Recombinant E. coli Aquaporin Z Protein

Beta LifeScience SKU/CAT #: BLA-7792P

Recombinant E. coli Aquaporin Z Protein

Beta LifeScience SKU/CAT #: BLA-7792P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

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Product Overview

Host Species Escherichia coli
Accession P60844
Description Recombinant E. coli Aquaporin Z Protein was expressed in E.coli. It is a Full length protein
Source E.coli
AA Sequence MFRKLAAECF GTFWLVFGGC GSAVLAAGFP ELGIGFAGVA LAFGLTVLTM AFAVGHISGG HFNPAVTIGL WAGGRFPAKE VVGYVIAQVV GGIVAAALLY LIASGKTGFD AAASGFASNG YGEHSPGGYS MLSALVVELV LSAGFLLVIH GATDKFAPAG FAPIAIGLAL TLIHLISIPV TNTSVNPARS TAVAIFQGGW ALEQLWFFWV VPIVGGIIGG LIYRTLLEKR D
Molecular Weight 28 kDa including tags
Purity >90% SDS-PAGE.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Measured by its binding ability in a functional ELISA. Immobilized the recombinant protein at 5 μg/ml can bind human ytfE, the EC50 of human ytfE protein is 197.90-259.70 μg/ml.
Formulation Liquid Solution
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped at 4°C. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity.
Subcellular Location Cell inner membrane; Multi-pass membrane protein.
Protein Families MIP/aquaporin (TC 1.A.8) family
Database References

Gene Functions References

  1. Induction of an immune response against AqpZ or its homologous regions can also trigger an autoimmune reaction against human Aqp4 and inflammation of the central nervous system. PMID: 23008451
  2. Data show that the open and closed states of AqpZ directly relate to the side chain conformation of residue R189. PMID: 21315687
  3. the 2.5 A resolution structure of AqpZ suggests aquaporin selectivity results both from a steric mechanism due to pore size and from specific amino acid substitutions that regulate the preference for a hydrophobic or hydrophilic substrate PMID: 14691544
  4. the difference in Arg-189 displacements is correlated with a strong electron density between first transmembrane helices of two open channels; the observed Arg-189 conformations are stabilized by asymmetrical subunit interactions in tAqpZ PMID: 16239219
  5. analysis of of Escherichia coli aquaporin AqpZ and GlpF single-channel water permeabilities PMID: 16399837
  6. biochemical analysis of permeability and solute transport characteristics of amphiphilic triblock-polymer vesicles containing the bacterial water-channel protein Aquaporin Z PMID: 18077364

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.

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