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NSJ Bioreagents

SKU:R31206

Aquaporin 9 Antibody

Aquaporin 9 Antibody

Regular price $449.00 USD
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Aquaporin-9 is a protein that in humans is encoded by the AQP9 gene. The gene encodes a 295-amino-acid protein with the amino acid sequence identity with AQP3(48%), AQP7(45%), and other aquaporins (approximately 30%), suggesting that AQP3, AQP7, and AQP9 belong to a subfamily of the aquaporin family. AQP9 is the major glycerol channel in mouse erythrocytes and suggest that this transport pathway may contribute to the virulence of intraerythrocytic stages of malarial infection.

Specifications

Family Primary antibody
Formulation 0.5mg/ml if reconstituted with 0.2ml sterile DI water
Format Antigen affinity purified
Host Animal Rabbit
Clonality Polyclonal (rabbit origin)
Isotype Rabbit IgG
Species Reactivity Mouse
Application WB
Application Details Western blot: 0.5-1ug/ml
Application Note The stated application concentrations are suggested starting amounts. Titration of the Aquaporin 9 antibody may be required due to differences in protocols and secondary/substrate sensitivity.
Immunogen An amino acid sequence from the C-terminus of mouse Aquaporin 9 (VLFIQMHHSNPDPEVK) was used as the immunogen for this Aquaporin 9 antibody.
Buffer Lyophilized from 1X PBS with 2.5% BSA and 0.025% sodium azide/thimerosal
Purity Antigen affinity
Storage After reconstitution, the Aquaporin 9 antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.
Limitation This Aquaporin 9 antibody is available for research use only.
Uniprot # Q9JJJ3
Status Available
PDF Link https://www.nsjbio.com/tds-pdf/aquaporin-9-antibody-r31206
Title Aquaporin 9 Antibody
Description Aquaporin-9 is a protein that in humans is encoded by the AQP9 gene. The gene encodes a 295-amino-acid protein with the amino acid sequence identity with AQP3(48%), AQP7(45%), and other aquaporins (approximately 30%), suggesting that AQP3, AQP7, and AQP9 belong to a subfamily of the aquaporin family. AQP9 is the major glycerol channel in mouse erythrocytes and suggest that this transport pathway may contribute to the virulence of intraerythrocytic stages of malarial infection.
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