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A4979

Sigma-Aldrich

Anti-Water Channel Aquaporin 5 antibody produced in rabbit

affinity isolated antibody, lyophilized powder

Synonyme(s) :

Anti-AQP-5, Anti-PPKB

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About This Item

Numéro MDL:
MFCD02262548
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

200

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

lyophilized powder

Espèces réactives

mouse, rat

Technique(s)

western blot: 1:200-1:500 using mouse salivary gland and rat lung

Numéro d'accès UniProt

Q9WTY4

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

mouse ... Aqp5(11830)
rat ... Aqp5(25241)

Description générale

Anti-Water Channel Aquaporin 5 binds to aquaporin 5 from mouse salivary gland and rat lung membranes.
Aquaporin-5 is part of a family of aquaporins that function to transport water across cell membranes. AQP5 is involved in tear, saliva, and sweat production.
Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0).

Immunogène

peptide corresponding to residues 251-265 of rat AQP5. The sequence is identical in mouse and 10/16 residues identical in human.

Application

Rabbit Anti-Water Channel Aquaporin 5 antibody can be used for western blot at a dilution of 1:200-1:500 using mouse salivary gland and rat lung tissue extracts.

Forme physique

Lyophilized from phosphate buffered saline, pH 7.4, 1% BSA, ≤0.1% sodium azide.

Clause de non-responsabilité

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Christian Müller et al.
The Journal of experimental biology, 209(Pt 20), 4067-4076 (2006-10-07)
Using primers against highly conserved regions of mammalian and bird aquaporins in RT-PCR experiments, we amplified products derived from duck (Anas platyrhynchos) nasal gland RNA that were identified as homologues of mammalian and chicken aquaporin 1 and aquaporin 5 cDNAs
A S Verkman et al.
American journal of physiology. Renal physiology, 278(1), F13-F28 (2000-02-08)
The aquaporins (AQPs) are a family of small membrane-spanning proteins (monomer size approximately 30 kDa) that are expressed at plasma membranes in many cells types involved in fluid transport. This review is focused on the molecular structure and function of
J W Snuggs et al.
Scientific reports, 11(1), 3164-3164 (2021-02-06)
The central region of the intervertebral disc (IVD) is rich in proteoglycans, leading to a hyperosmotic environment, which fluctuates with daily loading. The cells of the nucleus pulposus (NP cells) have adapted to this environment via the function of tonicity
Michael G Haase et al.
The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society, 62(5), 355-368 (2014-03-29)
Ionizing radiation (IR) leads to fibrosing alveolitis (FA) after a lag period of several weeks to months. In a rat model, FA starts at 8 weeks after IR. Before that, at 5.5 weeks after IR, the transcription factors Sp1 (stimulating
Peter Agre et al.
The Journal of physiology, 542(Pt 1), 3-16 (2002-07-04)
The water permeability of biological membranes has been a longstanding problem in physiology, but the proteins responsible for this remained unknown until discovery of the aquaporin 1 (AQP1) water channel protein. AQP1 is selectively permeated by water driven by osmotic
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