Unsealed tracers

Feasibility review

Sulfur-35 for research

The label for newly made proteins, G protein activation and sharp autoradiographs.

Half-life
87.37 days
Beta max
167.3 keV
Decay
Beta minus to Cl-35
Exempt quantity
100 µCi
Request an S-35 feasibility review

Request a feasibility review for S-35

No license file needed to ask. A scientist reads every request and replies with the next step.

How ordering works
S-35 at a glanceIAEA evaluated data
aSIMULATED BETA SPECTRUM050100150200Energy (keV)Electrons per keVEndpoint 167.3 keVMean 48.76 keVb06121824050100Time (months)Activity (%)T½ 87.37 d6% left after 1 year
a Energy of the emitted beta particles, calculated from the IAEA endpoint energy; dashed line: mean energy. b Activity left after the reference date. Data: IAEA [1]

Research applications

Where S-35 does the work.

Figures are simulated examples of each measurement.

  • aSIMULATED060120180240300Chase (min)050100% of maximum label140 kDa precursor160 kDa mature form

    Cell biology

    Pulse-chase of new proteins2, 3

    A short pulse of [³⁵S]methionine and cysteine labels only the proteins a cell makes in those minutes.

    More: Pulse-chase of new proteins

    A chase with unlabeled methionine then follows that group of proteins as it folds, matures, moves through the cell or is degraded.

    In a classic study, only about 25 percent of the newly made precursor of the membrane protein CFTR matured; the rest was degraded with a half-time of about 33 minutes.

  • bSIMULATED10⁻⁹10⁻⁷10⁻⁵10⁻³Dopamine (M)03060Over basal (%)D2 shortD2 longno receptor

    Pharmacology

    G protein activation4, 5, 6

    [³⁵S]GTPγS measures how strongly a ligand activates a G protein-coupled receptor.

    More: G protein activation

    An activated receptor makes its G protein exchange GDP for GTP. The non-hydrolyzable analog [³⁵S]GTPγS builds up on activated G proteins in cell membranes.

    Dopamine raised binding about 62 percent over basal through D2 receptors expressed in CHO cells, and not at all in cells without the receptor.

  • cSIMULATED071421Exposure (days)Signalfilmemulsionfilm range1 day film = 5 days emulsion

    Neuroscience

    In situ hybridization7, 8

    ³⁵S-labeled RNA probes show where a gene is expressed in tissue sections.

    More: In situ hybridization

    X-ray film maps the signal across a section in about 1 to 7 days. Photographic emulsion on the slide gives cell-level detail in one to several weeks; a day on film gives about the signal of 5 days under emulsion.

    Signal rises linearly with the amount of target mRNA, so sections can be compared quantitatively.

  • dSIMULATED³²PGATC³⁵SGATCSame sequencing reactions, two labels

    Molecular biology

    Sharper autoradiographs9

    ³⁵S gives sharper bands than ³²P, because its betas travel a shorter distance.

    More: Sharper autoradiographs

    In dideoxy sequencing, switching the label from ³²P to ³⁵S sharpened the bands and raised the resolution. Exposures ran 1.5 to 2 times longer.

  • eSIMULATEDuntreatednuclease-treated lysatenonenonemRNA 1mRNA 2200976645312114kDaReticulocyte lysate, 30 min at 30 °C

    Biochemistry

    Cell-free protein synthesis10, 11

    [³⁵S]methionine marks the proteins a reticulocyte lysate makes from added mRNA.

    More: Cell-free protein synthesis

    Nuclease treatment removes the lysate's own mRNA, so it translates only what you add, into full-size products of up to about 200 kDa. The labeled products are read on a gel by autoradiography.

  • fSIMULATED050100³⁵S incorporated (%)100%control10%chondroitin35%heparanWith 30 mM chlorate

    Glycobiology

    Sulfation of proteins and proteoglycans12, 13, 14

    Cells take up [³⁵S]sulfate and use it to sulfate proteins and proteoglycans.

    More: Sulfation of proteins and proteoglycans

    Tyrosine sulfation, found in every cell type and tissue examined, is traced this way.

    In endothelial cells, 30 mM chlorate cut chondroitin sulfation to 10 percent and heparan sulfation to 35 percent of controls.

Forms

S-35 forms researchers ask for

Every form is confirmed with its manufacturer before you order.

