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AB15123

Anti-Aquaporin 7 antibody

4

(1 Review)

|

(4 Publications)

Chicken Polyclonal Aquaporin 7 antibody. Suitable for ELISA, WB, ICC/IF and reacts with Rat samples. Cited in 4 publications.

View Alternative Names

Aquaporin-7, AQP-7, Aquaglyceroporin-7, Aqp7

Key facts

Host species

Chicken

Clonality

Polyclonal

Isotype

IgY

Carrier free

No

Reacts with

Rat

Applications

WB, ELISA, ICC/IF

applications

Immunogen

Synthetic Peptide within Rat Aquaporin-7. The exact immunogen used to generate this antibody is proprietary information.

P56403

Reactivity data

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Properties and storage information

Purity
Whole antiserum
Shipped at conditions
Blue Ice
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Aquaporin 7 (AQP7) sometimes referred to as AQPap is a protein channel that enables the transport of water and small molecules like glycerol across cell membranes. It has a molecular mass of approximately 28 kDa. This protein is widely expressed in adipose tissue kidney and testis where it facilitates critical cellular processes by regulating water and solute flow. The localization of AQP7 in these tissues highlights its key role in the body’s fluid management and metabolic regulation.
Biological function summary

AQP7 plays an important role in maintaining the balance of glycerol and water within cells which is essential for energy homeostasis. It does not function as part of a known complex but works as an individual tetrameric channel. In adipose tissue AQP7 facilitates the release of glycerol consequently affecting lipid metabolism and energy storage. This function contributes significantly to how organisms respond to energy demands and metabolic changes.

Pathways

AQP7 is critical in glycerol transport and lipid metabolism pathways impacting insulin signaling and glucose regulation. AQP7 is closely associated with proteins like adipose triglyceride lipase (ATGL) and hormone-sensitive lipase (HSL) which regulate lipid breakdown and mobilization. The interplay between these proteins and AQP7 illustrates its importance in pathways that govern energy balance and metabolic flexibility affecting how cells use stored energy.

AQP7 has associations with metabolic conditions such as obesity and type 2 diabetes. Altered expression or functionality of AQP7 in adipose tissue can influence glycerol release and consequently lipid and glucose metabolism. Dysregulation of AQP7 may also impact metabolic processes by interacting with proteins involved in lipid metabolism like ATGL and HSL. These connections highlight the significance of AQP7 in understanding the molecular basis of metabolic diseases.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Aquaglyceroporins form homotetrameric transmembrane channels, with each monomer independently mediating glycerol and water transport across the plasma membrane along their osmotic gradient. Could also be permeable to urea (PubMed : 9252401). Mediates the efflux of glycerol, formed upon triglyceride hydrolysis, to avoid its accumulation in adipocytes and to make it available to other tissues. In the kidney, mediates the reabsorption of glycerol, preventing its loss in urine, again participating to energy homeostasis. In pancreatic beta cells, it also mediates the efflux of glycerol, regulating its intracellular levels (By similarity).
See full target information Aquaporin-7

Publications (4)

Recent publications for all applications. Explore the full list and refine your search

Animals : an open access journal from MDPI 13: PubMed37048414

2023

Morphological and Molecular Investigations of Aquaporin-7 (AQP-7) in Male Reproductive Organs.

Applications

Unspecified application

Species

Unspecified reactive species

Thnaian A Al-Thnaian

Journal of oncology 2021:8114327 PubMed34512754

2021

Involvement of Expression in Hepatitis B Virus-Related Hepatocellular Carcinoma.

Applications

Unspecified application

Species

Unspecified reactive species

Shaoliang Zhu,Hang Ye,Xiaojie Xu,Weiru Huang,Ziyu Peng,Yingyang Liao,Ningfu Peng

ERJ open research 4: PubMed29577041

2018

Peripheral alveolar nitric oxide concentration reflects alveolar inflammation in autoimmune pulmonary alveolar proteinosis.

Applications

Unspecified application

Species

Unspecified reactive species

Taizou Hirano,Shinya Ohkouchi,Naoki Tode,Makoto Kobayashi,Manabu Ono,Teruyuki Satoh,Yoichiro Mitsuishi,Akira Watanabe,Masao Tabata,Toshiya Irokawa,Hiromasa Ogawa,Hisatoshi Sugiura,Toshiaki Kikuchi,Keiichi Akasaka,Ryushi Tazawa,Yoshikazu Inoue,Koh Nakata,Hajime Kurosawa,Masakazu Ichinose

Reproduction in domestic animals = Zuchthygiene 51:665-79 PubMed27405395

2016

Membrane Stress During Thawing Elicits Redistribution of Aquaporin 7 But Not of Aquaporin 9 in Boar Spermatozoa.

Applications

Unspecified application

Species

Unspecified reactive species

A Vicente-Carrillo,H Ekwall,M Álvarez-Rodríguez,H Rodríguez-Martínez
View all publications

Product promise

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