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AmeriDx® H. pylori Antigen - Recombinant UreA Protein (21231247), 1 mg

Cytotoxin associated gene A (CagA), recombinant CagA protein, cagA2d domain

$299.00
21231247
In stock

Minimum quantity for "AmeriDx® H. pylori Antigen - Recombinant UreA Protein (21231247), 1 mg" is 1.

Catalog Number: 21231247

Size: 100 ug

Source: E. coli derived H. pylori Urease subunit A (UreA) protein

             NCBI ID: AAK69738

Sequences:

MKLTPKELDKLMLHYAGELARKRKEKGIKLNYVEAVALISAHIMEEARAGKKSAAELMQEGRSLLKPDDV
MDGVASMIHEVGIEAMFPDGTKLVTVHTPIEANGKLVPGELFLKNEDITINEGKKAVSVKVKNVGDRPVQ
IGSHFHFFEVNRYLDFDREKTFGKRLDIASGTAVRFEPGEEKSVELIDIGGNRRIFGFNALVDRQADNES
KKIALHRAKERGFHGAKSDDNYVKTIKE

Host: E. coli

Format: Dry Powder

Reactivity: Immune assay with AmeriDx® H. pylori UreA antibodies.

QC Testing: Concentration Measurement, SDS-PAGE Analysis.

Formulation and Purity

Recombinant protein accession no AAK69738, over-expressed in E coli strain BL21, and affinity purification from cell pellet by Ni-NTA resin, and dialysis against 1x PBS. The protein is > 97% pure, as determined by SDS-PAGE. The concentration is measured by Nanodrop.

Storage Buffer: In PBS before lyophilized

Preparation and Storage

Upon received, save at freezer immediately if not used. After initial reconstitution with DI water (50-100uL), aliquot if necessary, and save the product at -80°C for future use.

Description

This enzyme may allow it to remain active at the cell surface at acidic gastric pH. Within this dodecameric structure the 12 active sites are clustered within the interior of the proteinaceous shell. This may allow a high local concentration of ammonia within the enzyme which may protect the nickel-chelating groups from protonation (https://www.uniprot.org/uniprot/P14916).

Product Notices

  • Since applications vary, each investigator should titrate the reagent to obtain optimal results.
  • Please refer to www.ameridx.com/ for technical protocols.

References

1.  Olivera-Severo, D., et al. (2017). "A New Role for Helicobacter pylori Urease: Contributions to Angiogenesis." Front Microbiol 8(1883).


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