Rabbit anti bip

Manufactured by Cell Signaling Technology

Sourced in United States, United Kingdom

Rabbit anti-BiP is a primary antibody that recognizes the Binding Immunoglobulin Protein (BiP), also known as Glucose-Regulated Protein 78 (GRP78). BiP is an endoplasmic reticulum chaperone protein that plays a crucial role in the unfolded protein response.

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Close spelling variants of this product

Anti-BiP (69 citations) Rabbit anti-Bip antibody (5 citations) Rabbit polyclonal anti-BIP (3 citations) Rabbit anti-human BiP (2 citations)

7 protocols using rabbit anti bip

Comprehensive Antibody Panel for Autophagy and UPR Analysis

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Rabbit anti-LC3B (#3868), rabbit anti-ATG5 (#12994), rabbit anti-ATG7 (#8558), rabbit anti-Beclin-1 (#3495), rabbit anti-ATG16L1 (#8089), rabbit anti-BIP (#3177), rabbit anti-ATF6 (#65880), rabbit anti-ATF4(#11815), rabbit anti-XBP1 (#12782), rabbit anti-PERK (#5683), rabbit anti-IRE1 (#3294), rabbit anti-p-eif2α (#3398), rabbit anti-FIP200 (#12436), and mouse anti-CHOP (#2895) antibodies were purchased from Cell Signaling Technology (Danvers, MA, USA) (dilution concentration 1:1000). Rabbit anti-p-IRE1 (PA1-16927) was purchased from Invitrogen (Waltham, MA, USA) (dilution concentration 1:1000). Mouse anti-p62 (18420-1-AP), mouse anti-HA-tag (66006-2-Ig), and mouse anti-β-actin (66009-1-Ig) were purchased from Proteintech (Wuhan, China) (dilution concentration 1:5000). HRP-conjugated goat anti-mouse (G1214) and goat anti-rabbit (G1213) were purchased from Servicebio (Wuhan City, China) (dilution concentration 2:5000). Alexa Fluor 568 goat anti-mouse IgG, IgM (H + L) (A-11004) and Alexa Fluor 647 goat anti-mouse-IgG (H + L) (A-21445) were purchased from Thermo Fisher (Waltham, MA, USA) (dilution concentration 1:500). Immunofluorescence antibodies were diluted in PBS. Immunoblot antibodies were diluted in TBST.

Su W.Q., Yu X.J, & Zhou C.M. (2021). SARS-CoV-2 ORF3a Induces Incomplete Autophagy via the Unfolded Protein Response. Viruses, 13(12), 2467.

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Immunohistochemistry of Rat ACC

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After deep anesthesia with pentobarbital sodium, the rats were transcardially perfused with 150 mL of 1 × phosphate buffered saline (PBS) (4 °C), followed by 150 mL of 4% paraformaldehyde (4 °C). The ACC was harvested, fixed with 4% paraformaldehyde for 48 h, and then dehydrated with 30% sucrose for 3 days at 4 °C. Subsequently, the ACC was transversely cut into slices (30-µm thick). The sections were blocked with 10% sheep or donkey serum for 2 h at room temperature and incubated with the following primary antibodies for 48 h at 4 °C: goat-anti-Iba1 (1:200, Abcam, Cambridge, UK), mouse anti-GFAP (1:500, Cell Signaling Technology), mouse anti-NeuN (1:2000, Abcam), rabbit anti-BIP (1:500, Cell Signaling Technology), and rabbit-anti-IRE-1 (1:1000, Proteintech). The sections were washed with 1 × PBS and incubated with fluorescent secondary antibodies in the dark for 2 h at room temperature. Finally, the sections were examined under a fluorescence microscope (FV3000; Olympus, Tokyo, Japan).

Ma L.W., Liu Y.F., Zhang H., Huang C.J., Li A., Qu X.Z., Lin J.P., Yang Y, & Yao Y.X. (2024). Electroacupuncture attenuates neuropathic pain via suppressing BIP-IRE-1α-mediated endoplasmic reticulum stress in the anterior cingulate cortex. Biological Research, 57, 34.

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Western Blot Analysis of ER Stress Markers

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After deep anesthesia with pentobarbital sodium, the rats were decapitated, the brain was harvested, and the ACC was divided into the left (Ipsi.) and right (Contra.) sections as described in our previous study [27 (link)]. The ipsilateral protein samples were separated by SDS-PAGE and transferred to a PVDF membrane. Subsequently, the membranes were blocked in 5% skim milk at room temperature for 1 h before incubation with the following primary antibodies for 24 h at 4 °C: rabbit-anti-BIP (1:500, Cell Signaling Technology, Danvers, MA, USA), rabbit-anti-IRE-1 (1:1000, Proteintech, Rosemont, IL, USA), rabbit-anti-pIRE-1 (1:1000, Proteintech), and mouse-anti-GAPDH (1:10,000, Proteintech). After washing with TBST, the membrane was incubated with an HRP-conjugated secondary antibody for 2 h at room temperature. The ChemiDoc MP System (Bio-Rad, Hercules, CA, USA) was used to detect complex immune bands.

