Anti bip

Manufactured by Agrisera

Sourced in Sweden

Anti-BiP is a polyclonal antibody raised against the endoplasmic reticulum chaperone protein BiP (Binding Immunoglobulin Protein), also known as GRP78 (Glucose-Regulated Protein 78). This antibody can be used to detect the expression of BiP in various cell and tissue samples.

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Lab products found in correlation

Anti gfp, by Thermo Fisher Scientific (1 mentions) Goat anti rabbit horseradish peroxidase conjugate, by Abcam (1 mentions) Anti h atpase, by Agrisera (1 mentions) Anti vp16, by Abcam (1 mentions) Anti rfp, by Abcam (1 mentions) Anti ha, by Roche (1 mentions) Gradient gel, by Bio-Rad (1 mentions) Supersignal west femto maximum sensitivity substrate, by Thermo Fisher Scientific (1 mentions) Nitrocellulose membrane, by Bio-Rad (1 mentions) Anti gfp, by Abcam (1 mentions) Trans blot, by Bio-Rad (1 mentions) Anti pr1, by Agrisera (1 mentions) Goat anti rabbit igg secondary antibody, by Thermo Fisher Scientific (1 mentions) Supersignal west femto maximum sensitivity chemiluminescent substrate, by Thermo Fisher Scientific (1 mentions) Anti coxii, by Agrisera (1 mentions) Pierce horseradish peroxidase, by Thermo Fisher Scientific (1 mentions) Imagelab software version 4, by Bio-Rad (1 mentions) Chemidoc mp imager, by Bio-Rad (1 mentions) V atpase, by Agrisera (1 mentions) Anti gfp ht801 01, by Transgene (1 mentions)

4 protocols using anti bip

Immunogold Labeling and Immunoblot Analysis

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Antibodies of anti‐low‐molecular‐weight glutenins‐glutenins (LMW‐GSs), HMW‐GSs and γ‐gliadins were synthesized as previously described (Loussert et al., 2008 ) and used at 1 : 100 for immunogold labelling. Anti‐BiP (AS09 481; Agrisera, Vännäs, Sweden), and gold‐conjugated anti‐rabbit IgG (10 nm, EM.GAR10; BBInternational, Cardiff, UK) were used at 1 : 100 for immunogold labelling. Anti‐ATG8 (AS14 2769; Agrisera), anti‐GFP (HT801‐01; TransGen Biotech, China), Anti‐BiP (AS09 481; Agrisera), anti‐eEF1α (AS10 934; Agrisera), anti‐actin (A0480; Sigma), anti‐mouse IgG (BE0102‐100; Easybio, China) and anti‐rabbit IgG (BE0101‐100; Easybio) antibodies were all used at 1 : 5000 for immunoblot analysis.

Chen Q., Yang C., Zhang Z., Wang Z., Chen Y., Rossi V., Chen W., Xin M., Su Z., Du J., Guo W., Hu Z., Liu J., Peng H., Ni Z., Sun Q, & Yao Y. (2022). Unprocessed wheat γ‐gliadin reduces gluten accumulation associated with the endoplasmic reticulum stress and elevated cell death. The New Phytologist, 236(1), 146-164.

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Immunoblotting Protocols for Protein Analysis

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The 5-kDa and 9-kDa small proteins were separated on 13% Tris-Tricine polyacrylamide gels. Proteins of molecular weight larger than 20-kDa were analyzed with 12% Tris-Glycine polyacrylamide gels, and then processed for immunoblotting, following the protocols described before [12 (link),28 (link),32 (link)]. Primary antibodies used included anti-GFP (Thermo, Waltham, MA, USA), anti-LIYV CP, anti-LIYV P26, anti-LIYV P5, anti-LIYV P9, and anti-BiP (Agrisera, Vännäs, Sweden) protein polyclonal antibodies produced in rabbit. The secondary antibody was horseradish peroxidase-conjugated goat anti-rabbit IgG.

