Skip to Content
Merck
All Photos(2)

Key Documents

L9010

Sigma-Aldrich

Lactalbumin enzymatic hydrolysate

powder, BioReagent, suitable for cell culture

Sign Into View Organizational & Contract Pricing


About This Item

CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.75

biological source

Porcine
bovine milk

Quality Level

product line

BioReagent

form

powder

nitrogen analysis

≥11.0% total

technique(s)

cell culture | mammalian: suitable

storage temp.

2-8°C

Looking for similar products? Visit Product Comparison Guide

Application

Lactalbumin enzymatic hydrolysate has been used: in the preparation of modified Caenorhabditis elegans habitation and reproduction medium (mCeHR), as a component in Dulbecco′s modified Eagle medium (DMEM) for matrix metalloproteinase-13 (MMP-13) preparation, as a supplement in 6M medium to cultivate baby hamster kidney fibroblasts (BHK 21/13) cells for a comparative study

Biochem/physiol Actions

Lactalbumin enzymatic hydrolysate can be used as an amino acid or peptide-rich supplement in several mammalian and microbial cell culture applications.

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

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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Tamika K Samuel et al.
Journal of visualized experiments : JoVE, (90), e51796-e51796 (2014-08-26)
In this protocol, we present the required materials, and the procedure for making modified C. elegans Habituation and Reproduction media (mCeHR). Additionally, the steps for exposing and acclimatizing C. elegans grown on E. coli to axenic liquid media are described.
Inna Solomonov et al.
Proceedings of the National Academy of Sciences of the United States of America, 113(39), 10884-10889 (2016-09-16)
It is well established that the expression profiles of multiple and possibly redundant matrix-remodeling proteases (e.g., collagenases) differ strongly in health, disease, and development. Although enzymatic redundancy might be inferred from their close similarity in structure, their in vivo activity

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service