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Recombinant Escherichia coli Aquaporin Z (aqpZ), partial

Recombinant Escherichia coli Aquaporin Z (aqpZ), partial

Code
MSDS	MSDS Datasheet
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Source
Conjugate
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Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

aqpZ

Uniprot NO.

P60844

Alternative Names

aqpZ; bniP; b0875; JW0859; Aquaporin Z; Bacterial nodulin-like intrinsic protein

Species

Escherichia coli (strain K12)

Source

Yeast

Protein Length

Partial

Tag Info

N-terminal His-tagged/Tag-Free
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.

Storage Condition

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.

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.

Notes

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

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Target Background

Function(From Uniprot)

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.

Gene References into Functions

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
Data show that the open and closed states of AqpZ directly relate to the side chain conformation of residue R189. PMID:21315687
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
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
analysis of of Escherichia coli aquaporin AqpZ and GlpF single-channel water permeabilities PMID:16399837
biochemical analysis of permeability and solute transport characteristics of amphiphilic triblock-polymer vesicles containing the bacterial water-channel protein Aquaporin Z PMID:18077364