The endoplasmic reticulum is an organelle consisting of a network of cisternae, tubules, and vesicles which are continuous with the outer membrane of the nuclear envelope. The endoplasmic reticulum occurs in two forms: smooth endoplasmic reticulum and rough endoplasmic reticulum.

The smooth endoplasmic reticulum varies in specific function depending on the cell type, but it is generally involved in lipid and steroid synthesis, detoxification, and calcium homeostasis. The rough endoplasmic reticulum is bound by ribosomes, which are the sites of protein synthesis. These proteins collect in the endoplasmic reticulum for transport throughout the cell.

Endoplasmic reticulum marker antibodies detect proteins specific to the endoplasmic reticulum and can aid in the study of the structure and functions of the endoplasmic reticulum. Endoplasmic reticulum marker antibodies can also help elucidate the role or roles a protein may play in a number of tasks that are centered in or influenced by the endoplasmic reticulum. Endoplasmic reticulum marker antibodies are particularly useful in labeling fixed cells. Quality Invitrogen endoplasmic reticulum marker antibodies are available for your research needs.

Endoplasmic reticulum marker antibody targets

  • APP
  • ATP2A2
  • BCHE
  • CALR
  • COL1A1
  • CYP2E1
  • DDIT3
  • DIg4
  • EGFR
  • HMOX1
  • HMOX2
  • HSP90B1
  • HSPA1A
  • IFNG
  • KDELR1
  • MYBPC2
  • P4HB
  • PDIA4
  • RYR1
  • TAP1
  • TAPBP
  • TP53
  • UGGT1
  • VCP

Featured product data

Immunohistochemistry detection of iNOS performed on normal deparaffinized human heart tissue. To expose target proteins, heat-induced antigen retrieval was performed using 10 mM sodium citrate (pH 6.0) buffer, microwaved for 8–15 minutes. Following antigen retrieval, tissues were blocked in 3% BSA-PBS for 30 minutes at room temperature. Tissues were then probed at a dilution of 1:200 with a rabbit polyclonal antibody recognizing iNOS (Cat. No. PA1-036) or without primary antibody (negative control) overnight at 4°C in a humidified chamber. Tissues were washed extensively with PBST and endogenous peroxidase activity was quenched with a peroxidase suppressor. Detection was performed using a biotin-conjugated secondary antibody and SA-HRP, followed by colorimetric detection using DAB. Tissues were counterstained with hematoxylin and prepped for mounting.


Immunohistochemistry detection of SERCA2 ATPase performed on normal deparaffinized human tonsil tissue tissues. To expose target proteins, heat-induced antigen retrieval was performed using 10 mM sodium citrate (pH 6.0) buffer, microwaved for 8–15 minutes. Following antigen retrieval tissues were blocked in 3% BSA-PBS for 30 minutes at room temperature. Tissues were then probed at a dilution of 1:200 with a mouse monoclonal antibody recognizing SERCA2 ATPase (Cat. No. MA3-919) or without primary antibody (negative control) overnight at 4°C in a humidified chamber. Tissues were washed extensively with PBST and endogenous peroxidase activity was quenched with a peroxidase suppressor. Detection was performed using a biotin-conjugated secondary antibody and SA-HRP, followed by colorimetric detection using DAB. Tissues were counterstained with hematoxylin and prepped for mounting.


Immunofluorescent analysis of Phalloidin (purple) and Calreticulin (green) in A431 cells. Formalin fixed cells were permeabilized with 0.1% Triton X-100 in PBS for 10 minutes at room temperature and blocked with 2% BSA (Cat. No. 37525) in PBS + 0.1% Triton X-100 for 30 minutes at room temperature. Cells were probed with a calreticulin polyclonal antibody (Cat. No. PA3-900) at a dilution of 1:75 for at least 1 hour at room temperature, washed with PBS, and incubated with DyLight 488−conjugated goat anti-rabbit IgG secondary antibody (Cat. No. 35552) at a dilution of 1:250 for 30 minutes at room temperature. F-actin was stained with DyLight 650−conjugated phalloidin (Cat. No. 21838) at a dilution of 1:120 (2.5 units/mL final concentration) and nuclei (blue) were stained with Hoechst 33342 dye (Cat. No. 62249) at a concentration of 1 µg/mL for 30 minutes.


Annotated product references

Cat. No. MA3-919 was used in western blot to study whether cleavage of the inositiol 1,4,5-trisphosphate receptor is a cause or an effect of apoptotic Ca2+ release. Akimzhanov AM, Barral JM, Boehning D (2013) Caspase 3 cleavage of the inositol 1,4,5-trisphosphate receptor does not contribute to apoptotic calcium release. Cell Calcium 53:152−158.

Cat. No. MA3-919 was used in immunohistochemistry and western blot to study the expression and localization of protein 4.1 isoforms in cardiac muscle and the significance for cardiomyocyte Ca2+ metabolism. Pinder JC, Taylor-Harris PM, Bennett PM et al. (2012) Isoforms of protein 4.1 are differentially distributed in heart muscle cells: relation of 4.1R and 4.1G to components of the Ca2+ homeostasis system. Exp Cell Res 318:1467−1479.

Cat. No. PA3-900 was used in western blot to study the correlation between serum calreticulin levels and rheumatoid arthritis disease activity. Ni M, Wei W, Wang Y et al. (2013) Serum levels of calreticulin in correlation with disease activity in patients with rheumatoid arthritis. J Clin Immunol 33:947−953.

Cat. No. PA3-900 was used in immunocytochemistry and immunohistochemistry to study the role of calreticulin levels in modulating motoneuron vulnerability to amyotrophic lateral sclerosis. Bernard-Marissal N, Moumen A, Sunyach C et al. (2012) Reduced calreticulin levels link endoplasmic reticulum stress and Fas-triggered cell death in motoneurons vulnerable to ALS. J Neurosci 32:4901− 4912.

Cat. No. PA1-036 was used in immunohistochemistry to study the protective effect of cannabidiol against renal ischemia/reperfusion injury in rats. Fouad AA, Al-Mulhim AS, Jresat I (2012) Cannabidiol treatment ameliorates ischemia/reperfusion renal injury in rats. Life Sci 91:284−292.

Cat. No. PA1-036 was used in western blot to study the role of the expression profile of iNOS and arginase in rat macrophages in their resistance to Toxoplasma gondii infection. Li Z, Zhao ZJ, Zhu XQ et al. (2012) Differences in iNOS and arginase expression and activity in the macrophages of rats are responsible for the resistance against T. gondii infection. PLoS One 7:e35834.

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