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H2899

Supelco

HPLC protein standard mixture

analytical standard

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NACRES:
NA.24

grade

analytical standard

Quality Level

form

solid

analyte chemical class(es)

amino acids, peptides, proteins

technique(s)

HPLC: suitable

application(s)

food and beverages

format

multi-component solution

storage temp.

−20°C

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This Item
H2016P8119P5369
Supelco

H2899

HPLC protein standard mixture

Supelco

H2016

HPLC peptide standard mixture

Protein Standard analytical standard, 80 mg/mL (HSA and gamma-globulins)

P8119

Protein Standard

Supelco

P5369

Protein Standard

format

multi-component solution

format

multi-component solution

format

multi-component solution

format

single component solution

technique(s)

HPLC: suitable

technique(s)

HPLC: suitable

technique(s)

gel permeation chromatography (GPC): suitable

technique(s)

gel permeation chromatography (GPC): suitable

grade

analytical standard

grade

analytical standard

grade

analytical standard

grade

analytical standard

analyte chemical class(es)

amino acids, peptides, proteins

analyte chemical class(es)

amino acids, peptides, proteins

analyte chemical class(es)

amino acids, peptides, proteins

analyte chemical class(es)

amino acids, peptides, proteins

application(s)

food and beverages

application(s)

food and beverages

application(s)

food and beverages

application(s)

food and beverages

Application

HPLC protein standard mixture has been used as a standard for the separation of proteins in cell extract samples of bacteria using high performance liquid chromatography (HPLC).

Packaging

Vial contains approximately 1 mg each of ribonuclease A, cytochrome c, holo-transferrin and apomyoglobin.

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

ppe

Eyeshields, Gloves, type N95 (US)


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Customers Also Viewed

Honglei Liu et al.
Applied and environmental microbiology, 80(5), 1799-1806 (2014-01-07)
Sulfur oxidation by chemolithotrophic bacteria is well known; however, sulfur oxidation by heterotrophic bacteria is often ignored. Sulfur dioxygenases (SDOs) (EC 1.13.11.18) were originally found in the cell extracts of some chemolithotrophic bacteria as glutathione (GSH)-dependent sulfur dioxygenases. GSH spontaneously
Distribution, diversity, and activities of sulfur dioxygenases in heterotrophic bacteria
Liu H, et al.
Applied and Environmental Microbiology, 80, 1799-1806 (2014)

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