It can easily be copied and pasted into a publication.

(We also have a field for grant numbers that perform a similar function. You can find this in your Edit page.)

You can learn more about the RRID initiative here

USEDIT

The Universal Scientific Equipment Discovery Tool (USEDit) is a universal database of scientific equipment. Each instrument entry contains a wealth of information about the product, its capabilities, and its own RRID. This makes the instrument itself citable in research publication. We partnered with USEDit to bring that into the CoreMarketplace.

Vermont Biomedical Research Network

More Features

We have included a number a new features into the Core Marketplace. Here's two:

Locating Core Facilities can be difficult. We provide a central repository to allow researchers and Core Facilities to more easily find each other. Researchers can quickly locate facilities that provide the services they need. Core Facilities can locate other such facilities to collaborate with and gain more users. This may help achieve sustainability.

Benefits:

Allows researchers to locate resources needed for their research
Provides a channel for facilities to collaborate
Facilitates cores to get the traffic needed to reach sustainability

The Vermont Genetics Network, in partnership with ABRF, established the Core Marketplace database to track and explore research services and technologies that are regionally accessible. This will allow researchers to find established facilities and avoid duplicating resources that are not cost effective at their own site.

Resources for Scientists

Delta Mass

A DATABASE OF PROTEIN POST TRANSLATIONAL MODIFICATIONS

Contributors
Please send new data or corrections to
info@abrf.org

The ABRF accepts no responsibility for the accuracy of these data which are freely donated by individuals.

