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rrm2  (Cell Signaling Technology Inc)


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    Structured Review

    Cell Signaling Technology Inc rrm2
    Expression of several senescence-associated proteins under HS conditions at 41 °C and 45 °C for 30 min in aged HFF-1 cells. (a) Detection of protein expression levels of GORAB, AURKB, RhoC, α-N-catenin, <t>RRM2,</t> AURKA, and PLK1 under 41 °C and 45 °C HS. Protein expression was quantified as fold-change relative to untreated controls (set to 1), normalized to GAPDH. (b) GORAB. (c) AURKB. (d) RhoC. (e) α-N-catenin. (f) <t>RRM2.</t> (g) AURKA. (h) PLK1. Representative blots were cropped only to improve presentation; the corresponding full-length, uncropped blots with molecular-weight markers and the associated GAPDH loading control are provided in <xref ref-type=Supplementary Figure S1 (the first lane corresponds to an unrelated sample and was not analyzed). Data are representative of three independent experiments, with results presented as mean ± SD. ** P < 0.01, *** P < 0.001, **** P < 0.0001, compared with the control group. " width="250" height="auto" />
    Rrm2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 46 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+anti+rrm2/RRM2+XP+Rabbit+mAb/pmc13049315-268-50-51
    Average 94 stars, based on 46 article reviews
    rrm2 - by Bioz Stars, 2026-09
    94/100 stars

    Images

    1) Product Images from "Proteomic and phenotypic profiling of replicative-senescent human foreskin fibroblasts under brief heat shock"

    Article Title: Proteomic and phenotypic profiling of replicative-senescent human foreskin fibroblasts under brief heat shock

    Journal: Cell Stress & Chaperones

    doi: 10.1016/j.cstres.2026.100174

    Expression of several senescence-associated proteins under HS conditions at 41 °C and 45 °C for 30 min in aged HFF-1 cells. (a) Detection of protein expression levels of GORAB, AURKB, RhoC, α-N-catenin, RRM2, AURKA, and PLK1 under 41 °C and 45 °C HS. Protein expression was quantified as fold-change relative to untreated controls (set to 1), normalized to GAPDH. (b) GORAB. (c) AURKB. (d) RhoC. (e) α-N-catenin. (f) RRM2. (g) AURKA. (h) PLK1. Representative blots were cropped only to improve presentation; the corresponding full-length, uncropped blots with molecular-weight markers and the associated GAPDH loading control are provided in <xref ref-type=Supplementary Figure S1 (the first lane corresponds to an unrelated sample and was not analyzed). Data are representative of three independent experiments, with results presented as mean ± SD. ** P < 0.01, *** P < 0.001, **** P < 0.0001, compared with the control group. " title="... protein expression levels of GORAB, AURKB, RhoC, α-N-catenin, RRM2, AURKA, and PLK1 under 41 °C and 45 ..." property="contentUrl" width="100%" height="100%"/>
    Figure Legend Snippet: Expression of several senescence-associated proteins under HS conditions at 41 °C and 45 °C for 30 min in aged HFF-1 cells. (a) Detection of protein expression levels of GORAB, AURKB, RhoC, α-N-catenin, RRM2, AURKA, and PLK1 under 41 °C and 45 °C HS. Protein expression was quantified as fold-change relative to untreated controls (set to 1), normalized to GAPDH. (b) GORAB. (c) AURKB. (d) RhoC. (e) α-N-catenin. (f) RRM2. (g) AURKA. (h) PLK1. Representative blots were cropped only to improve presentation; the corresponding full-length, uncropped blots with molecular-weight markers and the associated GAPDH loading control are provided in Supplementary Figure S1 (the first lane corresponds to an unrelated sample and was not analyzed). Data are representative of three independent experiments, with results presented as mean ± SD. ** P < 0.01, *** P < 0.001, **** P < 0.0001, compared with the control group.

    Techniques Used: Expressing, Molecular Weight, Control

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    Incubation:

    Article Title: IGF-1 secreted by mesenchymal stem cells affects the function of lymphatic endothelial progenitor cells: a potential strategy for the treatment of lymphedema
    Article Snippet: The isolated proteins were then transferred to a polyvinylidene difluoride membrane (PVDF) (Millipore, United States). .. PDVF membranes were incubated at 4°C with rabbit anti-p-Akt (Ser473) (1:1000, CST, United States), rabbit anti-p-S6 (1:1000, CST, United States), rabbit anti-Akt (1:1000, CST, United States), rabbit anti-S6 (1:1000, CST, United States), rabbit anti-Bax (1:2000, Proteintech, China), rabbit anti-Bcl-2 (1:2000, Proteintech, China), rabbit anti-caspase3 (1:2000, Proteintech, China), rabbit anti-RRM1 (1:1000, CST, United States), rabbit anti-RRM2 (1:1000, CST, United States) and mouse anti-GAPDH primary antibody (1:2000, zsgb bio, China) were incubated overnight. .. Subsequently, the membrane was subjected to an incubation with goat anti-rabbit (1:2000, Zsgb Bio, China) or goat anti-mouse (1:2000, Zsgb Bio, China) for 60 min at room temperature.

