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Gibco™ Aeromonas Aminopeptidase Recombinant Protein, PeproTech®

Product Code. 17850143
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Quantity:
100 μg
2 x 500 μg
500 μg
Unit Size:
100µg
1mg
500µg
Pack of 2
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Product Code. Quantity unitSize
17850143 100 μg 100µg
17880783 2 x 500 μg 1mg
30088079 2 x 500 μg Pack of 2
17810793 500 μg 500µg
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Product Code. 17850143 Supplier Gibco™ Supplier No. 10010100UG

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Recombinant Protein

100-10-1MG will be provided as 2 x 500 μg (100-10-500UG) Recombinant Aeromonas Aminopeptidase is a 31.4 kDa protein containing 291 amino acid residues. This product is shipped at ambient temperature. For storage, handling and reconstitution information, please see the lot-specific Certificate of Analysis

The enzyme (29 KD) aeromonas aminopeptidase is used in the processing of pharmaceutical proteins produced by genetic engineering as well as for physical and structural investigations and for sequence and amino-terminal determinations. This exopeptidase recognizes a specific stop sign at -X- Pro and requires a free a-amino group in the L-configuration. It is therefore suitable for the removal of the redundant N-terminal methionine often added to engineered proteins.
TRUSTED_SUSTAINABILITY

Spezifikation

For Use With (Application) Functional Assay
Formulation protein with no preservative
Molecular Weight (g/mol) 31.4 kDa
Name Aeromonas Aminopeptidase
Quantity 100 μg
Source E. coli
Regulatory Status RUO
Endotoxin Concentration <1 EU/ μg
Common Name Aeromonas Aminopeptidase
Biological Activity Sequentially cleaves N-terminal amino acids except E, D, and X-P.
Conjugate Unconjugated
Recombinant Recombinant
Sequence MPPITQQATV TAWLPQVDAS QITGTISSLE SFTNRFYTTT SGAQASDWIA SEWQALSASL PNASVKQVSH SGYNQKSVVM TITGSEAPDE WIVIGGHLDS TIGSHTNEQS VAPGADDDASGIAAVTEVIR VLSENNFQPK RSIAFMAYAA EEVGLRGSQD LANQYKSEGK NVVSALQLDM TNYKGSAQDV VFITDYTDSN FTQYLTQLMD EYLPSLTYGF DTCGYACSDH ASWHNAGYPAAMPFESKFND YNPRIHTTQD TLANSDPTGS HAKKFTQLGL AYAIEMGSAT G
Content And Storage -20°C
Expression System E. coli
Form Lyophilized
Purity or Quality Grade ≥ 98% by SDS-PAGE gel and HPLC analyses.
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