Na+/H+ Exchanger-1 Antibody [K9D3]

Application: Reactivity: Mouse, Human, Amphibian, Fish, Avian, Vertebrates

Lane 1: U87MG, Lane 2: THP-1, Lane 3: 22RV1, Lane 4: Mouse brain

Usage Information

Dilution
WB1:500

Application
WB

Reactivity
Mouse, Human, Amphibian, Fish, Avian, Vertebrates

Source
Mouse Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
~100-110 kDa

Datasheet & SDS

Biological Description

Specificity
Na+/H+ Exchanger-1 Antibody [K9D3] detects endogenous levels of total Na+/H+ Exchanger-1 protein.

Clone
K9D3

Synonym(s)
Sodium/hydrogen exchanger 1; APNH; Na(+)/H(+) antiporter, amiloride-sensitive; Na(+)/H(+) exchanger 1 (NHE-1); Solute carrier family 9 member 1; SLC9A1; APNH1; NHE1

Background
Na+/H+ Exchanger-1 (NHE1, SLC9A1) is a ubiquitously expressed integral membrane antiporter that plays a central role in regulating intracellular pH (pHi) homeostasis. NHE1 is composed of 12 transmembrane helices (TMHs) with both N- and C-termini facing the cytosol. Key transport segments include TM IV, VII, and IX, along with reentrant loops IL2 and IL4, and glycosylation sites on extracellular loop 5 (EL5) that confer structural stability. The extended ~315-residue C-terminal cytoplasmic domain contains numerous serine/threonine phosphorylation sites and ezrin-binding motifs (residues 553–564), anchoring NHE1 to the actin cytoskeleton. NHE1 is allosterically activated by intracellular acidification, which promotes proton binding to a non-transport modifier site (Hill coefficient ~3), triggering conformational changes from inward- to outward-facing states through helix tilting and water-filled access pathways, similar to the bacterial NhaA transporter. It mediates electrogenic exchange of extracellular Na+ (Km 5–50 mM) for intracellular H+ in a 1:1 stoichiometry, utilizing the transmembrane Na+ gradient as its driving force without direct energy input. This allows rapid recovery of pHi following acidosis, regulation of cell volume via Na+ influx, and scaffolding of lamellipodia protrusion through ERM-actin interactions. Hormonal and growth factor signaling can phosphorylate C-terminal serines (e.g., S703, Thr653) via NHERF1, ERK, and PKA pathways, shifting the pHi set-point toward alkalinity. Pathologically, in ischemia-reperfusion injury, acid-activated NHE1 promotes cytotoxic Na+/Ca2+ overload via reverse-mode NCX activity, exacerbating myocardial infarction. Chronic NHE1 upregulation is also implicated in tumor invasion through pericellular alkalinization and matrix remodeling, as well as in cardiac hypertrophy.

Background

Na+/H+ Exchanger-1 (NHE1, SLC9A1) is a ubiquitously expressed integral membrane antiporter that plays a central role in regulating intracellular pH (pHi) homeostasis. NHE1 is composed of 12 transmembrane helices (TMHs) with both N- and C-termini facing the cytosol. Key transport segments include TM IV, VII, and IX, along with reentrant loops IL2 and IL4, and glycosylation sites on extracellular loop 5 (EL5) that confer structural stability. The extended ~315-residue C-terminal cytoplasmic domain contains numerous serine/threonine phosphorylation sites and ezrin-binding motifs (residues 553–564), anchoring NHE1 to the actin cytoskeleton. NHE1 is allosterically activated by intracellular acidification, which promotes proton binding to a non-transport modifier site (Hill coefficient ~3), triggering conformational changes from inward- to outward-facing states through helix tilting and water-filled access pathways, similar to the bacterial NhaA transporter. It mediates electrogenic exchange of extracellular Na+ (Km 5–50 mM) for intracellular H+ in a 1:1 stoichiometry, utilizing the transmembrane Na+ gradient as its driving force without direct energy input. This allows rapid recovery of pHi following acidosis, regulation of cell volume via Na+ influx, and scaffolding of lamellipodia protrusion through ERM-actin interactions. Hormonal and growth factor signaling can phosphorylate C-terminal serines (e.g., S703, Thr653) via NHERF1, ERK, and PKA pathways, shifting the pHi set-point toward alkalinity. Pathologically, in ischemia-reperfusion injury, acid-activated NHE1 promotes cytotoxic Na+/Ca2+ overload via reverse-mode NCX activity, exacerbating myocardial infarction. Chronic NHE1 upregulation is also implicated in tumor invasion through pericellular alkalinization and matrix remodeling, as well as in cardiac hypertrophy.

References
https://pubmed.ncbi.nlm.nih.gov/34108458/ https://pubmed.ncbi.nlm.nih.gov/33273619/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%