Proteintech anti p re ss primary
Anti P Re Ss Primary, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/anti+tyms/pm41935067-260-5-12?v=Proteintech
Average 93 stars, based on 1 article reviews

anti p re ss primary - by Bioz Stars, 2026-08

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anti tyms (Proteintech)

Proteintech anti tyms
Anti Tyms, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/anti+tyms/pmc07226198-126-3-5?v=Proteintech
Average 93 stars, based on 1 article reviews

anti tyms - by Bioz Stars, 2026-08

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anti tyms (Cusabio)

Cusabio anti tyms
Anti Tyms, supplied by Cusabio, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/anti+tyms/pmc11131976-80-31-34?v=Cusabio
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anti tyms - by Bioz Stars, 2026-08

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monoclonal anti-tyms, clone ts106 #mab4130 (Merck KGaA)

Merck KGaA monoclonal anti-tyms, clone ts106 #mab4130
Monoclonal Anti Tyms, Clone Ts106 #Mab4130, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/anti+tyms/pm37894370-59-20-22?v=Merck+KGaA
Average 90 stars, based on 1 article reviews

monoclonal anti-tyms, clone ts106 #mab4130 - by Bioz Stars, 2026-08

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rabbit anti tyms (MyBiosource Biotechnology)

MyBiosource Biotechnology rabbit anti tyms

Scheme of the nuclear dTMP‐SC catalytic <t>cycle.</t> <t>SHMT1,</t> DHFR and <t>TYMS</t> are SUMOylated and translocate to the nucleus during G1/S‐phase, where they are proposed to assemble to form the dTMP synthesis complex (dTMP‐SC), anchored to the nuclear lamina . The oligomeric state of the three enzymes is also reported.

Rabbit Anti Tyms, supplied by MyBiosource Biotechnology, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/anti+tyms/pmc09299187-181-16-18?v=MyBiosource+Biotechnology
Average 90 stars, based on 1 article reviews

rabbit anti tyms - by Bioz Stars, 2026-08

90/100 stars

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rabbit anti-human tyms polyclonal antibody (Cusabio)

N/A

Rabbit anti-Human TYMS Polyclonal Antibody

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anti-tyms (aa 263-313) polyclonal antibody (Creative BioMart)

N/A

Contributes to the de novo mitochondrial thymidylate biosynthesis pathway.Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze / thaw cycles.http://www.creative-diagnostics.com/Anti-TYMS-PAb-202496-147.htm

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anti-tyms monoclonal antibody, clone fqs5656 (Creative BioMart)

N/A

Contributes to the de novo mitochondrial thymidylate biosynthesis pathway.Store at -20°C. Stable for 12 months at -20°Chttp://www.creative-diagnostics.com/Anti-TYMS-MAb-160134-144.htm

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mouse anti-human tyms (RayBiotech)

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Human TYMS monoclonal antibody (100 ug)

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rcombinant anti-human tyms antibody scfv fragment (Creative BioMart)

N/A

Recombinant Mouse Antibody scFv Fragment binds specifically to Human TYMS, expressed in E. coli.Formats of immunological tests: Enzyme-linked Immunosorbent Assay; Immunoprecipitation; Functional StudyStore at 4°C short term (1-2 weeks). Aliquot and store at -20°C long

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anti-thymidylate synthase tyms antibody (Boster Bio)

N/A

Boster Bio Anti-Thymidylate Synthase TYMS Antibody (Catalog # A04320-1). Tested in WB applications. This antibody reacts with Human.

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Image Search Results

Scheme of the nuclear dTMP‐SC catalytic cycle. SHMT1, DHFR and TYMS are SUMOylated and translocate to the nucleus during G1/S‐phase, where they are proposed to assemble to form the dTMP synthesis complex (dTMP‐SC), anchored to the nuclear lamina . The oligomeric state of the three enzymes is also reported.