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Characterization of Autophagy Pathways in Cervical Cancer Cells

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Human cervical carcinoma HeLa and SiHa cells were cultured in Dulbecco Modified Eagle Medium (DMEM) containing 10% fetal bovine serum and 1% antibiotics (penicillin, streptomycin, and amphotericin B) at 37°C in a humidified 5% CO₂ incubator. CaSKi cells were cultured in RPMI 1640 medium under the same conditions. When the cells reached 80% confluence, they were trypsinized and seeded into plates/dishes for experiments. WGA (SI-L0636), Z-VAD-FMK (V116), Baf-A1 (B1793), and cycloheximide (C4850) were purchased from Sigma-Aldrich (St. Louis, MO, USA). The rabbit anti-Alfy antibody (AV50850) was also obtained from Sigma-Aldrich. The rabbit anti-LC3B antibody, phosphorylated and total MAPK Family Antibody Sampler Kit, mouse anti-ubiquitin, rabbit anti-Bip, mouse-anti ubiquitin, rabbit anti-phosphorylated ERK and Akt, mouse anti-β-actin, and GAPDH antibodies were purchased from Cell Signaling Technology (Danvers, MA, USA). The ER-tracker was purchased from Invitrogen (Eugene, Oregon, USA).

Tsai T.L., Wang H.C., Hung C.H., Lin P.C., Lee Y.S., Chen H.H, & Su W.C. (2017). Wheat germ agglutinin-induced paraptosis-like cell death and protective autophagy is mediated by autophagy-linked FYVE inhibition. Oncotarget, 8(53), 91209-91222.

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Immunofluorescence Staining of SARS-CoV-2 Organelles

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Rabbit anti-beta-actin (Cell Signaling Technology #4967, RRID:AB_330288); mouse anti-beta tubulin (Sigma-Aldrich #T8328, RRID:AB_1844090); rabbit anti-BiP (Cell Signaling Technology #3177S, RRID:AB_2119845); mouse anti-EEA1 (BD Biosciences #610457, RRID:AB_397830, used at 1:200); mouse anti-ERGIC53 (Enzo Life Sciences #ALX-804-602-C100, RRID:AB_2051363, used at 1:200); anti-GM130; rabbit anti-GRP78 BiP (Abcam #Ab21685, RRID:AB_2119834); rabbit anti–SARS-CoV–nucleocapsid protein (NP) (Rockland #200-401-A50, RRID:AB_828403); rabbit anti-PDI (protein disulfide isomerase) (Cell Signaling Technology #3501, RRID:AB_2156433); mouse anti-Strep tag (QIAGEN #34850, RRID:AB_2810987, used at 1:5000); mouse anti-strepMAB (IBA Lifesciences #2-1507-001, used at 1:1000); rabbit anti–Strep-tag II (Abcam #ab232586); rabbit anti-Tom20 (Proteintech #11802-1-AP, RRID:AB_2207530, used at 1:1000); rabbit anti-Tom20 (Cell Signaling Technology #42406, RRID:AB_2687663); mouse anti-Tom22 (Santa Cruz Biotechnology #sc-101286, RRID:AB_1130526); rabbit anti-Tom40 (Santa Cruz Biotechnology #sc-11414, RRID:AB_793274); mouse anti-Tom70 (Santa Cruz #sc-390545, RRID:AB_2714192, used at 1:500); Rabbit anti-STX5 (Synaptic Systems 110 053, used at 1:500); and ActinStaining Kit 647-Phalloidin (Hypernol #8817-01, used at 1:400).

