H6758
L-Histidyldiazobenzylphosphonic acid-Agarose
saline suspension
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About This Item
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form
saline suspension
extent of labeling
≥6 μmol per mL
matrix
Cross-linked 4% beaded agarose
matrix activation
cyanogen bromide
matrix attachment
α-amino
matrix spacer
1 atom
storage temp.
2-8°C
Application
L-Histidyldiazobenzylphosphonic acid-agarose is an agarose conugate in saline suspension used in affinity chromatography, protein chromatography and amino acid resins. L-Histidyldiazobenzylphosphonic acid agarose has been used to study psychrophilic organisms that have successfully adapted to various low-temperature environments such as cold ocean waters.
Physical form
Suspension in 1.0 M NaCl containing preservative
Disclaimer
For U.S. Customers: Contains mercury; Do not place in trash - dispose according to local, state, or federal laws.
Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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G Dong et al.
Enzyme and microbial technology, 21(5), 335-340 (1997-10-10)
A hyperthermophilic alkaline phosphatase was purified from Thermotoga neapolitana by heat treatment at 100 degrees C in the presence of Co2+ followed by ion-exchange and affinity chromatographies. The enzyme was purified 2,880-fold with 44% yield. The purified enzyme showed a
M Landt et al.
Biochemistry, 17(5), 915-919 (1978-03-07)
Five phosphonic acid derivatives were synthesized, coupled to agarose, and tested for affinity chromatographic binding of alkaline phosphatase from bovine intestine. Agarose coupled to L-histidyldiazobenzylphosphonic acid was found to be a highly effective adsorbent. In order to understand the large
Hauksson et al.
Enzyme and microbial technology, 27(1-2), 66-73 (2000-06-23)
Psychrophilic organisms have successfully adapted to various low-temperature environments such as cold ocean waters. Catalysts with increased catalytic efficiencies are produced, generally at the expense of thermal stability due to fewer non-covalent stabilizing interactions. A marine bacterial strain producing a
An alkaline phosphatase from <I>Thermus</I> sp strain Rt41A.
Hartog, A.T., and Daniel, R.M.
The International Journal of Biochemistry, 24(10), 1657-1660 (1992)
Ying Qi et al.
Journal of cellular biochemistry, 86(1), 79-89 (2002-07-12)
PTP-MEG2 is an intracellular protein tyrosine phosphatase with a putative lipid-binding domain at the N-terminus. The present study reports expression, purification, and characterization of the full-length form of the enzyme plus a truncated form containing the catalytic domain alone. Full-length
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