rabbit anti his tag polyclonal antibody  (Epizyme Inc)

Journal: BMC Infectious Diseases

Article Title: Development and evaluation of novel Brucella diagnostic antigen protein ST

doi: 10.1186/s12879-025-12393-1

Figure Lengend Snippet: Validation of ST protein expression and purification. A . SDS-PAGE electrophoresis results. M: Marker; Lane 1: Before IPTG induction; Lane 2: Supernatant of 0.5 M IPTG-induced at 37 °C; Lane 3: Supernatant of 1 M IPTG-induced at 37 °C; Lane 4: Supernatant of 0.5 M IPTG-induced at 25 °C; Lane 5: Supernatant of 1 M IPTG-induced at 25 °C; Lane 6: Supernatant of 0.5 M IPTG-induced at 16 °C; Lane 7: Supernatant of 1 M IPTG-induced at 16 °C; Lane 8: Deposition of 0.5 M IPTG-induced at 37 °C; Lane 9: Deposition of 1 M IPTG-induced at 37 °C; Lane 10: Deposition of 0.5 M IPTG-induced at 25 °C; Lane 11: Deposition of 1 M IPTG-induced at 25 °C; Lane 12: Deposition of 0.5 M IPTG-induced at 16 °C; Lane 13: Deposition of 1 M IPTG-induced at 16 °C. B . Western blot (WB) results of purified HIS tag protein. M: Marker; Lane 1: Purified recombinant protein ST protein

Article Snippet: Finally, the purified ST protein was electrophoresed on a 10% SDS-PAGE gel (Bio-Rad, Hercules, USA; Cat. 161–0183), transferred to a PVDF membrane (Millipore, Burlington, USA; Cat. IPVH00010), washed three times with TBST buffer containing 0.05% Tween 20 (Amersham Biosciences, Little Chalfont, UK; Cat. GE2000) for 10 min each time, and subjected to Western blotting with rabbit anti-His tag polyclonal antibody (Proteintech, Rosemont, USA; Cat. 13844-1-AP) and HRP-labeled goat anti-rabbit IgG antibody (Santa Cruz Biotechnology, Dallas, USA; Cat. sc-2004).

Techniques: Biomarker Discovery, Expressing, Purification, SDS Page, Electrophoresis, Marker, Western Blot, Recombinant

Journal: Cell reports

Article Title: Rice B2 and B3 subgroup RAF kinases play central roles in both ABA and osmotic stress signaling.

doi: 10.1016/j.celrep.2025.115894

Figure Lengend Snippet: Figure 6. Rice B2 and B3 RAFs phosphorylate SAPK9 in vitro and are required for SAPK activation in vivo (A) Add-back assay showing the capability of rice B2 and B3 RAFs to complement the ABA-induced expression of RD29B-LUC in the protoplasts of Arabidopsis OK100-nonu. Values are means ± SD (n = 4 biological replicates). **p < 0.01 and ***p < 0.001, two-sided Student’s t test. (B) Recombinant OsRAF-KDs were used to phosphorylate recombinant SAPK9K51R in the presence of [γ-32p] ATP. Autoradiograph (upper) and Coomassie staining (lower) show phosphorylation and loading of OsRAF-KD and SAPK9K51R, respectively. Asterisks indicate the bands of different OsRAF-KDs. (C) Recombinant OsRAF-KDs phosphorylate the conserved sites in SAPK9K51R in vitro. Autoradiograph (upper) and Coomassie staining (lower) show phos phorylation and loading of OsRAF-KD and SAPK9K51R, respectively. Asterisks indicate the bands of different OsRAF-KDs. (D) Immunoblot by anti-pS166 antibody showing the phosphorylation of the conserved serine corresponding to Ser166 in AtSnRK2.4 (Ser176 in SAPK9) before and after ABA treatment in WT/NIP, raf-b2, raf-b3q, and raf-b2/3q. (E) Immunoblot by anti-pS166 antibody showing the phosphorylation of the conserved serine corresponding to Ser166 in AtSnRK2.4 (Ser176 in SAPK9) before and after ABA treatment in WT/NIP, raf-b2/3q, and pyl1/2/3/4/5/6/12. (F) Immunoblot by anti-pS166 antibody showing the phosphorylation of the conserved serine corresponding to Ser166 in AtSnRK2.4 (Ser176 in SAPK9) before and after mannitol treatment in WT/NIP, raf-b2, raf-b3q, and raf-b2/3q. (G) Immunoblot by anti-pS166 antibody showing the phosphorylation of the conserved serine corresponding to Ser166 in AtSnRK2.4 (Ser176 in SAPK9) before and after mannitol treatment in WT/NIP, raf-b2/3q, and pyl1/2/3/4/5/6/12. Images shown are representative of at least five independent experiments in (D)–(G).

Article Snippet: REAGENT or RESOURCE SOURCE IDENTIFIER Antibodies Mouse monoclonal anti-His ABclonal AE028 Mouse monoclonal anti-GST ABclonal AE077 Rabbit polyclonal anti-pS166 This study N/A Anti-mouse Bio-Rad 1706516 Anti-rabbit ABclonal AS014 Bacterial and virus strains E. coli BL21-CodonPlus (DE3)-RIPL WEIDI EC1007 Agrobacterium tumefaciens (strain GV3101) WEIDI AC1001 Agrobacterium tumefaciens (EHA105) WEIDI AC1010 Biological samples Arabidopsis thaliana: WT (Col-0) N/A Arabidopsis thaliana: OK100-B2 Lin et al., 2021.13 N/A Arabidopsis thaliana: OK100-nonu Lin et al., 2021.13 N/A Arabidopsis thaliana: pyr1/pyl1/2/3/5/8 Gonzalez-Guzman et al., 2012.22 N/A O. sativa L. ssp. Japonica cultivar Nipponbare: WT/NIP N/A Physcomitrium patens: WT N/A Physcomitrium patens: Ppark-1 This study N/A Physcomitrium patens: Ppark-2 This study N/A Rice: raf-b1-48 This study N/A Rice: raf-b1-213 This study N/A Rice: raf-b2-223 This study N/A Rice: raf-b2-238 This study N/A Rice: raf-b3q-478 This study N/A Rice: raf-b3q-502 This study N/A Rice: raf-b2/3q-714 This study N/A Rice: raf-b2/3q-824 This study N/A Rice: pyl1/2/3/4/5/6/12 Miao et al., 2018.46 N/A Rice: OsMAPKKK40pro::OsMAPKKK40pro-mVenus/NIP This study N/A Rice: OsMAPKKK44pro::OsMAPKKK44pro-mVenus/NIP This study N/A Rice: OsMAPKKK1pro::OsMAPKKK1pro-mVenus/NIP This study N/A Rice: OsMAPKKK7pro::OsMAPKKK7pro-mVenus/NIP This study N/A Chemicals, peptides, and recombinant proteins Abscisic Acid Sigma-Aldrich A1049 D-Mannitol Diamond A100122 MES hydrate Sigma-Aldrich M8250 Murashige & skoog basal salt mixture Phytotech M524 Yoshida’s solution Coolaber NS1040-S Minimal SD Base TaKaRa 630411 Agar OKA D11291 Driselase enzyme Sigma D9515 G418 Sulfate Yeasen 60220ES08 Luciferase assay reagent Promega E1483 (Continued on next page) 16 Cell Reports 44, 115894, July 22, 2025

Techniques: In Vitro, Activation Assay, In Vivo, Expressing, Recombinant, Autoradiography, Staining, Phospho-proteomics, Western Blot