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stromal interaction molecule 1 stim1 cst  (Proteintech)


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    Proteintech stromal interaction molecule 1 stim1 cst
    FIGURE 4 Environment-induced heat stress altered calcium regulatory proteins in LV. In LV (a) environment-induced heat stress increased the relative protein abundance of the PLB/SERCA2a complex, <t>STIM1,</t> CaMKII, p-PKC pan, and p-PKC alpha/beta II compared to TN; while the monomeric and oligomeric forms of PLB, p-CaMKII, and p-PLB were similar between groups. In RV (b) relative protein abundance of the oligomeric form of PLB and p-PKC alpha/beta II increased by EIHS compared to TN; whereas the monomeric form of PLB, PLB/SERCA2a complex, STIM1, CaMKII, p-CaMKII, p-PLB, and p-PKC pan were similar between groups. Treatments: EIHS, environment-induced heat stress; TN, thermoneutral. Results are expressed as means ± standard deviation. * indicates p < 0.05. (a) LV: Monomer, oligomer, SERCA2a complex, CaMKII, p-CaMKII, p-PLB, p-PKC pan, and p-PKC alpha/beta II n = 7/group, one outlier from EIHS CaMKII and p-CaMKII and one outlier removed from TN p = PKC pan and p-PKC alpha/beta II; STIM1 n = 6/group, one outlier removed from EIHS. (b) RV: Monomer, oligomer, SERCA2a complex, CaMKII, p-CaMKII, p-PLB, n = 7/group, one outlier removed from TN oligomer; STIM1 n = 8/group, one outlier removed EIHS; p-PKC pan and p-PKC alpha/beta II TN n = 6/group, EIHS n = 8/group, one outlier removed from EIHS p-PKC alpha/beta II.
    Stromal Interaction Molecule 1 Stim1 Cst, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 90 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/stromal+interaction+molecule+1+stim1+cst/pm40483549-46-215-211?v=Proteintech
    Average 94 stars, based on 90 article reviews
    stromal interaction molecule 1 stim1 cst - by Bioz Stars, 2026-08
    94/100 stars

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    1) Product Images from "Environment-induced heat stress causes ventricular-dependent biochemical changes in the heart in female pigs."

    Article Title: Environment-induced heat stress causes ventricular-dependent biochemical changes in the heart in female pigs.

    Journal: Physiological reports

    doi: 10.14814/phy2.70414

    FIGURE 4 Environment-induced heat stress altered calcium regulatory proteins in LV. In LV (a) environment-induced heat stress increased the relative protein abundance of the PLB/SERCA2a complex, STIM1, CaMKII, p-PKC pan, and p-PKC alpha/beta II compared to TN; while the monomeric and oligomeric forms of PLB, p-CaMKII, and p-PLB were similar between groups. In RV (b) relative protein abundance of the oligomeric form of PLB and p-PKC alpha/beta II increased by EIHS compared to TN; whereas the monomeric form of PLB, PLB/SERCA2a complex, STIM1, CaMKII, p-CaMKII, p-PLB, and p-PKC pan were similar between groups. Treatments: EIHS, environment-induced heat stress; TN, thermoneutral. Results are expressed as means ± standard deviation. * indicates p < 0.05. (a) LV: Monomer, oligomer, SERCA2a complex, CaMKII, p-CaMKII, p-PLB, p-PKC pan, and p-PKC alpha/beta II n = 7/group, one outlier from EIHS CaMKII and p-CaMKII and one outlier removed from TN p = PKC pan and p-PKC alpha/beta II; STIM1 n = 6/group, one outlier removed from EIHS. (b) RV: Monomer, oligomer, SERCA2a complex, CaMKII, p-CaMKII, p-PLB, n = 7/group, one outlier removed from TN oligomer; STIM1 n = 8/group, one outlier removed EIHS; p-PKC pan and p-PKC alpha/beta II TN n = 6/group, EIHS n = 8/group, one outlier removed from EIHS p-PKC alpha/beta II.
    Figure Legend Snippet: FIGURE 4 Environment-induced heat stress altered calcium regulatory proteins in LV. In LV (a) environment-induced heat stress increased the relative protein abundance of the PLB/SERCA2a complex, STIM1, CaMKII, p-PKC pan, and p-PKC alpha/beta II compared to TN; while the monomeric and oligomeric forms of PLB, p-CaMKII, and p-PLB were similar between groups. In RV (b) relative protein abundance of the oligomeric form of PLB and p-PKC alpha/beta II increased by EIHS compared to TN; whereas the monomeric form of PLB, PLB/SERCA2a complex, STIM1, CaMKII, p-CaMKII, p-PLB, and p-PKC pan were similar between groups. Treatments: EIHS, environment-induced heat stress; TN, thermoneutral. Results are expressed as means ± standard deviation. * indicates p < 0.05. (a) LV: Monomer, oligomer, SERCA2a complex, CaMKII, p-CaMKII, p-PLB, p-PKC pan, and p-PKC alpha/beta II n = 7/group, one outlier from EIHS CaMKII and p-CaMKII and one outlier removed from TN p = PKC pan and p-PKC alpha/beta II; STIM1 n = 6/group, one outlier removed from EIHS. (b) RV: Monomer, oligomer, SERCA2a complex, CaMKII, p-CaMKII, p-PLB, n = 7/group, one outlier removed from TN oligomer; STIM1 n = 8/group, one outlier removed EIHS; p-PKC pan and p-PKC alpha/beta II TN n = 6/group, EIHS n = 8/group, one outlier removed from EIHS p-PKC alpha/beta II.

