Rabbit anti calnexin antibody

Manufactured by Cell Signaling Technology

Sourced in United States

Rabbit anti-Calnexin antibody is a primary antibody that specifically recognizes the calnexin protein, a calcium-binding chaperone protein located in the endoplasmic reticulum of eukaryotic cells. It is used in various applications, such as Western blotting, immunoprecipitation, and immunofluorescence, to detect and study the expression and localization of calnexin.

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Calnexin (137 citations) Anti-calnexin (54 citations) Rabbit anti-calnexin (16 citations) Calnexin antibody (3 citations) Anti‐Calnexin antibody (2 citations)

3 protocols using rabbit anti calnexin antibody

Subcellular Localization of ATP11A

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36-48 hours after COS7 cells transfection, the transfected cells were washed twice with PBS, fixed with 4% paraformaldehyde, and washed three times with PBS. Cells were then permeabilized and blocked with normal goat serum, Triton X-100, and NaN₃ in PBS for 1 hour at room temperature. ATP11A protein was labeled with mouse anti-Flag antibody (1 : 2000, Sigma, Germany), and the endoplasmic reticulum (ER) was labeled with a rabbit anti-Calnexin antibody (1 : 1000, Cell Signaling Technology, CA, USA). The Golgi apparatus was labeled with a rabbit anti-GM130 antibody (1 : 1000, BD Biosciences, Mississauga, ON). The secondary antibodies used were Alexa 488 goat anti-rabbit IgG, Alexa 594 goat anti-mouse IgG (1 : 500, Invitrogen, USA). The images were captured under a Zeiss LSM 800 confocal scanning microscope.

Sun K., Tian W., Li X., Liu W., Yang Y, & Zhu X. (2020). Disease Mutation Study Identifies Critical Residues for Phosphatidylserine Flippase ATP11A. BioMed Research International, 2020, 7342817.

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Exosome Protein Marker Analysis

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The presence of exosome‐specific protein markers and the absence of non‐EV markers on the isolated vesicles were determined by western blotting. Whole‐cell proteins or EVs (5 μg) were separated by 10%–20% SDS‐PAGE, transferred to nitrocellulose membranes, and blocked for 60 min. The membranes were incubated in primary antibody cocktails (diluted in TBS‐T with 5% BSA) overnight at 4°C, washed thrice for 10 min each in TBS‐T, and incubated in secondary antibody cocktails for 60 min at room temperature. The membranes were washed thrice for 10 min each in TBS‐T and developed using the ECL prime detection kit (GE Healthcare, Chicago, IL, USA). The emitted light was measured using the C‐DiGit blot scanner, and the images were analysed using Image studio for C‐DiGit (LI‐COR Biosciences, Lincoln, NE, USA). The antibodies used were mouse anti‐CD9 antibody (12A12; COSMO BIO), 1/1,000; mouse anti‐CD81 antibody (12C4; COSMO BIO), 1/1,000; mouse anti‐ALIX antibody (ab117600; Abcam, Cambridge, UK), 1/500; mouse anti‐GAPDH antibody (ab8245; Abcam), 1/1,000; rabbit anti‐calnexin antibody (2679; Cell Signalling Technology, Danvers, MA, USA), 1/1,000; anti‐mouse IgG, HRP‐linked antibody (7076; Cell Signalling Technology), 1/2,000; and anti‐rabbit IgG, HRP‐linked antibody (7074; Cell Signalling Technology), 1/2,000.

Yamana K., Inoue J., Yoshida R., Sakata J., Nakashima H., Arita H., Kawaguchi S., Gohara S., Nagao Y., Takeshita H., Maeshiro M., Liu R., Matsuoka Y., Hirayama M., Kawahara K., Nagata M., Hirosue A., Toya R., Murakami R., Kuwahara Y., Fukumoto M, & Nakayama H. (2021). Extracellular vesicles derived from radioresistant oral squamous cell carcinoma cells contribute to the acquisition of radioresistance via the miR‐503‐3p‐BAK axis. Journal of Extracellular Vesicles, 10(14), e12169.

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Subcellular Localization of TMEM30A and ATP8A2

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COS7 cells were cultured in Dulbecco’s modified Eagle’s medium/GlutaMAX (Invitrogen, CA, USA) supplemented with 10% fetal bovine serum (Invitrogen) and 100 units/ml penicillin/streptomycin (Invitrogen) under 5% CO₂ at 37 °C. The cells were transiently transfected with HA-tagged TMEM30A or Flag-tagged ATP8A2. After 2 days, the transfected cells were fixed with 4% paraformaldehyde, and the TMEM30A proteins were visualized using rat anti-HA antibody (Roche, Redwood City, CA, USA). The ER marker proteins were labeled with a rabbit anti-Calnexin antibody (Cell Signaling Technology, CA, USA), the Golgi markers were labeled with a rabbit anti-GM130 antibody (BD Biosciences, Mississauga, ON). The early endosomes were labeled with an antibody against the specific marker Rab11a (BD Biosciences, Heidelberg, Germany). The secondary antibodies used included goat anti-rabbit Alexa 488, goat anti-rabbit Alexa 594, goat anti-mouse Alexa 488, goat anti-mouse Alexa 594, donkey anti-rat Alexa 488 and donkey anti-rat Alexa 633 (Invitrogen). The images were captured under a Zeiss LSM 800 confocal scanning microscope.

Yang Y., Sun K., Liu W., Zhang L., Peng K., Zhang S., Li S., Yang M., Jiang Z., Lu F, & Zhu X. (2018). Disruption of Tmem30a results in cerebellar ataxia and degeneration of Purkinje cells. Cell Death & Disease, 9(9), 899.

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