Journal: The Febs Journal

Article Title: Cytosolic localization and in vitro assembly of human de novo thymidylate synthesis complex

doi: 10.1111/febs.16248

Figure Lengend Snippet: Scheme of the nuclear dTMP‐SC catalytic cycle. SHMT1, DHFR and TYMS are SUMOylated and translocate to the nucleus during G1/S‐phase, where they are proposed to assemble to form the dTMP synthesis complex (dTMP‐SC), anchored to the nuclear lamina . The oligomeric state of the three enzymes is also reported.

Article Snippet: The antibodies used were: rabbit anti‐SHMT1 (HPA0233314; Atlas Antibodies, Stokholm, Sweden); mouse anti‐DHFR (WH0001719M1; Sigma‐Aldrich); rabbit anti‐TYMS (MBS126074; Mybiosource, San Diego, CA, USA) indicated as TYMS R ; mouse anti‐TYMS (sc‐33679; Santa Cruz Biotechnology, Inc.) indicated as TYMS M ; mouse anti‐PCNA Alexa Fluor® 488‐conjugated antibody (ab201672, PC10 clone; Abcam, Waltham, MA, USA), mouse anti‐α‐Tubulin (T5168, clone B512; Sigma‐Aldrich); mouse anti‐tubulin‐FITC (f2168; Sigma‐Aldrich); rabbit anti‐Histone‐H3 (H0164; Sigma‐Aldrich); mouse anti‐SHMT1 (sc‐365203; Santa Cruz Biotechnology, Inc.); rabbit anti‐SHMT1 (D3B3J, cell signaling technology); anti‐DHFR (sc‐377091; Santa Cruz Biotechnology, Inc.); anti‐chicken tubulin (ab89984; Abcam); anti‐mouse FITC (AB_2338; Jackson ImmunoResearch, West Grove, PA, USA); anti‐rabbit FITC (AB_2337977; Jackson ImmunoResearch); anti‐mouse Rhodamine (AB_23387;66 Jackson ImmunoResearch); anti‐rabbit CY3 (AB_2338000; Jackson ImmunoResearch); mouse anti‐rabbit IgG‐HRP (sc‐2357; Santa Cruz Biotechnology, Inc.); m‐IgGκ BP‐HRP (sc‐516102; Santa Cruz Biotechnology, Inc.); anti‐chicken Alexa Fluor 647 (703605155; Jackson ImmunoResearch); Duolink is ‐pla probe anti‐mouse minus (duo92004‐100rxn; Sigma‐Aldrich); and Duolink is ‐pla probe anti‐rabbit plus (duo92002‐100rxn; Sigma‐Aldrich).

Techniques:

Identification of proteins proximity in cancer cell lines. (A) Scheme of the is‐PLA: 1, primary antibodies bind specific proteins; 2, secondary antibodies conjugated with oligonucleotides (proximity probes) bind to anti‐rabbit or mouse primary antibodies; 3, if the two proteins are interacting (< 40 nm apart), the proximity probes can hybridize with the two connector oligos; 4, the ligation step produces a circular DNA template; 5, circular DNA is then amplified by DNA polymerase. Detection oligos coupled to fluorochromes hybridize to repeating sequences in the amplicons yielding the is‐PLA signal detected by fluorescent microscopy as discrete spots (inset). (B) is‐PLA signals, corresponding to DHFR/SHMT, SHMT/TYMS and DHFR/TYMS interactions, are shown (red dots). TYMS M and TYMS R both indicate antibodies against TYMS but anti‐mouse and anti‐rabbit, respectively. The is‐PLA spots of interaction of proteins are shown in A549 cells synchronised in the S‐phase after a 24‐h single thymidine block (upper) or in A549 asynchronous cells (bottom). Scale bars = 10 µm. The merge with DAPI signal is shown on the right. Controls are shown in Fig. . (C) Nuclear localization of the is‐PLA signal (number of spots within the normalized nucleus area). In all of the experiments, the number of PLA spots increase in the S‐enriched cells ( t ‐test: ** P < 0.005; **** P < 0.0001). At least 160 cells were analysed per condition. (D) Left: representation of PCNA positive cells, corresponding to S‐phase of the cell cycle. Scale bar = 10 µm. Right: immunofluorescence signal in an asynchronous population or after a single thymidine block of A549. The histogram on the right shows the percentage of PCNA positive or negative cells after and before synchronisation. At least 500 cells were counted per conditions, from three independent experiments; SD values are shown. After synchronisation, the cells in S‐phase comprise approximately 80% of the cellular population.