Qiao W., Helpio E.L, & Falk B.W. (2018). Two Crinivirus-Conserved Small Proteins, P5 and P9, Are Indispensable for Efficient Lettuce infectious yellows virus Infectivity in Plants. Viruses, 10(9), 459.

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Immunoblot Analysis of Protein Expression

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Samples were suspended in the Laemmli buffer and resolved on SDS-PAGE using 4%–20% gradient gels (Bio-Rad, Hercules, CA, USA) at ∼5 mg/lane total protein. For immunoblot, proteins resolved on gels were transferred to nitrocellulose membranes (Bio-Rad) using Transblot (Bio-Rad). After incubating in blocking buffer (5% [w/v] nonfat dry milk, 1×Tris-buffered saline [TBS; 150 mM NaCl, 50 mM Tris–HCl, pH 7.5, 0.1% Tween-20]), membranes were first probed with primary antibodies diluted in 2.5% (w/v) nonfat dry milk, 1× TBS; anti-SYP132 (1:3,000, Agrisera), anti-AHA1 (1:3,000, Eurogentec), anti-RFP (1: 10,000; Abcam, Cambridge, UK), anti-GFP (1:10,000; Abcam), anti-H⁺-ATPase (1:10,000; Agrisera), anti-PR1 (1:10,000; Agrisera), anti-BIP (1:10,000; Agrisera), anti-HA (1:10,000; Roche, Basel, Switzerland), or anti-VP16 (1:10,000; Abcam). Subsequently, after washing with wash buffer (1× TBS), secondary antibody goat anti-rabbit-horseradish peroxidase conjugate (1:20,000; Abcam) was applied. Proteins were visualized using SuperSignal West Femto Maximum Sensitivity Substrate (Thermo Scientific) and imaged by Fusion Chemiluminescence imager (Vilber, Marne-la-Vallée, France). Total proteins were visualized by staining the membrane with Coomassie or Ponceau. Band density was measured by densitometry using the ImageJ software.

Baena G., Xia L., Waghmare S, & Karnik R. (2022). SNARE SYP132 mediates divergent traffic of plasma membrane H+-ATPase AHA1 and antimicrobial PR1 during bacterial pathogenesis. Plant Physiology, 189(3), 1639-1661.

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Protein Fractions Separation and Western Blotting

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Protein fractions (10 μg of each) were separated using NuPAGE Novex 4%–12% Bis-Tris Protein SDS-PAGE Gels (ThermoFisher Scientific) and proteins transferred onto nitrocellulose membranes using the iBLOT 2 dry blot system (Life Technologies, Carlsbad, CA, USA) according to the manufacturer’s instructions. Western blotting was performed using the SNAP2 blot system (Merck Millipore, Billerica, MA, USA). Membranes were probed with 1:1000 dilutions of antibodies directed against the following proteins: reversibly glycosylated protein 1 (α-RGP 1) from pea (kindly provided by Kanwarpal Dhugga, Dupont Pioneer, Aurelia, IA, USA) as a marker for the GA, the PM H⁺-ATPase (Agrisera, Vännäs, Sweden) as a PM marker, cytochrome-c oxidase subunit II (anti-COX II) (Agrisera) as a marker for mitochondria (MT), luminal-binding protein (anti-BiP) (Agrisera) as a marker for ER and the vanadate-sensitive ATPase epsilon subunit (V-ATPase) (Agrisera) as a vacuole marker. Primary antibodies were detected with goat anti-rabbit IgG secondary antibody (1:2000 dilution) conjugated to Pierce horseradish peroxidase (ThermoFisher Scientific) and SuperSignal West Femto Maximum Sensitivity chemiluminescent substrate (ThermoFisher Scientific), then digitally captured using a Chemi-Doc MP imager (Bio-Rad, Hercules, CA, USA) and analyzed using the Image Lab software version 4.1 (Bio-Rad).

Ford K.L., Chin T., Srivastava V., Zeng W., Doblin M.S., Bulone V, & Bacic A. (2016). Comparative “Golgi” Proteome Study of Lolium multiflorum and Populus trichocarpa. Proteomes, 4(3), 23.

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