H6390
Hemin−Agarose
Type I, saline suspension
Synonym(s):
Hemin Agarose, Hemin Binding Gel, Hemin-Agarose Gel
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About This Item
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biological source
hemin from bovine
type
Type I
form
saline suspension
extent of labeling
≥4 μmol (per ml)
technique(s)
affinity chromatography: suitable
matrix
Cross-linked 4% beaded agarose
matrix activation
epoxy
matrix attachment
carboxyl
matrix spacer
12 atoms
suitability
suitable for chromatography
storage temp.
2-8°C
Application
Hemin Type I-agarose is an agarose conjugate in saline suspension used in affinity chromatography, protein chromatography and specialty resins. Hemin-agarose has been used to evaluate protection against invasion by Gram-negative bacteria.
Physical form
Suspension in 0.5 M NaCl containing preservative
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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S Yamamoto et al.
FEMS microbiology letters, 128(2), 195-200 (1995-05-01)
Several clinical isolates of Vibrio parahaemolyticus were examined for their ability to utilize either hemin or hemoglobin as a sole source of iron. Both compounds appeared to be equally good iron sources. Maximum growth was obtained at 5 microM hemin
Inducible glutathione S-transferase (IrGST1) from the tick Ixodes ricinus is a haem-binding protein
Perner J, et al.
Insect Biochemistry and Molecular Biology, 95, 44-54 (2018)
Hye-Jung Lee et al.
Journal of experimental botany, 63(16), 5967-5978 (2012-09-20)
The Arabidopsis thaliana L. SOUL/haem-binding proteins, AtHBPs belong to a family of five members. The Arabidopsis cytosolic AtHBP1 (At1g17100) and AtHBP2 (At2g37970) have been shown to bind porphyrins and metalloporphyrins including haem. In contrast to the cytosolic localization of these
C S Bracken et al.
Journal of bacteriology, 181(19), 6063-6072 (1999-09-28)
The abilities of two bacterial active heme transporters, HmbR of Neisseria meningitidis and HemR of Yersinia enterocolitica, to use different heme sources were compared. While HmbR-expressing cells used only hemoglobin (Hb) and heme, HemR-expressing bacteria were able to grow on
Swapna Asuthkar et al.
Infection and immunity, 75(9), 4582-4591 (2007-06-20)
In an earlier study, based on the ferric enterobactin receptor FepA of Escherichia coli, we identified and modeled a TonB-dependent outer membrane receptor protein (LB191) from the genome of Leptospira interrogans serovar Lai. Based on in silico analysis, we hypothesized
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