    Techniques Used: Quantitative Proteomics, Standard Deviation



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    Proteintech stromal interaction molecule 1 stim1 cst
    FIGURE 4 Environment-induced heat stress altered calcium regulatory proteins in LV. In LV (a) environment-induced heat stress increased the relative protein abundance of the PLB/SERCA2a complex, <t>STIM1,</t> CaMKII, p-PKC pan, and p-PKC alpha/beta II compared to TN; while the monomeric and oligomeric forms of PLB, p-CaMKII, and p-PLB were similar between groups. In RV (b) relative protein abundance of the oligomeric form of PLB and p-PKC alpha/beta II increased by EIHS compared to TN; whereas the monomeric form of PLB, PLB/SERCA2a complex, STIM1, CaMKII, p-CaMKII, p-PLB, and p-PKC pan were similar between groups. Treatments: EIHS, environment-induced heat stress; TN, thermoneutral. Results are expressed as means ± standard deviation. * indicates p < 0.05. (a) LV: Monomer, oligomer, SERCA2a complex, CaMKII, p-CaMKII, p-PLB, p-PKC pan, and p-PKC alpha/beta II n = 7/group, one outlier from EIHS CaMKII and p-CaMKII and one outlier removed from TN p = PKC pan and p-PKC alpha/beta II; STIM1 n = 6/group, one outlier removed from EIHS. (b) RV: Monomer, oligomer, SERCA2a complex, CaMKII, p-CaMKII, p-PLB, n = 7/group, one outlier removed from TN oligomer; STIM1 n = 8/group, one outlier removed EIHS; p-PKC pan and p-PKC alpha/beta II TN n = 6/group, EIHS n = 8/group, one outlier removed from EIHS p-PKC alpha/beta II.
    Stromal Interaction Molecule 1 Stim1 Cst, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/stromal+interaction+molecule+1+stim1+cst/pm40483549-46-215-211?v=Proteintech
    Average 94 stars, based on 1 article reviews
    stromal interaction molecule 1 stim1 cst - by Bioz Stars, 2026-08
    94/100 stars
      Buy from Supplier

    Image Search Results


    FIGURE 4 Environment-induced heat stress altered calcium regulatory proteins in LV. In LV (a) environment-induced heat stress increased the relative protein abundance of the PLB/SERCA2a complex, STIM1, CaMKII, p-PKC pan, and p-PKC alpha/beta II compared to TN; while the monomeric and oligomeric forms of PLB, p-CaMKII, and p-PLB were similar between groups. In RV (b) relative protein abundance of the oligomeric form of PLB and p-PKC alpha/beta II increased by EIHS compared to TN; whereas the monomeric form of PLB, PLB/SERCA2a complex, STIM1, CaMKII, p-CaMKII, p-PLB, and p-PKC pan were similar between groups. Treatments: EIHS, environment-induced heat stress; TN, thermoneutral. Results are expressed as means ± standard deviation. * indicates p < 0.05. (a) LV: Monomer, oligomer, SERCA2a complex, CaMKII, p-CaMKII, p-PLB, p-PKC pan, and p-PKC alpha/beta II n = 7/group, one outlier from EIHS CaMKII and p-CaMKII and one outlier removed from TN p = PKC pan and p-PKC alpha/beta II; STIM1 n = 6/group, one outlier removed from EIHS. (b) RV: Monomer, oligomer, SERCA2a complex, CaMKII, p-CaMKII, p-PLB, n = 7/group, one outlier removed from TN oligomer; STIM1 n = 8/group, one outlier removed EIHS; p-PKC pan and p-PKC alpha/beta II TN n = 6/group, EIHS n = 8/group, one outlier removed from EIHS p-PKC alpha/beta II.