  • [³⁵S]methionine and cysteine

    Labeled amino acids in solution

    Metabolic labeling and pulse-chase

    Feasibility review
  • [³⁵S]GTPγS

    Labeled nucleotide analog in solution

    G protein activation assays

    Feasibility review
  • ³⁵S-labeled nucleotides

    For example UTP labeled with ³⁵S, in solution

    RNA probes for in situ hybridization

    Feasibility review
  • [³⁵S]sulfate

    Sodium sulfate in aqueous solution

    Sulfation labeling

    Feasibility review

Activity, certificate and lead time are set with the manufacturer at quote.

Before you order

Plan for decay and licensing.

Plan around decay

S-35 has a half-life of 87.37 days and loses about 5.4 percent of its activity each week. Ask for the activity you need on the day you start using it.

Activity remaining after
  1. 30 days78.8%
  2. 90 days49%
  3. 6 months24%
  4. 1 year5.5%

Licensing

Exempt quantityNeeds a license100 µCi
Activity of one vial, log scale

A single quantity of S-35 at or below 100 µCi is an exempt quantity under 10 CFR 30.71, Schedule B. Above that, your institution needs a license that covers it.

  • Combining exempt quantities to exceed the limit is not covered.
  • Sulfur-35 betas travel about 26 cm in air and 0.3 mm in water, so millicurie amounts need no shielding. Liquid scintillation counting is the best readily available way to count its wipe tests.
  • Labeled amino acids give off small amounts of volatile ³⁵S, especially when vials are thawed and labeled cultures are incubated. Vent thawing vials in a hood through charcoal, and vent incubated cultures through charcoal filter paper.
  • Agreement States apply equivalent rules. Your RSO reviews the exact material before you order.

Sources: 15, 16, 17

Start a request

Request a feasibility review for S-35.

No license file needed to ask. A scientist reads every request and replies with the next step.

  1. Name the compoundGive the labeled molecule, the specific activity and the amount you need.
  2. Plan for volatilityLabeled amino acids release a little volatile ³⁵S; have a hood and charcoal traps ready.
  3. Time the experimentActivity halves about every three months.
  1. 01Need
  2. 02Details
  3. 03Contact
Where are you starting?

You get Feasibility reply and a candidate supplier path

Decay data

S-35 decay data

Decay schemeS-35 to Cl-35
35S87.37 dQ 167.322 keV35Cl0β− 100%
Energies in keV, with emission probability per decay. Levels not to scale. Data: IAEA [1]
Half-life
87.37 days ± 0.04
Decay mode
Beta minus (100%)
Daughter
Cl-35
Decay energy (Q)
167.322 keV
S-35 emissions
RadiationEnergy (keV)Per 100 decays
Beta167.3 max, 48.8 mean100

Source: IAEA LiveChart of Nuclides, ENSDF evaluation by JUN CHEN and JOHN CAMERON AND BALRAJ SINGH (literature cutoff 20 October 2011), retrieved 25 September 2026 [1]. Reference values; a manufacturer's certificate states the activity of a specific lot.

Questions, answered

S-35 questions

How long does sulfur-35 last?

Its half-life is 87.37 days, so it loses about 5.4 percent a week and about half remains after three months.

Can we buy sulfur-35 without a radioactive materials license?

For small amounts, possibly. A single quantity of S-35 at or below 100 microcuries is an exempt quantity under 10 CFR 30.71, and a distributor licensed under 10 CFR 32.18 can supply exempt quantities to users without a license. Larger amounts need a license that covers them. Your RSO decides how your institution handles each case.

Is labeled methionine volatile?

Slightly. Labeled methionine and cysteine release small amounts of volatile ³⁵S, most when vials are thawed and labeled cultures are incubated. Thaw vials in a hood and trap the vapor with charcoal.

Why use sulfur-35 rather than phosphorus-32 for autoradiography?

Its betas travel a shorter distance, so bands are sharper, and its weaker emission lowers the dose during handling. Exposures take about 1.5 to 2 times longer.

How is sulfur-35 detected?

By liquid scintillation counting, including wipe tests of work surfaces.

Which forms do labs ask for?

[³⁵S]methionine and cysteine for labeling proteins, [³⁵S]GTPγS for G protein assays, ³⁵S-labeled UTP for RNA probes, and [³⁵S]sulfate for sulfation.

