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Anti rbcs

Manufactured by Agrisera
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Sourced in Sweden

Anti-RbcS is a laboratory product used to detect and quantify the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase (RbcS), a key enzyme involved in the carbon fixation process of photosynthesis. It provides a tool for researchers to study the expression and regulation of this important photosynthetic protein.

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Lab products found in correlation

Anti rbcl, by Agrisera (4 mentions) Anti plant actin rabbit polyclonal antibody, by EASYBIO (2 mentions) Anti psad, by Agrisera (2 mentions) Anti atpb, by Agrisera (2 mentions) Anti psbc, by Agrisera (2 mentions) Anti ra, by Agrisera (2 mentions) Anti ugpase antibodies, by Agrisera (2 mentions) Las 4000 image analyzer, by GE Healthcare (1 mentions) Tnt quick coupled transcription translation system, by Promega (1 mentions) Ecl detection system, by GE Healthcare (1 mentions) Anti psba, by Agrisera (1 mentions)

4 protocols using anti rbcs

1

Protein Expression and Phosphorylation Analysis

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Protein expression and phosphorylation were assessed using standard Western blotting protocols described by Chen and colleagues [63]. Blots were probed with rabbit polyclonal anti-AtpB, anti-PsaD, anti-PsbC, anti-RA, anti-RbcL, anti-RbcS, and anti-UGPase antibodies (Agrisera Antibodies, Vännäs, Sweden) and an anti-plant-actin rabbit polyclonal antibody (EasyBio, Beijing, China). The rabbit polyclonal anti-PPDK and anti-PEPCK antibodies were prepared by our laboratory.
Gao Z.F., Shen Z., Chao Q., Yan Z., Ge X.L., Lu T., Zheng H., Qian C.R, & Wang B.C. (2020). Large-scale Proteomic and Phosphoproteomic Analyses of Maize Seedling Leaves During De-etiolation. Genomics, Proteomics & Bioinformatics, 18(4), 397-414.
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2

Isolation and Analysis of Chloroplast Proteins

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The protocol for isolating intact chloroplasts from 21‐day‐old leaves was described previously (Sun, Chen, Lin, & Li, 2001 (link)). [35S]‐methionine‐labeled proteins were synthesized through in vitro transcription and in vitro translation of wheat germ extracts (TnT Quick Coupled Transcription/Translation System, Promega) according to the manufacturer's specifications. Labeled proteins were separated by 10% SDS‐PAGE and quantified with a PhosphorImager SP system (Molecular Dynamics). For immunoblot analysis, 25 μg of chloroplast proteins were fractionated by 4%–12% SDS‐PAGE, blotted onto polyvinylidene difluoride membrane, and hybridized with anti‐Toc33, anti‐RbcL, anti‐RbcS, or anti‐GS2 antiserum (Agrisera, Sweden) according to manufacturer's suggestion. Western blot signals were quantified using a LAS 4000 image analyzer (GE Healthcare) and calibrated based on the signals for Col‐0.
Yang C., Yan W., Chang H, & Sun C. (2022). Arabidopsis CIA2 and CIL have distinct and overlapping functions in regulating chloroplast and flower development. Plant Direct, 6(1), e380.
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3

Protein Profiling of Plant Extracts

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Protein extracts from plants were subjected to SDS-PAGE followed by either Coomassie Brilliant Blue (CBB) staining or immunoblot analysis. Immunoreactive signals were detected using an ECL detection system (GE Healthcare) with the following antibodies: anti-RBCL (1:1000 dilution), anti-RBCS (1:1000), anti-PSBA (1:5000), and anti-PGL35 (1:1000) (Agrisera, Sweden).
Tamura K., Kawabayashi T., Shikanai T, & Hara-Nishimura I. (2016). Decreased Expression of a Gene Caused by a T-DNA Insertion in an Adjacent Gene in Arabidopsis. PLoS ONE, 11(2), e0147911.
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4

Western Blot Analysis of Photosynthetic Proteins

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Protein expression and phosphorylation were assessed using standard western blotting protocols described by Chen et al. [64] . Blots were probed with rabbit polyclonal anti-AtpB, anti-PsaD, anti-PsbC, anti-RA, anti-RbcL, anti-RbcS and anti-UGPase antibodies (Agrisera Antibodies, Vä nnä s, Sweden) and an anti-plant-actin rabbit polyclonal antibody (EasyBio, Beijing, China). The rabbit polyclonal anti-PPDK, anti-PEPCK and phosphosite-specific anti-PT527 PPDK antibodies were prepared by our laboratory.
Gao Z., Shen Z., Chao Q., Yan Z., Ge X., Lu T., Zheng H., Qian C., & Wang B. (2020). Large-scale Proteomic and Phosphoproteomic Analysis of Maize Seedling Leaves During De-etiolation.
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