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Key Documents

Safety Information

P0521

Millipore

Peptone from Glycine max (soybean)

Type IV, powder, Component of microbiological growth media

Synonym(s):

Protein from soybean, Soya peptone type IV

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About This Item

EC Number:
293-434-7
UNSPSC Code:
41106212
NACRES:
NA.85

biological source

Glycine max (soybean)

Quality Level

200

sterility

non-sterile

type

Type IV

form

powder

nitrogen analysis

~2.0% amino, ~8.0% total

application(s)

food and beverages
microbiology
vitamins, nutraceuticals, and natural products

storage temp.

10-30°C

Related Categories

General description

Peptone from Glycine max (soybean), Type IV is an enzymatically hydrolysed soy protein. This peptone is used in fermentation broths as a carbohydrate and nitrogen source (peptides and free amino acids), producing consistent results. It acts comparatively well as peptones obtained from animal sources.

Application

Peptone acts as the main source of nitrogen in microbiological culture media to meet nutrient requirements of microorganisms being cultivated.
Peptone from Glycine max as a nutrient, displays comparative or better growth features of cultivated microorganisms than peptone from other sources

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

P0521-VAR:
P0521-100G:
P0521-500G:
P0521-50KG:
P0521-BULK:
P0521-1KG:

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Certificates of Analysis (COA)

Lot/Batch Number
108K0180V
108K0180
029K0155
108K0181V
108K0181

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Meiyappan Lakshmanan et al.
Biotechnology and bioengineering, 116(9), 2117-2129 (2019-05-09)
Chinese hamster ovary (CHO) cells are the most prevalent mammalian cell factories for producing recombinant therapeutic proteins due to their ability to synthesize human-like post-translational modifications and ease of maintenance in suspension cultures. Currently, a wide variety of CHO host

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