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Merck

H6390

Sigma-Aldrich

Hemin−-Agarose

Type I, saline suspension

Synonym(e):

Hemin Agarose, Hemin Binding Gel, Hemin-Agarose Gel

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About This Item

MDL-Nummer:
UNSPSC-Code:
41106500
NACRES:
NA.56

Biologische Quelle

hemin from bovine

Qualitätsniveau

Typ

Type I

Form

saline suspension

Kennzeichnungsgrad

≥4 μmol (per ml)

Methode(n)

affinity chromatography: suitable

Matrix

Cross-linked 4% beaded agarose

Matrixaktivierung

epoxy

Matrixanbindung

carboxyl

Matrix-Spacer

12 atoms

Eignung

suitable for chromatography

Lagertemp.

2-8°C

Anwendung

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.

Physikalische Form

Suspension in 0.5 M NaCl, enthält 0.02% Thiomersal

Lagerklassenschlüssel

12 - Non Combustible Liquids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


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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)
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
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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