|Reactivity||Human, Mouse, Rat|
|Calculated MW||91403 Da|
|Homology||Mouse - identical; human - 12/16 amino acid residues identical.|
|Other Names||Sodium/hydrogen exchanger 2, H7, Na(+)/H(+) exchanger 2, NHE-2, Solute carrier family 9 member 2, Slc9a2, Nhe2|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide (C)RASEPGNRKGRLGNEK, corresponding to amino acid residues 797-812 of rat NHE-2 (Accession P48763). Intracellular, C-terminus.|
|Peptide Confirmation||Confirmed by mass-spectrography and amino acid analysis.|
|Format||Affinity purified antibody, lyophilized powder|
|Reconstitution||50 µl or 0.2 ml deionized water, depending on the sample size.|
|Antibody Concentration After Reconstitution||0.8 mg/ml.|
|Buffer After Reconstitution||Phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.05% NaN3.|
|Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Storage After Reconstitution||The reconstituted solution can be stored at 4ºC for up to 2 weeks. For longer periods, small aliquots should be stored at -20ºC or below. Avoid multiple freezing and thawing. The further dilutions should be made using a carrier protein such as BSA (1%). Centrifuge all antibody preparations before use (10000 × g 5 min).|
|Control Antigen Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Control Antigen Reconstitution||100 µl DDW.|
|Control Antigen Storage After Reconstitution||-20ºC.|
|Preadsorption Control||1 µg peptide per 1 µg antibody.|
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Provided below are standard protocols that you may find useful for product applications.
In order to function in optimal conditions, cells must maintain a close to neutral intracellular pH. They have adopted various mechanisms in order to do so, one of which is via Na+/H+ exchangers (NHEs). Genes belonging to this group are expressed along a very broad range of organisms and are essential for protecting cells against intracellular acidification1. To date, nine genes have been identified in mammals; NHE1-9. These membrane proteins have 10-12 transmembrane domains depending on whether a splice variant is expressed and an intracellular N-terminal. The C-terminal domain can be either intracellular or extracellular, also depending whether a splice variant of the protein is involved. The C-terminal part of the protein also undergoes posttranslational modification such as phosphorylation2. Both NHE-1 and NHE-2 have an extracellular loop which is glycosylated1,3,4. Under physiological conditions, the Na+/H+ exchanger mediates the exchange of one extracellular Na+ ion for one intracellular proton, thereby keeping the overall charge neutral1. The extracellular binding site of Na+ is not selective as it can also bind Li+ and H+ 1,5,6. K+ ions inhibit NHE-1 but have no effect on NHE-27. The activation of NHE-1 and NHE-2 is sensitive to intracellular acidic pH. Under physiological conditions, both exchangers are not active and upon a drop of intracellular pH, they are rapidly activated1,5,8. NHE-2 is detected in the intestine, kidney and parietal cells2,9-11. It is also detected in skeletal muscle and testis2,12. Abgent is pleased to offer a highly specific antibody directed against an epitope of rat NHE-2. Anti-Na+/H+ Exchanger 2 (NHE-2) antibody (#AG1161) can be used in western blot analysis and immunohistochemistry applications, and has been designed to recognize NHE-2 from human, rat and mouse samples.
References 1. Counillon, L. and Pouyssegur, J. (2000) J. Biol. Chem. 275, 1. 2. Kemp, G. et al. (2008) Channels 2, 329. 3. Counillon, L. et al. (1994) Biochemistry 33, 10463. 4. Tse, C. et al. (1994) Biochemistry 33, 12954. 5. Paris, S. and Poouyssegur, J. (1983) J. Biol. Chem. 258, 3503. 6. Aronson, P.S. et al. (1983) J. Biol. Chem. 258, 6767. 7. Yu, F.H. et al. (1993) J. Biol. Chem. 268, 25536. 8. Aronson, P.S. et al. (1982) Nature 299, 161. 9. Bookstein, C. et al. (1997) Am. J. Physiol. 273, 1496. 10. Chambrey, R. et al. (1998) Am. J. Physiol. 275, 379. 11. Schultheis, P.J. et al. (1998) Nat. Genet. 19, 282. 12. Malakooti, J. et al. (1999) Am. J. Physiol. 277, 383.
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