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H6390

Sigma-Aldrich

Hemin−Agarose

Type I, saline suspension

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About This Item

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

biological source

hemin from bovine

Quality Level

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


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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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