Average Masses

Avg. Mass Change	Modification
-79	5' dephospho
-58	Desmosine (from Lysine)
-48	decomposed carboxymethylated Methionine
-44	Decarboxylation of gamma carboxy Glutamate
-43	Gamma-glutamyl semialdehyde (from arginine)
-42	Ornithine (from Arginine)
-34	Lysinoalanine (from Cysteine)
-34	Lanthionine (from Cysteine)
-34	Dehydroalanine (from Cysteine)
-30	Homoserine formed from Met by CNBr treatment
-27	Oxidation of arginine (to glutamic acid)
-18	Formylglycine (from cysteine)
-18	Pyroglutamic Acid formed from Glutamic Acid
-18	Dehydration (-H2O)
-18	S-gamma-Glutamyl (crosslinked to Cysteine)
-18	O-gamma-Glutamyl- (Crosslink to Serine)
-18	Serine to Dehydroalanine
-18	Alaninohistidine (Serine crosslinked to theta or pi carbon of Histidine)
-18	Misincorporation of Norleucine for Methionine
-18	Succinimide formation from aspartic acid
-17	Pyroglutamic Acid formed from Gln
-17	N-pyrrolidone carboxyl (N terminus)
-17	N alpha -(gamma-Glutamyl)-lysine
-17	N-(beta-Aspartyl)-Lysine (Crosslink)
-17	Succinimide formation from asparagine
-17	S-carbamoylmethylcysteine cyclization (N-terminus)
-16	Pyruvoyl- (Serine)
-5	Crosslink between Arg and His sidechains
-4	3,3',5,5'-TerTyr (Crosslink)
-2	Formylglycine (from serine)
-2	Disulphide bond formation (Cystine)
-2	S-(2-Histidyl)- (Crosslinked to Cysteine)
-2	S-(3-Tyr) (Crosslinked to Cysteine)
-2	3,3'-BiTyr (Crosslink)
-2	IsodiTyr (Crosslink)
-1	Allysine (from Lysine)
-1	Amide formation (C terminus)
-1	Oxidation of lysine (to aminoadipic semialdehyde)
1	Deamidation of Asparagine and Glutamine to Aspartate and Glutamate
1	Citruline (from Arginine)
2	Cysteine x2, reduction of Cystine (Cys-Cys)
2	Reduction of indole double bond of Trp
4	Oxidation of Trp to kynurenine
12	Lysine epsilon amino to imine
12	Cysteine (N-term) formaldehyde adduct (Cys to Thioproline conversion)
12	Formaldehyde adduct of Trp
13	Syndesine (from Lysine)
13	CM-Cys vs PAM-Cys
14	Methylation (N terminus, N epsilon of Lysine, O of Serine, Threonine or C terminus, N of Asparagine)
14	CAM-Cys vs PAM-Cys
14	Methylation (methyl esterification of Asp and Glu side chains)
15	Delta-Hydroxy-allysine (from Lysine)
15	Oxidation of lysine (to aminoadipic acid)
16	Hydroxylation (of delta C of Lysine, beta C of Tryptophan, C3 or C4 of Proline, beta C of Aspartate)
16	Oxidation of Methionine (to Sulphoxide)
16	3,4-Dihydroxy-Phenylalanine (from Tyrosine) (DOPA)
16	Oxohistidine (from histidine)
16	Sulfenic Acid (from Cysteine)
16	Oxidation of proline (to gamma-glutamyl semialdehyde)
22	Sodium
28	Ethyl
28	N,N dimethylation (of Arginine or Lysine)
28	2,4-BisTrp-6,7-dione (from Tryptophan)
28	Formylation (CHO)
30	6,7 Dione (from Tryptophan)
32	3,4,6-Trihydroxy-Phenylalanine (from Tyrosine) (TOPA)
32	3,4-Dihydroxylation (of Proline)
32	Oxidation of Methionine (to Sulphone)
32	Oxidation of proline (to glutamic acid)
32	Double oxidation of Trp
32	Trisulfide bond (additional sulfur in disulfide bond)
34	3-Chlorination (of Tyrosine with 35Cl)
36	3-Chlorination (of Tyrosine with 37Cl)
38	Potassium
42	Acetylation (N terminus, N epsilon of Lysine, O of Serine) (Ac)
42	N-Trimethylation (of Lysine)
43	Carbamylation
44	disodium
45	Nitro (NO2)
46	beta-Methylthio-aspartic acid
48	Cysteic acid, oxidation of cysteine
51	Piperidine adduct to C-terminal Cys
56	t-butyl ester(OtBu) and t-butyl (tBu)
57	Glycyl (-G-,-Gly-)
57	Carboxamidomethyl (on Cysteine and other residues)
58	Carboxymethyl (on Cysteine and other residues)
60	sodium + potassium
64	Selenocysteine (from Serine)
67	Asp transamidation with piperidine
68	3,5-Dichlorination (of Tyrosine with 35Cl)
69	Dehydroalanine (Dha)
70	3,5-Dichlorination (of Tyrosine with mixture of 35Cl and 37Cl))
70	Pyruvate
71	Sarcosyl
71	Alanyl (-A-, -Ala-)
71	Acetamidomethyl (Acm)
71	Propionamide or Acrylamide adduct