Journal: The Febs Journal

Article Title: Cytosolic localization and in vitro assembly of human de novo thymidylate synthesis complex

doi: 10.1111/febs.16248

Figure Lengend Snippet: Identification of proteins proximity in cancer cell lines. (A) Scheme of the is‐PLA: 1, primary antibodies bind specific proteins; 2, secondary antibodies conjugated with oligonucleotides (proximity probes) bind to anti‐rabbit or mouse primary antibodies; 3, if the two proteins are interacting (< 40 nm apart), the proximity probes can hybridize with the two connector oligos; 4, the ligation step produces a circular DNA template; 5, circular DNA is then amplified by DNA polymerase. Detection oligos coupled to fluorochromes hybridize to repeating sequences in the amplicons yielding the is‐PLA signal detected by fluorescent microscopy as discrete spots (inset). (B) is‐PLA signals, corresponding to DHFR/SHMT, SHMT/TYMS and DHFR/TYMS interactions, are shown (red dots). TYMS M and TYMS R both indicate antibodies against TYMS but anti‐mouse and anti‐rabbit, respectively. The is‐PLA spots of interaction of proteins are shown in A549 cells synchronised in the S‐phase after a 24‐h single thymidine block (upper) or in A549 asynchronous cells (bottom). Scale bars = 10 µm. The merge with DAPI signal is shown on the right. Controls are shown in Fig. . (C) Nuclear localization of the is‐PLA signal (number of spots within the normalized nucleus area). In all of the experiments, the number of PLA spots increase in the S‐enriched cells ( t ‐test: ** P < 0.005; **** P < 0.0001). At least 160 cells were analysed per condition. (D) Left: representation of PCNA positive cells, corresponding to S‐phase of the cell cycle. Scale bar = 10 µm. Right: immunofluorescence signal in an asynchronous population or after a single thymidine block of A549. The histogram on the right shows the percentage of PCNA positive or negative cells after and before synchronisation. At least 500 cells were counted per conditions, from three independent experiments; SD values are shown. After synchronisation, the cells in S‐phase comprise approximately 80% of the cellular population.

Techniques: Ligation, Amplification, Microscopy, Blocking Assay, Immunofluorescence

Immunofluorescence co‐localization analysis. (A) Co‐localization of DHFR/SHMT1, SHMT1/TYMS and TYMS/DHFR in asynchronous A549 cells. Co‐localization is evident both in the cytosol (tubulin alpha, cyan) and in the nucleus (DAPI, blue) for all the three couples. The original red fluorescence signal of tubulin was changed to cyan for better visualization of the merged images. The merge of green, red and cyan pixels yields white pixels.

Journal: The Febs Journal

Article Title: Cytosolic localization and in vitro assembly of human de novo thymidylate synthesis complex

doi: 10.1111/febs.16248

Figure Lengend Snippet: Immunofluorescence co‐localization analysis. (A) Co‐localization of DHFR/SHMT1, SHMT1/TYMS and TYMS/DHFR in asynchronous A549 cells. Co‐localization is evident both in the cytosol (tubulin alpha, cyan) and in the nucleus (DAPI, blue) for all the three couples. The original red fluorescence signal of tubulin was changed to cyan for better visualization of the merged images. The merge of green, red and cyan pixels yields white pixels.