Gordon D.E., Hiatt J., Bouhaddou M., Rezelj V.V., Ulferts S., Braberg H., Jureka A.S., Obernier K., Guo J.Z., Batra J., Kaake R.M., Weckstein A.R., Owens T.W., Gupta M., Pourmal S., Titus E.W., Cakir M., Soucheray M., McGregor M., Cakir Z., Jang G., O’Meara M.J., Tummino T.A., Zhang Z., Foussard H., Rojc A., Zhou Y., Kuchenov D., Hüttenhain R., Xu J., Eckhardt M., Swaney D.L., Fabius J.M., Ummadi M., Tutuncuoglu B., Rathore U., Modak M., Haas P., Haas K.M., Naing Z.Z., Pulido E.H., Shi Y., Barrio-Hernandez I., Memon D., Petsalaki E., Dunham A., Marrero M.C., Burke D., Koh C., Vallet T., Silvas J.A., Azumaya C.M., Billesbølle C., Brilot A.F., Campbell M.G., Diallo A., Dickinson M.S., Diwanji D., Herrera N., Hoppe N., Kratochvil H.T., Liu Y., Merz G.E., Moritz M., Nguyen H.C., Nowotny C., Puchades C., Rizo A.N., Schulze-Gahmen U., Smith A.M., Sun M., Young I.D., Zhao J., Asarnow D., Biel J., Bowen A., Braxton J.R., Chen J., Chio C.M., Chio U.S., Deshpande I., Doan L., Faust B., Flores S., Jin M., Kim K., Lam V.L., Li F., Li J., Li Y.L., Li Y., Liu X., Lo M., Lopez K.E., Melo A.A., Moss FR I.I.I., Nguyen P., Paulino J., Pawar K.I., Peters J.K., Pospiech TH J.r., Safari M., Sangwan S., Schaefer K., Thomas P.V., Thwin A.C., Trenker R., Tse E., Tsui T.K., Wang F., Whitis N., Yu Z., Zhang K., Zhang Y., Zhou F., Saltzberg D., Hodder A.J., Shun-Shion A.S., Williams D.M., White K.M., Rosales R., Kehrer T., Miorin L., Moreno E., Patel A.H., Rihn S., Khalid M.M., Vallejo-Gracia A., Fozouni P., Simoneau C.R., Roth T.L., Wu D., Karim M.A., Ghoussaini M., Dunham I., Berardi F., Weigang S., Chazal M., Park J., Logue J., McGrath M., Weston S., Haupt R., Hastie C.J., Elliott M., Brown F., Burness K.A., Reid E., Dorward M., Johnson C., Wilkinson S.G., Geyer A., Giesel D.M., Baillie C., Raggett S., Leech H., Toth R., Goodman N., Keough K.C., Lind A.L., Klesh R.J., Hemphill K.R., Carlson-Stevermer J., Oki J., Holden K., Maures T., Pollard K.S., Sali A., Agard D.A., Cheng Y., Fraser J.S., Frost A., Jura N., Kortemme T., Manglik A., Southworth D.R., Stroud R.M., Alessi D.R., Davies P., Frieman M.B., Ideker T., Abate C., Jouvenet N., Kochs G., Shoichet B., Ott M., Palmarini M., Shokat K.M., García-Sastre A., Rassen J.A., Grosse R., Rosenberg O.S., Verba K.A., Basler C.F., Vignuzzi M., Peden A.A., Beltrao P, & Krogan N.J. (2020). Comparative host-coronavirus protein interaction networks reveal pan-viral disease mechanisms. Science (New York, N.y.), 370(6521), eabe9403.

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Western Blot Analysis of GDAP1 Protein

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Snap frozen on dry ice tissues were homogenized in lysis buffer (50mM Tris HCl pH 7.4, 1.5 mM MgCl₂, 5 mM EDTA, 1% Triton X-100, 50 mM NaF, 1mM NA₂VO₃) containing protease inhibitors (Roche). Tissue lysates (30μg) were collected and resolved in sodium docecyl sulfate polyacrylamide gels and transferred onto polyvinylidene difluoride Immobilon-P transfer membrane filters (Millipore, Billerica, MA, USA) using an Amersham Biosciences (Piscataway, NJ, USA) semidry Trans-Blot according to the manufacturer's instructions. The membranes were blotted with rabbit anti-GDAP1 and rabbit anti-β-actin (Sigma-Aldrich), rabbit anti-calreticulin, rabbit anti-β-tubulin, rabbit anti-BiP and rabbit-IP3 Receptor (Cell Signaling) antibodies. Blots were developed using the ECL Prime chemiluminiscent substrate (GE Healthcare Amersham).

Barneo-Muñoz M., Juárez P., Civera-Tregón A., Yndriago L., Pla-Martin D., Zenker J., Cuevas-Martín C., Estela A., Sánchez-Aragó M., Forteza-Vila J., Cuezva J.M., Chrast R, & Palau F. (2015). Lack of GDAP1 Induces Neuronal Calcium and Mitochondrial Defects in a Knockout Mouse Model of Charcot-Marie-Tooth Neuropathy. PLoS Genetics, 11(4), e1005115.

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Immunodetection of membrane proteins

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The following antibodies and reagents were used: mouse anti-Na,K-ATPase β-subunit (clone M17-P5-F11) (Thermo Scientific, Rockford, IL, USA), rabbit anti-GFP (Santa Cruz Biotechnology, Dallas, TX, USA), mouse anti-Na,K-ATPase α-subunit (Merck Millipore, Darmstadt, Germany), rabbit anti-β-actin (Sigma Aldrich, St. Louis, MO, USA), mouse anti-transferrin receptor (Invitrogen, Rockford, IL, USA), rabbit anti-PDI (Cell Signaling, Danvers, MA, USA), rabbit anti-GM130 (Cell Signaling, Danvers, MA, USA), rabbit anti-calnexin (Abcam, Cambridge, UK), rabbit anti-BiP (Cell Signaling, Danvers, MA, USA), HRP-conjugated anti-mouse and anti-rabbit IgG (Cell Signaling, Danvers, MA, USA), and Alexa Fluor 488 and 594 conjugated anti-rabbit, anti-mouse (Thermo Scientific, Eugene, OR, USA). α-ketoglutaric acid was obtained from Sigma Aldrich, St. Louis, MO, USA.

Kryvenko V., Wessendorf M., Morty R.E., Herold S., Seeger W., Vagin O., Dada L.A., Sznajder J.I, & Vadász I. (2020). Hypercapnia Impairs Na,K-ATPase Function by Inducing Endoplasmic Reticulum Retention of the β-Subunit of the Enzyme in Alveolar Epithelial Cells. International Journal of Molecular Sciences, 21(4), 1467.

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