Recombinant E.Coli Adenylate Kinase (ADK) Protein (His)

Name: Recombinant E.Coli Adenylate Kinase (ADK) Protein (His)
Brand: Beta LifeScience
SKU: BLC-08258P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant E.Coli Adenylate Kinase (ADK) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P69441
Target Symbol	ADK
Synonyms	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)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MRIILLGAPGAGKGTQAQFIMEKYGIPQISTGDMLRAAVKSGSELGKQAKDIMDAGKLVTDELVIALVKERIAQEDCRNGFLLDGFPRTIPQADAMKEAGINVDYVLEFDVPDELIVDRIVGRRVHAPSGRVYHVKFNPPKVEGKDDVTGEELTTRKDDQEETVRKRLVEYHQMTAPLIGYYSKEAEAGNTKYAKVDGTKPVAEVRADLEKILG
Expression Range	1-214aa
Protein Length	Full Length
Mol. Weight	27.6kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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.
Subcellular Location	Cytoplasm.
Protein Families	Adenylate kinase family
Database References	KEGG: ecj:JW0463 STRING: 316385.ECDH10B_0430

Gene Functions References

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

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.