More isotopes

Sources

References

  1. IAEA Nuclear Data Section. LiveChart of Nuclides, S-35 decay data (ENSDF evaluation). Retrieved 25 September 2026. www-nds.iaea.org/relnsd/vcharthtml/VChartHTML.html
  2. Simon E, Kornitzer D. Pulse-chase analysis to measure protein degradation. Methods Enzymol. 2014;536:65-75. doi.org/10.1016/B978-0-12-420070-8.00006-4
  3. Ward CL, Kopito RR. Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins. J Biol Chem. 1994;269(41):25710-25718. doi.org/10.1016/S0021-9258(18)47306-1
  4. Harrison C, Traynor JR. The [35S]GTPγS binding assay: approaches and applications in pharmacology. Life Sci. 2003;74(4):489-508. doi.org/10.1016/j.lfs.2003.07.005
  5. Strange PG. Use of the GTPγS ([35S]GTPγS and Eu-GTPγS) binding assay for analysis of ligand potency and efficacy at G protein-coupled receptors. Br J Pharmacol. 2010;161(6):1238-1249. doi.org/10.1111/j.1476-5381.2010.00963.x
  6. Gardner B, Hall DA, Strange PG. Pharmacological analysis of dopamine stimulation of [35S]-GTPγS binding via human D2short and D2long dopamine receptors expressed in recombinant cells. Br J Pharmacol. 1996;118(6):1544-1550. doi.org/10.1111/j.1476-5381.1996.tb15572.x
  7. Simmons DM, Arriza JL, Swanson LW. A complete protocol for in situ hybridization of messenger RNAs in brain and other tissues with radio-labeled single-stranded RNA probes. J Histotechnol. 1989;12(3):169-181. doi.org/10.1179/his.1989.12.3.169
  8. Chen CC, Wada K, Jarvis ED. Radioactive in situ hybridization for detecting diverse gene expression patterns in tissue. J Vis Exp. 2012;(62):3764. doi.org/10.3791/3764
  9. Biggin MD, Gibson TJ, Hong GF. Buffer gradient gels and 35S label as an aid to rapid DNA sequence determination. Proc Natl Acad Sci U S A. 1983;80(13):3963-3965. doi.org/10.1073/pnas.80.13.3963
  10. Pelham HR, Jackson RJ. An efficient mRNA-dependent translation system from reticulocyte lysates. Eur J Biochem. 1976;67(1):247-256. doi.org/10.1111/j.1432-1033.1976.tb10656.x
  11. Soto Rifo R, Ricci EP, Décimo D, Moncorgé O, Ohlmann T. Back to basics: the untreated rabbit reticulocyte lysate as a competitive system to recapitulate cap/poly(A) synergy and the selective advantage of IRES-driven translation. Nucleic Acids Res. 2007;35(18):e121. doi.org/10.1093/nar/gkm682
  12. Huttner WB. Sulphation of tyrosine residues: a widespread modification of proteins. Nature. 1982;299(5880):273-276. doi.org/10.1038/299273a0
  13. Lee RW, Huttner WB. Tyrosine-O-sulfated proteins of PC12 pheochromocytoma cells and their sulfation by a tyrosylprotein sulfotransferase. J Biol Chem. 1983;258(18):11326-11334. doi.org/10.1016/S0021-9258(17)44421-8
  14. Humphries DE, Silbert JE. Chlorate: a reversible inhibitor of proteoglycan sulfation. Biochem Biophys Res Commun. 1988;154(1):365-371. doi.org/10.1016/0006-291X(88)90694-8
  15. U.S. Nuclear Regulatory Commission. 10 CFR 30.71, Schedule B (exempt quantities). eCFR, current as of 23 September 2026. www.ecfr.gov/current/title-10/section-30.71
  16. U.S. Nuclear Regulatory Commission. 10 CFR 30.18, Exempt quantities. eCFR, current as of 23 September 2026. www.ecfr.gov/current/title-10/section-30.18
  17. University of Wyoming Safety. Nuclide safety data sheet: sulfur-35. www.uwyo.edu/safety/_files/Docs/Procedures/NuclearSafetyDataSheets/35SPDF.pdf

Technical review by ConductScience, 25 September 2026. Next review 25 September 2027.

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