    Journal: Physiological reports

    Article Title: Environment-induced heat stress causes ventricular-dependent biochemical changes in the heart in female pigs.

    doi: 10.14814/phy2.70414

    Figure Lengend Snippet: FIGURE 4 Environment-induced heat stress altered calcium regulatory proteins in LV. In LV (a) environment-induced heat stress increased the relative protein abundance of the PLB/SERCA2a complex, STIM1, CaMKII, p-PKC pan, and p-PKC alpha/beta II compared to TN; while the monomeric and oligomeric forms of PLB, p-CaMKII, and p-PLB were similar between groups. In RV (b) relative protein abundance of the oligomeric form of PLB and p-PKC alpha/beta II increased by EIHS compared to TN; whereas the monomeric form of PLB, PLB/SERCA2a complex, STIM1, CaMKII, p-CaMKII, p-PLB, and p-PKC pan were similar between groups. Treatments: EIHS, environment-induced heat stress; TN, thermoneutral. Results are expressed as means ± standard deviation. * indicates p < 0.05. (a) LV: Monomer, oligomer, SERCA2a complex, CaMKII, p-CaMKII, p-PLB, p-PKC pan, and p-PKC alpha/beta II n = 7/group, one outlier from EIHS CaMKII and p-CaMKII and one outlier removed from TN p = PKC pan and p-PKC alpha/beta II; STIM1 n = 6/group, one outlier removed from EIHS. (b) RV: Monomer, oligomer, SERCA2a complex, CaMKII, p-CaMKII, p-PLB, n = 7/group, one outlier removed from TN oligomer; STIM1 n = 8/group, one outlier removed EIHS; p-PKC pan and p-PKC alpha/beta II TN n = 6/group, EIHS n = 8/group, one outlier removed from EIHS p-PKC alpha/beta II.

    Article Snippet: Antibody Company/product No. Primary dilution Secondary dilution Calmodulin (CaM) Abcam, ab45689 1:1000 1:2000 Calmodulin- dependent protein kinase II (CaMKII) Santa Cruz Technologies (SC), #5306 1:500 1:1000 Phophorylated- Calmodulin- dependent protein kinase II (p- CaMKII) (Thr286) Cell Signaling Techology (CST), #12716 1:500 1:1000 Calpain 1 Large Subunit (Mu- Type CST, #2556 1:1000 1:2000 Calpain 2 Large Subunit (M- Type) CST, #2539 1:1000 1:2000 Calpastatin CST, #4146 1:1000 1:2000 Troponin T Millipore Sigma, #T6277 1:1000 1:2000 Calsequestrin Invitrogen, #VIIID12 1:500 1:1000 Calumenin SC, #271357 1:1000 1:2000 Junctophilin2 SC, #377086 1:1000 1:2000 Muscle atrophy F- box protein (MAFbx/Atrogin- 1) SC, #166806 1:1000 1:2000 Muscle RING finger protein 1 (MuRF- 1) SC, #398608 1:1000 1:2000 ORAI1 ProteinTech, #66223–1 1:1000 1:3000 Plasma membrane calcium ATPase (PMCA) SC, #211917 1:1000 1:2000 mouse Phospholamban (PLB) Novus, #NBP2- 19807 1:3000 (5% milk) 1:3000 (5% milk) Phosphorylated- Phospholamban (S16/Thr17) CST, #8496 1:1000 1:2000 Phosphorylated Protein Kinase C (p- PKC) Novus Biologicals, #BP2- 19807 1:3000 (5% milk) 1:3000 (5% milk) Phosphorylated Protein Kinase C (p- PKC) CST, #9580 1:1000 (5% milk) 1:4000 (5% milk) Ryanodine Receptor 2 (RyR2) Invitrogen, #MA3- 916 1:1000 1:2000 Phospho- Ryanodine Receptor (p- RyR2) Invitrogen, #PA5- 36758 1:1000 1:2000 Sarco/endoplasmic Reticulum Calcium ATPase (ATP2A2/ SERCA2) CST, #4388 1:1000 (5% milk) 1:4000 (5% milk) Sodium/Calcium exchanger 1 (NXC1) ProteinTech, #28447 1:1000 1:2000 Stromal interaction molecule 1 (STIM1) CST, #4916 1:1000 1:2000 Ubiquitin CST, #3933 1:1000 1:2000 Voltage dependent anion channel 2 (VDAC2) CST, #9412 1:1000 1:2000 nloaded from https://physoc.onlinelibrary.w iley.com /doi/10.14814/phy2.70414, W iley O nline L ibrary on [10/06/2025].

    Techniques: Quantitative Proteomics, Standard Deviation