Product Details

Purity

>85% (SDS-PAGE)

Target Names

nhaA

Uniprot No.

P13738

Alternative Names

nhaA; ant; b0019; JW0018; Na(+)/H(+) antiporter NhaA; Sodium/proton antiporter NhaA

Species

Escherichia coli (strain K12)

Protein Length

Partial

Tag Info

Tag type will be determined during the manufacturing process.

The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Form

Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer before Lyophilization

Tris/PBS-based buffer, 6% Trehalose, pH 8.0

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet

Please contact us to get it.

Target Background

Function

Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons. Catalyzes the exchange of 2 H(+) per Na(+). Can mediate sodium uptake when a transmembrane pH gradient is applied. Active at alkaline pH. Activity is strongly down-regulated below pH 6.5.

Gene References into Functions

analysis of NhaA pH-dependent activation by molecular dynamics simulation of atomic details of proton-coupled transport across membrane PMID: 27708266
Lysine 300 has an essential role in stability but not electrogenic transport of Escherichia coli NhaA PMID: 28330875
Data show that the Li(+) binding, H(+) release and antiporter activity were all affected to the same extent by Na(+), Li(+)/H(+) antiporter (NhaA) mutations in the Li(+) binding site (D163E, D163N, D164N, D164E). PMID: 27021484
Data show that the two aspartic acid residues of Na+/H+ antiporter NhaA, D163 and D164, act as Na+ trap and energetic barrier for the transport of Na+. PMID: 26392528
NhaA antiporter functions using 10 helices, and an additional 2 contribute to assembly/stability. PMID: 26417087
As it has been previously suggested that Asp163 is one of the two residues through which proton transport occurs, these results have clear implications to the current mechanistic models of sodium-proton antiport in NhaA. PMID: 25422503
Data indicate that binding of Li+ to purified Na(+)/H(+) antiporter NhaA is enthalpy-driven, highly specific, and pH-dependent and involves a single binding site. PMID: 22915592
Data show that a Trp at position 136 specifically monitors a pH-induced conformational change that activates NhaA, whereas a Trp at position 339 senses a ligand-induced conformational change that does not occur until NhaA is activated at alkaline pH. PMID: 21873214
functional and structural interactions between transmembrane domains; an active conformation of NhaA PMID: 15039449
The molecular interactions established on Na(+) binding may represent an early step in NhaA activation. PMID: 15962009
crystal structure of pH-downregulated NhaA, the main antiporter of Escherichia coli PMID: 15988517
In the passive downhill uptake mode pH regulation of the carrier affects both apparent Km as well as turnover (Vmax). PMID: 16139785
folding rates of structural segments ranged from 0.31 s(-1) to 47 s(-1), providing detailed insight into a distinct folding hierarchy of an unfolded polypeptide into the native membrane protein structure PMID: 16298390
The protonation states of residues in the sodium proton exchanger NhaA from Escherichia coli were investigated. PMID: 16477015
under extreme stress conditions (0.1 m LiCl or 0.7 m NaCl at pH 8.5), the dimeric native NhaA was much more efficient than the monomeric mutant in conferring extreme stress resistance. PMID: 17635927
combinatorial approach based on molecular dynamics simulations led to formulation of a model of NhaA transport mechanism, pH regulation & cation selectivity consistent with experimental data PMID: 17690293
Model structure of the Na+/H+ exchanger 1 in human and E. coli PMID: 17981808
Na+/H+ antiporter genes may contribute to sodium-lithium countertransport activity and salt homeostasis in humans PMID: 18000046
A novel structural fold creates a delicately balanced electrostatic environment in the middle of the membrane, which might be essential for ion binding and translocation. Review. PMID: 18707888
NhaA dimers are crucial for the stability of the antiporter under extreme stress conditions. PMID: 19129192
N-terminus verified by Edman degradation on complete protein PMID: 8381959

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Subcellular Location

Cell inner membrane; Multi-pass membrane protein.

Protein Families

NhaA Na(+)/H(+) (TC 2.A.33) antiporter family

Database Links

KEGG: ecj:JW0018

STRING: 316385.ECDH10B_0020

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Recombinant Escherichia coli Na (+)/H (+) antiporter nhaA, partial

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