    Immunostaining:

    Article Title: Proteomic analysis of cell cycle progression in asynchronous cultures, including mitotic subphases, using PRIMMUS
    Article Snippet: .. The primary antibodies used for immunostaining are rabbit anti-RRM2 (HPA056994, RRID: AB_2683304), mouse anti- H3S10ph (Cell Signaling Technology 9706, RRID: AB_331748), rat anti-H3S28ph HTA28 (Abcam ab10543, RRID: AB_2295065), and mouse anti-alpha tubulin (Sigma DM1a, RRID: AB_477593). ..

    Article Title: Proteomic analysis of cell cycle progression in asynchronous cultures, including mitotic subphases, using PRIMMUS
    Article Snippet: .. The primary antibodies used for immunostaining are rabbit anti-RRM2 (HPA056994, RRID: AB_2683304 ), mouse anti-H3S10ph (Cell Signaling Technology 9706, RRID: AB_331748 ), rat anti-H3S28ph HTA28 (Abcam ab10543, RRID: AB_2295065 ), and mouse anti-alpha tubulin (Sigma DM1a, RRID: AB_477593 ). ..

    Formalin-fixed Paraffin-Embedded:

    Article Title: Quantitative transcriptomic and proteomic analysis reveals corosolic acid inhibiting bladder cancer via suppressing cell cycle and inducing mitophagy in vitro and in vivo.
    Article Snippet: Corosolic acid (CA) is a plant-derived terpenoid compound with many health benefits.. However, the anti-tumor effects of CA in bladder cancer remain unexplored.. Here, we found that CA inhibited bladder tumor both in vitro and in vivo, and had no significant toxicity in mice.

    Immunofluorescence:

    Article Title: Quantitative transcriptomic and proteomic analysis reveals corosolic acid inhibiting bladder cancer via suppressing cell cycle and inducing mitophagy in vitro and in vivo.
    Article Snippet: Corosolic acid (CA) is a plant-derived terpenoid compound with many health benefits.. However, the anti-tumor effects of CA in bladder cancer remain unexplored.. Here, we found that CA inhibited bladder tumor both in vitro and in vivo, and had no significant toxicity in mice.

    Staining:

    Article Title: Quantitative transcriptomic and proteomic analysis reveals corosolic acid inhibiting bladder cancer via suppressing cell cycle and inducing mitophagy in vitro and in vivo.
    Article Snippet: Corosolic acid (CA) is a plant-derived terpenoid compound with many health benefits.. However, the anti-tumor effects of CA in bladder cancer remain unexplored.. Here, we found that CA inhibited bladder tumor both in vitro and in vivo, and had no significant toxicity in mice.