Techniques: Immunofluorescence, Fluorescence

$Immunofluorescence analysis. (A–C) Compartmentalization of the three proteins with respect to the cellular phase by Immunofluorescence analysis. SHMT1 (A), DHFR (B) and TYMS (C) show a cytoplasmic localization both in the asynchronous and S‐phase synchronised cells. Scale bar = 10 µm. (D) Nuclear localization (as deduced by the normalized intensity of the fluorescence signal) is clearly more abundant in the S‐enriched cells for SHMT1; a slight increase is observed for TYMS (with both the antibodies used in the PLA experiments; rabbit, TYMS R ; and mouse, TYMS M ; see Materials and methods). No change was observed for DHFR. ( t ‐test: * P < 0.05; ** P < 0.005; **** P < 0.0001). Error bars represent the SD. At least 80 cells per condition from two independent experiment were analysed. (E) Western blot of subcellular fractionation of both asynchronous and S‐phase enriched A549 cell lines. Western blotting analysis was performed using a 1 : 1000 dilution of the primary antibodies. For Histone H3, the correct band is boxed in red. The other bands detected in the cytosol have a molecular weight lower than 15 kDa and are also present in the nuclear fractions. Giving that the molecular weight of Histone H3 is 17 kDa, and the bands recur in all the four lanes, it is plausible that they are detected because of non‐specific interactions of the primary or secondary antibody. In this experiment, the quantitative analysis was not performed, but it is still possible to detect the bands of SHMT1 and TYMS only in the nucleus of the S‐phase enriched cells. As shown in the IF experiments, it was not possible to detect an increase of the presence of DHFR in the nucleus of the synchronised cells.$

Journal: The Febs Journal

Article Title: Cytosolic localization and in vitro assembly of human de novo thymidylate synthesis complex

doi: 10.1111/febs.16248

Figure Lengend Snippet: Immunofluorescence analysis. (A–C) Compartmentalization of the three proteins with respect to the cellular phase by Immunofluorescence analysis. SHMT1 (A), DHFR (B) and TYMS (C) show a cytoplasmic localization both in the asynchronous and S‐phase synchronised cells. Scale bar = 10 µm. (D) Nuclear localization (as deduced by the normalized intensity of the fluorescence signal) is clearly more abundant in the S‐enriched cells for SHMT1; a slight increase is observed for TYMS (with both the antibodies used in the PLA experiments; rabbit, TYMS R ; and mouse, TYMS M ; see Materials and methods). No change was observed for DHFR. ( t ‐test: * P < 0.05; ** P < 0.005; **** P < 0.0001). Error bars represent the SD. At least 80 cells per condition from two independent experiment were analysed. (E) Western blot of subcellular fractionation of both asynchronous and S‐phase enriched A549 cell lines. Western blotting analysis was performed using a 1 : 1000 dilution of the primary antibodies. For Histone H3, the correct band is boxed in red. The other bands detected in the cytosol have a molecular weight lower than 15 kDa and are also present in the nuclear fractions. Giving that the molecular weight of Histone H3 is 17 kDa, and the bands recur in all the four lanes, it is plausible that they are detected because of non‐specific interactions of the primary or secondary antibody. In this experiment, the quantitative analysis was not performed, but it is still possible to detect the bands of SHMT1 and TYMS only in the nucleus of the S‐phase enriched cells. As shown in the IF experiments, it was not possible to detect an increase of the presence of DHFR in the nucleus of the synchronised cells.

Techniques: Immunofluorescence, Fluorescence, Western Blot, Fractionation, Molecular Weight

is‐PLA analysis on HeLa cells and is‐PLA negative controls on A549 cells. (A) PLA signal of protein interaction is shown in HeLa non‐synchronized cells. (B) Negative controls of is‐PLA signals. PLA experiment was performed without one of the primary antibodies (A549 cells). In these conditions, there is no or little PLA signal. TYMS M and TYMS R both indicate antibodies against TYMS but anti‐mouse and anti‐rabbit, respectively. (C–E) is‐PLA for the three protein–protein interaction performed on A549 cells 48 h after transfection with scrambled or siRNA for shmt1 . For the DHFR/SHMT1 and TYMS/SHMT1 interactions the PLA signal is significantly lower in the RNAi cells, whereas, for the DHFR/TYMS interaction, the signal of the scramble and RNAi samples is similar. For all panels (A‐E), the scale bar in the bottom right corner is 10 µm. (F) SHMT1 expression control of RNAi.