72	3,5-Dichlorination (of Tyrosine with 37Cl)
74	S-(sn-1-Glyceryl) (on Cysteine)
74	Glycerol Ester (on Glutamic acid side chain)
75	Glycine (G, Gly)
76	Phenyl ester (OPh) (on acidic)
76	Beta mercaptoethanol adduct
78	3-Bromination (of Tyrosine with 79Br)
78	3-o-bromination of Phe with 79Br
80	L-o-bromination of Phe with 81Br
80	Sulphonation (SO3H) (of PMC group)
80	Sulphation (of O of Tyrosine)
80	Phosphorylation (O of Serine, Threonine, Tyrosine and Aspartate, N epsilon of Lysine)
80	3-Bromination (of Tyrosine with 81Br)
82	Cyclohexyl ester (OcHex)
83	Dehydroamino butyric acid (Dhb)
83	Homoseryl lactone
85	2-Aminobutyric acid (Abu)
85	2-Aminoisobutyric acid (Aib)
85	Gamma Aminobutyryl
86	t-butyloxymethyl (Bum)
86	Diaminopropionyl
87	N-(4-NH2-2-OH-butyl)- (of Lysine) (Hypusine)
87	Seryl (-S-, -Ser-)
88	t-butylsulfenyl (StBu)
89	Alanine (A, Ala)
89	Sarcosine (Sar)
90	Anisyl
90	Benzyl (Bzl) and benzly ester (OBzl)
93	1,2-ethanedithiol (EDT)
95	Dehydroprolyl
96	Trifluoroacetyl (TFA)
97	N-hydroxysuccinimide (ONSu, OSu)
97	Prolyl (-P-, -Pro-)
98	Cysteic acid x2, oxidation of cystine
98	Tetramethylguanidinium termination by-product on amine
98	Phosphate/sulphate adduct of proteins
99	Valyl (-V-, -Val-)
99	Isovalyl (-I-,-Iva-)
100	t-Butyloxycarbonyl (tBoc)
101	Threoyl (-T-, -Thr-)
101	Homoseryl (-Hse-)
103	Cystyl (-C-, -Cys-)
104	4-Methylbenzyl (Meb)
104	Benzoyl (Bz)
105	Serine (S, Ser)
105	Pyridylethylation of cysteine
106	HMP (hydroxymethylphenyl) linker
106	Thioanisyl
106	Thiocresyl
111	2-Piperidinecarboxylic acid (Pip)
111	Pyroglutamyl
113	Hydroxyprolyl (-Hyp-)
113	Isoleucyl (-I-, -Ile-)
113	Leucyl (-L-, -Leu-)
113	Norleucyl (-Nle-)
114	Asparagyl (-N-, -Asn-)
114	t-amyloxycarbonyl (Aoc)
114	Ornithyl (-Orn-)
115	Proline (P, Pro)
115	Aspartyl (-D-, -Asp-)
117	Succinyl
117	Valine (V, Val)
117	Hydroxybenzotriazole ester (HOBt)
118	Dimethylbenzyl (diMeBzl)
119	Threonine (T, Thr)
119	Cysteinylation
120	Benzyloxymethyl (Bom)
120	p-methoxybenzyl (Mob, Mbzl)
121	4-Nitrophenyl, p-Nitrophenyl (ONp)
121	Cysteine (C, Cys)
125	Chlorobenzyl (ClBzl)
126	Iodination (of Histidine[C4] or Tyrosine[C3])
126	octanoylation
128	Glutamyl (-Q-, -Gln-)
128	Lysyl (-K-, -Lys-)
129	Glutamyl (-E-, -Glu-)
129	O-Methyl Aspartamyl
130	N alpha -(gamma-Glutamyl)-Glu
131	Norleucine (Nle)
131	Hydroxyproline (Hyp)
131	Isoleucine (I, Ile)
131	Leucine (L, Leu)
131	Methionyl (-M-, -Met-)
131	Hydroxy Aspartamyl
131	bb-dimethyl Cystenyl
132	Asparagine (N, Asn)
132	Pentoses (Ara, Rib, Xyl)
133	Aspartic Acid (D, Asp)
134	Benzyloxycarbonyl (Z)
134	Adamantyl (Ada)
135	p-Nitrobenzyl ester (ONb)
137	Histidyl (-H-, -His-)
142	N-methyl Glutaminyl
142	N-methyl Lysyl
143	O-methyl Glutamyl
143	Diphthamide (from Histidine)
144	Hydroxy Lysyl (-Hyl-)
145	Methyl Methionyl
146	Glutamine (Q, Gln)
146	Deoxyhexoses (Fuc, Rha)
146	Lysine (K, Lys)
146	Pentosyl
146	Aminoethyl Cysteinyl (AECys)
147	4-Glycosyloxy- (pentosyl,C5) (of Proline)
147	Glutamic Acid (E, Glu)
147	Phenylalanyl- (-F-, -Phe-)
147	Methionyl Sulfoxide
148	Pyridyl Alanyl
149	2-Nitrobenzoyl (NBz)
149	Methionine (M, Met)
149	Fluorophenylalanyl
150	Dimethoxybenzyl Trp
153	2-Nitrophenylsulphenyl (Nps)
154	4-Toluenesulphonyl (Tosyl, Tos)
154	3-nitro-2-pyridinesulfenyl (Npys)
155	Histidine (H, His)
156	3,5-Dibromination (of Tyrosine with 79Br)
156	Arginyl (-R-, -Arg-)
157	Citrulline
158	3,5-Dibromination (of Tyrosine with mixture of 79Br and 81Br)
159	Dichlorobenzyl (Dcb)
160	3,5-Dibromination (of Tyrosine with 81Br)
160	Carboxyamidomethyl Cystenyl
161	Hexosamines (GalN, GlcN)
161	Carboxymethyl cysteine (Cmc)
161	Carboxymethyl Cystenyl
161	Methylphenylalanyl
162	Inositol
162	N-Glucosyl (N terminus or N epsilon of Lysine) (Aminoketose)
162	O-Glycosyl- (to Serine or Threonine)
162	Linker attached to peptide in Fmoc peptide synthesis