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    Cell Signaling Technology Inc rrm2
    Expression of several senescence-associated proteins under HS conditions at 41 °C and 45 °C for 30 min in aged HFF-1 cells. (a) Detection of protein expression levels of GORAB, AURKB, RhoC, α-N-catenin, <t>RRM2,</t> AURKA, and PLK1 under 41 °C and 45 °C HS. Protein expression was quantified as fold-change relative to untreated controls (set to 1), normalized to GAPDH. (b) GORAB. (c) AURKB. (d) RhoC. (e) α-N-catenin. (f) <t>RRM2.</t> (g) AURKA. (h) PLK1. Representative blots were cropped only to improve presentation; the corresponding full-length, uncropped blots with molecular-weight markers and the associated GAPDH loading control are provided in <xref ref-type=Supplementary Figure S1 (the first lane corresponds to an unrelated sample and was not analyzed). Data are representative of three independent experiments, with results presented as mean ± SD. ** P < 0.01, *** P < 0.001, **** P < 0.0001, compared with the control group. " width="250" height="auto" />
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    Expression of several senescence-associated proteins under HS conditions at 41 °C and 45 °C for 30 min in aged HFF-1 cells. (a) Detection of protein expression levels of GORAB, AURKB, RhoC, α-N-catenin, <t>RRM2,</t> AURKA, and PLK1 under 41 °C and 45 °C HS. Protein expression was quantified as fold-change relative to untreated controls (set to 1), normalized to GAPDH. (b) GORAB. (c) AURKB. (d) RhoC. (e) α-N-catenin. (f) <t>RRM2.</t> (g) AURKA. (h) PLK1. Representative blots were cropped only to improve presentation; the corresponding full-length, uncropped blots with molecular-weight markers and the associated GAPDH loading control are provided in <xref ref-type=Supplementary Figure S1 (the first lane corresponds to an unrelated sample and was not analyzed). Data are representative of three independent experiments, with results presented as mean ± SD. ** P < 0.01, *** P < 0.001, **** P < 0.0001, compared with the control group. " width="250" height="auto" />
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    Expression of several senescence-associated proteins under HS conditions at 41 °C and 45 °C for 30 min in aged HFF-1 cells. (a) Detection of protein expression levels of GORAB, AURKB, RhoC, α-N-catenin, <t>RRM2,</t> AURKA, and PLK1 under 41 °C and 45 °C HS. Protein expression was quantified as fold-change relative to untreated controls (set to 1), normalized to GAPDH. (b) GORAB. (c) AURKB. (d) RhoC. (e) α-N-catenin. (f) <t>RRM2.</t> (g) AURKA. (h) PLK1. Representative blots were cropped only to improve presentation; the corresponding full-length, uncropped blots with molecular-weight markers and the associated GAPDH loading control are provided in <xref ref-type=Supplementary Figure S1 (the first lane corresponds to an unrelated sample and was not analyzed). Data are representative of three independent experiments, with results presented as mean ± SD. ** P < 0.01, *** P < 0.001, **** P < 0.0001, compared with the control group. " width="250" height="auto" />
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    Image Search Results


    Expression of several senescence-associated proteins under HS conditions at 41 °C and 45 °C for 30 min in aged HFF-1 cells. (a) Detection of protein expression levels of GORAB, AURKB, RhoC, α-N-catenin, RRM2, AURKA, and PLK1 under 41 °C and 45 °C HS. Protein expression was quantified as fold-change relative to untreated controls (set to 1), normalized to GAPDH. (b) GORAB. (c) AURKB. (d) RhoC. (e) α-N-catenin. (f) RRM2. (g) AURKA. (h) PLK1. Representative blots were cropped only to improve presentation; the corresponding full-length, uncropped blots with molecular-weight markers and the associated GAPDH loading control are provided in <xref ref-type=Supplementary Figure S1 (the first lane corresponds to an unrelated sample and was not analyzed). Data are representative of three independent experiments, with results presented as mean ± SD. ** P < 0.01, *** P < 0.001, **** P < 0.0001, compared with the control group. " width="100%" height="100%">

    Journal: Cell Stress & Chaperones

    Article Title: Proteomic and phenotypic profiling of replicative-senescent human foreskin fibroblasts under brief heat shock

    doi: 10.1016/j.cstres.2026.100174

    Figure Lengend Snippet: Expression of several senescence-associated proteins under HS conditions at 41 °C and 45 °C for 30 min in aged HFF-1 cells. (a) Detection of protein expression levels of GORAB, AURKB, RhoC, α-N-catenin, RRM2, AURKA, and PLK1 under 41 °C and 45 °C HS. Protein expression was quantified as fold-change relative to untreated controls (set to 1), normalized to GAPDH. (b) GORAB. (c) AURKB. (d) RhoC. (e) α-N-catenin. (f) RRM2. (g) AURKA. (h) PLK1. Representative blots were cropped only to improve presentation; the corresponding full-length, uncropped blots with molecular-weight markers and the associated GAPDH loading control are provided in Supplementary Figure S1 (the first lane corresponds to an unrelated sample and was not analyzed). Data are representative of three independent experiments, with results presented as mean ± SD. ** P < 0.01, *** P < 0.001, **** P < 0.0001, compared with the control group.

    Article Snippet: Membranes were blocked with 5% nonfat milk for 1 h at room temperature and incubated overnight at 4 °C with primary antibodies against GORAB (Proteintech, Wuhan, China; 17798–1-AP; 1:1000), AURKA (Cell Signaling Technology, Danvers, MA, USA; 14475T; 1:1000), AURKB (Cell Signaling Technology; 28711T; 1:1000), RhoC (Cell Signaling Technology; 3430T; 1:1000), RRM2 (Cell Signaling Technology; 65939T; 1:2000), PLK1 (Cell Signaling Technology; 4513T; 1:1000), α-N-catenin (Cell Signaling Technology; 2163T; 1:1000), and GAPDH (Abcam, Cambridge, UK; ab125247; 1:10,000) as the loading control.

    Techniques: Expressing, Molecular Weight, Control