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Key Documents

H6390

Sigma-Aldrich

Hemin−Agarose

Type I, saline suspension

Synonyma:

Hemin Agarose, Hemin Binding Gel, Hemin-Agarose Gel

Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen
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About This Item

MDL number:
MFCD00163149
UNSPSC Code:
41106500
NACRES:
NA.56

biological source

hemin from bovine

Quality Level

200

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

12 - Non Combustible Liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

Osvědčení o analýze (COA)

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Human Serum from human male AB plasma, USA origin, sterile-filtered

Sigma-Aldrich

H4522

Human Serum

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
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
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
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