Journal: The Febs Journal

Article Title: Cytosolic localization and in vitro assembly of human de novo thymidylate synthesis complex

doi: 10.1111/febs.16248

Figure Lengend Snippet: is‐PLA analysis on HeLa cells and is‐PLA negative controls on A549 cells. (A) PLA signal of protein interaction is shown in HeLa non‐synchronized cells. (B) Negative controls of is‐PLA signals. PLA experiment was performed without one of the primary antibodies (A549 cells). In these conditions, there is no or little PLA signal. TYMS M and TYMS R both indicate antibodies against TYMS but anti‐mouse and anti‐rabbit, respectively. (C–E) is‐PLA for the three protein–protein interaction performed on A549 cells 48 h after transfection with scrambled or siRNA for shmt1 . For the DHFR/SHMT1 and TYMS/SHMT1 interactions the PLA signal is significantly lower in the RNAi cells, whereas, for the DHFR/TYMS interaction, the signal of the scramble and RNAi samples is similar. For all panels (A‐E), the scale bar in the bottom right corner is 10 µm. (F) SHMT1 expression control of RNAi.

Techniques: Transfection, Expressing

Designing human DHFR‐TYMS Chimera. (A) Cartoon representation of the chimeric model of human DHFR‐TYMS (in purple and blue, respectively; the linker is shown in red; the N‐terminus position is also indicated) superposed with the structure of the bifunctional enzyme from B. bovis (PDB ID: 3I3R ) in light grey. The enzyme is dimeric, the partner subunit is shown as surface representation. (B) Electrostatic surface potentials, as calculated using apbs (Adaptive Poisson–Boltzmann Solver) , at the modelled interface between hDHFR and hTYMS, showing a perfect complementarity. Partially positive or negative regions are indicated in blue and red, respectively. (C) Scheme of the final constructs differing only for the linker length and consequently named Chimera‐Long and Chimera‐Short. Structural renderings were produced using pymol .

Journal: The Febs Journal

Article Title: Cytosolic localization and in vitro assembly of human de novo thymidylate synthesis complex

doi: 10.1111/febs.16248

Figure Lengend Snippet: Designing human DHFR‐TYMS Chimera. (A) Cartoon representation of the chimeric model of human DHFR‐TYMS (in purple and blue, respectively; the linker is shown in red; the N‐terminus position is also indicated) superposed with the structure of the bifunctional enzyme from B. bovis (PDB ID: 3I3R ) in light grey. The enzyme is dimeric, the partner subunit is shown as surface representation. (B) Electrostatic surface potentials, as calculated using apbs (Adaptive Poisson–Boltzmann Solver) , at the modelled interface between hDHFR and hTYMS, showing a perfect complementarity. Partially positive or negative regions are indicated in blue and red, respectively. (C) Scheme of the final constructs differing only for the linker length and consequently named Chimera‐Long and Chimera‐Short. Structural renderings were produced using pymol .

