Product Details

Purity

Greater than 90% as determined by SDS-PAGE.

Target Names

adk

Uniprot No.

P69441

Research Area

Others

Alternative Names

adk; dnaW; plsA; b0474; JW0463; Adenylate kinase; AK; EC 2.7.4.3; ATP-AMP transphosphorylase; ATP:AMP phosphotransferase; Adenylate monophosphate kinase

Species

Escherichia coli (strain K12)

Source

E.coli

Expression Region

1-214aa

Target Protein Sequence

MRIILLGAPGAGKGTQAQFIMEKYGIPQISTGDMLRAAVKSGSELGKQAKDIMDAGKLVTDELVIALVKERIAQEDCRNGFLLDGFPRTIPQADAMKEAGINVDYVLEFDVPDELIVDRIVGRRVHAPSGRVYHVKFNPPKVEGKDDVTGEELTTRKDDQEETVRKRLVEYHQMTAPLIGYYSKEAEAGNTKYAKVDGTKPVAEVRADLEKILG
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.

Mol. Weight

27.6kDa

Protein Length

Full Length

Tag Info

N-terminal 6xHis-tagged

Form

Liquid or 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

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is 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°C/-80°C. 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.

Notes

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

Datasheet & COA

Please contact us to get it.

Target Background

Function

Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.

Gene References into Functions

These results are consistent with an induced-fit model in which the transition of AdK from an open state to a closed state is initiated by ATP binding. PMID: 28767234
Fast closure of N-terminal long loops but slow formation of beta strands precedes the folding transition state of Escherichia coli adenylate kinase. PMID: 24787383
As both open and closed states sampled a wide range of conformation transitions, our simulation strongly supported the conformational selection mechanism for Escherichia coli ADK. PMID: 23936827
fast subdomain folding prior to global refolding transition of adenylate kinase; applied double kinetics method to test the hypothesis that specific short native-like intramolecular distances between residues separated by long chain segments in a globular protein can be formed in the collapsed state, prior to the cooperative folding transition PMID: 22898349
In Cartesian space, LID domain closure precedes NMP domain closure in the bound simulation, consistent with prior coarse-grained models of the adenylate kinase conformational transition. PMID: 20471396
Results demonstrate that the conformational ensemble of adenylate kinase is significantly populated by a locally unfolded state and that the excited-state can be manipulated through mutation, independent of perturbations of the ground-state structures. PMID: 19805185
The dynamics of adenylate kinase of Escherichia coli, and its complex with the inhibitor AP(5)A, are characterized PMID: 15382240
Simulation supports the hypothesis that hydrogen bonds between AMP's adenine and the protein are at the origin of the high nucleoside monophosphate (NMP) specificity of adenylate kinase PMID: 15521058
AK molecules undergo fast collapse to an ensemble of compact structures where the local environment of surface probes seems to be native-like but the two labeled secondary structure elements remain unfolded. PMID: 16098987
Data describe the plastic network model, used to generate a conformational change pathway for Escherichia coli adenylate kinase based on two crystal structures, namely that of an open and a closed conformer. PMID: 16139299
Adenylate kinase from E coli have two highly flexible domains which close over bound substrates. PMID: 16302237
for adenylate kinase, the change in the number of interdomain contacting atoms upon closure showed a considerable increase, suggesting that adk undergoes closure through a hinge mechanism PMID: 17299745
Results describe the atomistic mechanism of conformational transition in adenylate kinase. PMID: 18682219
Results show that the flexible subdomains of adk fold into their native structure in a noncooperative manner with respect to the CORE subdomain. PMID: 19219996

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Subcellular Location

Cytoplasm.

Protein Families

Adenylate kinase family

Database Links

KEGG: ecj:JW0463

STRING: 316385.ECDH10B_0430

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Code	CSB-RP163274Ba
MSDS	MSDS
Size	US$388
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Image	(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Recombinant Escherichia coli Adenylate kinase (adk)

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