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Mouse Anti-AQP8 Recombinant Antibody (1A1) (CBMAB-A0438-LY)

The product is antibody recognizes AQP8. The antibody 1A1 immunoassay techniques such as: WB, ELISA.
See all AQP8 antibodies
Published Data
Fig.1 Detection of marker proteins for myoepithelial cell in parotid glands.
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Fig.2 Immunohistochemistry of parotid glands from diabetic NOD mouse, non-diabetic NOD mouse and control mouse was performed with antibodies for anti-aquaporin 8.
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Fig.3 Decreased marker signals in parotid glands of diabetic NOD mice.
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Summary

Host Animal
Mouse
Specificity
Human, Rat
Clone
1A1
Antibody Isotype
IgG2a, κ
Application
WB, ELISA

Basic Information

Immunogen
AQP8 (AAH40630, 1 a.a. ~ 255 a.a) full-length recombinant protein with GST tag.
Host Species
Mouse
Specificity
Human, Rat
Antibody Isotype
IgG2a, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, pH 7.4
Preservative
None
Concentration
Batch dependent
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
aquaporin 8
Introduction
Aquaporin 8 (AQP8) is a water channel protein. Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). Aquaporin 8 mRNA is found in pancreas and colon but not other tissues. [provided by RefSeq]
Entrez Gene ID
Human343
Rat29172
UniProt ID
HumanO94778
RatP56405
Function
Forms a water-specific channel; mercury-sensitive. Not permeable to glycerol or urea.
Biological Process
Cellular response to cAMP Source: UniProtKB
Water transport Source: Reactome
Cellular Location
Mitochondrion membrane
Topology
Cytoplasmic: 1-36 aa
Helical: 37-57 aa
Extracellular: 58-84 aa
Helical: 85-105 aa
Cytoplasmic: 106-107 aa
Helical: 108-128 aa
Extracellular: 129-156 aa
Helical: 157-177 aa
Cytoplasmic: 178-183 aa
Helical: 184-204 aa
Extracellular: 205-228 aa
Helical: 229-249 aa
Cytoplasmic: 250-261 aa

Li, W., Song, Y., Pan, C., Yu, J., Zhang, J., & Zhu, X. (2021). Aquaporin-8 is a novel marker for progression of human cervical cancer cells. Cancer Biomarkers, (Preprint), 1-10.

Krüger, C., Jörns, A., Kaynert, J., Waldeck-Weiermair, M., Michel, T., Elsner, M., & Lenzen, S. (2021). The importance of aquaporin-8 for cytokine-mediated toxicity in rat insulin-producing cells. Free Radical Biology and Medicine, 174, 135-143.

Cui, F., Hu, M., Li, R., Li, B., Huang, D., Ma, W., ... & Lv, Z. (2021). Insulin on changes in expressions of aquaporin-1, aquaporin-5, and aquaporin-8 in submandibular salivary glands of rats with Streptozotocin-induced diabetes. International Journal of Clinical and Experimental Pathology, 14(2), 221.

O’Brien, S. J., Kalbfleisch, T., Srivastava, S., Pan, J., Rai, S., Petras, R. E., ... & Galandiuk, S. (2021). Decreased Tumoral Expression of Colon-Specific Water Channel Aquaporin 8 Is Associated With Reduced Overall Survival in Colon Adenocarcinoma. Diseases of the Colon & Rectum, 64(9), 1083-1095.

Capiglioni, A. M., Muller, G. L., Marrone, J., Alvarez, M. D. L., & Marinelli, R. A. (2021). Enhanced ammonia detoxification to urea in hepatocytes transduced with human aquaporin‐8 gene. Biotechnology and Bioengineering.

Vilchis‐Landeros, M., Guinzberg, R., Riveros‐Rosas, H., Villalobos‐Molina, R., & Piña, E. (2020). Aquaporin 8 is involved in H2O2‐mediated differential regulation of metabolic signaling by α1‐and β‐adrenoceptors in hepatocytes. FEBS letters, 594(10), 1564-1576.

Schnabel, B., Kuhrt, H., Wiedemann, P., Bringmann, A., & Hollborn, M. (2020). Osmotic regulation of aquaporin-8 expression in retinal pigment epithelial cells in vitro: Dependence on KATP channel activation. Molecular Vision, 26, 797.

Wang, D., Di, X., Wang, J., Li, M., Zhang, D., Hou, Y., ... & Su, W. (2018). Increased formation of follicular antrum in aquaporin-8-deficient mice is due to defective proliferation and migration, and not steroidogenesis of granulosa cells. Frontiers in physiology, 9, 1193.

Bestetti, S., Medraño-Fernandez, I., Galli, M., Ghitti, M., Bienert, G. P., Musco, G., ... & Sitia, R. (2018). A persulfidation-based mechanism controls aquaporin-8 conductance. Science advances, 4(5), eaar5770.

Hayashi, R., Hayashi, S., Fukuda, K., Sakai, M., & Machida, S. (2017). Immunolocation of aquaporin 8 in human cataractous lenticular epithelial cells. Biomedicine hub, 2(3), 1-5.

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For research use only. Not intended for any clinical use.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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