Techniques: Construct, Produced

IP and FWB. (A) FWB: The prey proteins (SHMT1 or Chimera‐Long) were resolved alone by SDS/PAGE, electroblotted on a PVDF membrane, refolded and then incubated with 50 ng·mL −1 of the bait protein at 4 °C o.n. Left: the band detected at SHMT1 lane and height represents Chimera, and the band detected at Chimera lane and height, on the right image represents SHM1. The bait proteins were used in place of the prey proteins as positive controls, whereas RmcA (a bi‐domain bacterial protein construct from P. aeruginosa for which the two domains have a molecular weight comparable to DHFR and TYMS) was used as a negative control . The formation of the complex between SHMT1 and Chimera‐Short (B) or SHMT1 dimeric mutant and Chimera‐Long (C) was tested by following the experimental set‐up described previously. Nevertheless, and despite over exposition of the membranes, in both cases, formation of the complex was not observed. (D) IP experiment: SHMT1 and Chimera‐Long were mixed at a ratio of 1 : 2 at a final concentration of 18 μ m for SHMT1 and 36 μ m for Chimera‐Long. The proteins were attached to the Protein G‐agarose beads by using specific antibodies (anti‐TYMS or anti‐SHMT1). The samples were incubated at 4 °C o.n. In the first two images (left), the detected band represents Chimera‐Long, whereas, in the image on the right, the detected band refers to SHMT1.

Journal: The Febs Journal

Article Title: Cytosolic localization and in vitro assembly of human de novo thymidylate synthesis complex

doi: 10.1111/febs.16248

Figure Lengend Snippet: IP and FWB. (A) FWB: The prey proteins (SHMT1 or Chimera‐Long) were resolved alone by SDS/PAGE, electroblotted on a PVDF membrane, refolded and then incubated with 50 ng·mL −1 of the bait protein at 4 °C o.n. Left: the band detected at SHMT1 lane and height represents Chimera, and the band detected at Chimera lane and height, on the right image represents SHM1. The bait proteins were used in place of the prey proteins as positive controls, whereas RmcA (a bi‐domain bacterial protein construct from P. aeruginosa for which the two domains have a molecular weight comparable to DHFR and TYMS) was used as a negative control . The formation of the complex between SHMT1 and Chimera‐Short (B) or SHMT1 dimeric mutant and Chimera‐Long (C) was tested by following the experimental set‐up described previously. Nevertheless, and despite over exposition of the membranes, in both cases, formation of the complex was not observed. (D) IP experiment: SHMT1 and Chimera‐Long were mixed at a ratio of 1 : 2 at a final concentration of 18 μ m for SHMT1 and 36 μ m for Chimera‐Long. The proteins were attached to the Protein G‐agarose beads by using specific antibodies (anti‐TYMS or anti‐SHMT1). The samples were incubated at 4 °C o.n. In the first two images (left), the detected band represents Chimera‐Long, whereas, in the image on the right, the detected band refers to SHMT1.

Techniques: SDS Page, Incubation, Construct, Molecular Weight, Negative Control, Mutagenesis, Concentration Assay

dTMP‐SC formation equilibrium in the cytosol. Scheme of the processes that may be affected by the assembly of the dTMP‐SC in the cytosol. After complex formation, some regions of the three enzymes may become less accessible. This may in turn affect: (A) the SUMOylation/deSUMOylation equilibrium, which controls nuclear translocation and possibly other functions; (B) the ability of the proteins to bind mRNA and cross‐regulate protein homeostasis and, in the case of SHMT1, also the catalytic activity (riboregulation) with a direct effect on the folate cycle and OCM; (C) other PPI or post‐transcriptional modifications, as well as the mitochondrial import of TYMS.

Journal: The Febs Journal

Article Title: Cytosolic localization and in vitro assembly of human de novo thymidylate synthesis complex

doi: 10.1111/febs.16248

Figure Lengend Snippet: dTMP‐SC formation equilibrium in the cytosol. Scheme of the processes that may be affected by the assembly of the dTMP‐SC in the cytosol. After complex formation, some regions of the three enzymes may become less accessible. This may in turn affect: (A) the SUMOylation/deSUMOylation equilibrium, which controls nuclear translocation and possibly other functions; (B) the ability of the proteins to bind mRNA and cross‐regulate protein homeostasis and, in the case of SHMT1, also the catalytic activity (riboregulation) with a direct effect on the folate cycle and OCM; (C) other PPI or post‐transcriptional modifications, as well as the mitochondrial import of TYMS.

Techniques: Translocation Assay, Activity Assay

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