162	Hexoses (Fru, Gal, Glc, Man)
163	Tyrosinyl (-Y-, -Tyr-)
163	MethionylSulphone
165	Phenylalanine (F, Phe)
166	2,4 -dinitrophenyl (Dnp)
166	Pentaflourophenyl (Pfp)
166	Diphenylmethyl (Dpm)
167	Phospho Seryl
169	2-Chlorobenzyloxycarbonyl (ClZ)
169	Napthyl acetyl
170	N-acetyl Lysyl
170	N-methyl Arginyl
170	Decanoic acid modification of Cys in active site
172	Ethanedithiol/TFA cyclic adduct
173	Carboxy Glutamyl (Gla)
174	Arginine (R, Arg)
174	Acetamidomethyl Cystenyl
174	Acrylamidyl Cystenyl
176	N-Glucuronyl (N terminus)
177	delta-Glycosyloxy- (of Lysine) or beta-Glycosyloxy- (of Phenylalanine or Tyrosine)
177	4-Glycosyloxy- (hexosyl,C6) (of Proline)
177	Benzyl Seryl
177	N-methyl Tyrosinyl
178	a-N-Gluconoylation (His Tagged proteins)
179	p-Nitrobenzyloxycarbonyl (4Nz)
179	2,4,5-Trichlorophenyl
180	2,4,6-trimethyloxybenzyl (Tmob)
180	Xanthyl (Xan)
181	Tyrosine (Y, Tyr)
182	Chlorophenylalanyl
182	Mesitylene-2-sulfonyl (Mts)
183	AEBSF
184	Isopropyl Lysyl
186	Tryptophanyl (-W-, - Trp-)
186	Carboxymethyl Lysyl
188	N-Lipoyl- (on Lysine)
190	Matrix alpha cyano MH+
191	Benzyl Threonyl
193	Benzyl Cystenyl
197	Napthyl Alanyl
198	Succinyl Aspartamyl
201	HMP (hydroxymethylphenyl)/TFA adduct
203	N-acetylhexosamines (GalNAc, GlcNAc)
204	Tryptophan (W, Trp)
204	Cystine ((Cys)2)
204	Farnesylation
206	S-Farnesyl-
206	Myristoylation-4H (2 double bonds)
208	Myristoleylation (myristoyl with one double bond)
208	Pyridylethyl Cystenyl
210	Myristoylation
212	4-Methoxy-2,3,6-trimethylbenzenesulfonyl (Mtr)
213	2-Bromobenzyloxycarbonyl (BrZ)
214	Formyl Tryptophanyl
219	Benzyl Glutamyl
219	Anisole Adducted Glutamyl
222	9-Fluorenylmethyloxycarbonyl (Fmoc)
222	S-cystenyl Cystenyl
226	Biotinylation (amide bond to lysine)
226	Dimethoxybenzhydryl (Mbh)
229	N-Pyridoxyl (on Lysine)
231	Pyridoxal phosphate (Schiff Base formed to lysine)
233	Dansyl (Dns)
233	Nicotinyl Lysyl
238	2-(p-biphenyl)isopropyl-oxycarbonyl (Bpoc)
238	Palmitoylation
242	Triphenylmethyl (Trityl, Trt)
243	Tyrosinyl Sulphate
243	Phospho Tyrosinyl
252	Pbf (pentamethyldihydrobenzofuransulfonyl)
252	3,5-Diiodination (of Tyrosine)
258	a-N-6-Phosphogluconoylation (His Tagged proteins)
259	N alpha -(gamma-Glutamyl)-Glu2
266	Stearoylation
266	Pmc (2,2,5,7,8- Pentamethylchroman-6-sulphonyl)
272	Geranylgeranylation
272	Monomethoxytrityl
276	S-Geranylgeranyl
283	O-GlcNAc-1-phosphorylation (of Serine)
289	5'phos dCytidinyl
289	iodo Tyrosinyl
290	Aldohexosyl Lysyl
291	Sialyl
291	N-acetylneuraminic acid (Sialic acid, NeuAc, NANA, SA)
304	5'phos dThymidinyl
305	5'phos Cytidinyl
305	Glutathionation
306	O-Uridinylylation (of Tyrosine)
306	5'phos Uridinyl
307	N-glycolneuraminic acid (NeuGc)
307	S-farnesyl Cystenyl
313	5'phos dAdenosyl
324	O-pantetheinephosphorylation (of Serine)
327	SucPhencarb Lysyl
329	5'phos dGuanosyl
329	5'phos Adenosinyl
329	O-5'-Adenosylation ( of Tyrosine)
339	4'-Phosphopantetheine
342	S-palmityl Cystenyl
345	5'phos Guanosyl
354	Biotinyl Lysyl
359	Fluorescein labelling of peptide N-terminal using NHS ester
365	Hex-HexNAc
388	N alpha -(gamma-Glutamyl)-Glu3
391	Dioctyl Phthalate
395	PMC Lysyl
409	Aedans Cystenyl
413	Dioctyl Phthalate Sodium Adduct
415	di-iodo Tyrosinyl
423	PMC Arginyl
454	S-Coenzyme A
457	AMP Lysyl
470	3,5,3'-Triiodothyronine (from Tyrosine)
524	S-(sn-1-Dipalmitoyl-glyceryl)- (on Cysteine)
541	S-(ADP-ribosyl)- (on Cysteine)
541	N-(ADP-ribosyl)- (on Arginine)
541	O-ADP-ribosylation (on Glutamate or C terminus)
541	ADP-rybosylation (from NAD)
587	S-Phycocyanobilin (on Cysteine)
617	S-Heme (on Cysteine)
648	N theta -(ADP-ribosyl) diphthamide (of Histidine)
657	NeuAc-Hex-HexNAc
783	O-8 alpha-Flavin [FAD])- (of Tyrosine)
784	S-(6-Flavin [FAD])- (on Cysteine)
784	N theta and N pi-(8alpha-Flavin) (on Histidine)
893	(Hex)3-HexNAc-HexNAc
1,039	(Hex)3-HexNAc-(dHex)HexNAc