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Merck

PF048

Heregulin, Human, Recombinant, E. coli

Synonym(s):

Neu Differentiation Marker, NDF

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About This Item

UNSPSC Code:
12352202
Assay:
≥97% (SDS-PAGE)
Form:
lyophilized
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assay

≥97% (SDS-PAGE)

Quality Level

form

lyophilized

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze

shipped in

wet ice

storage temp.

−20°C

General description

Recombinant, human heregulin expressed in E. coli. Human recombinant heregulin whose DNA sequence encoding the EGF domain of heregulin α (amino acids 177-241) expressed in and purified from E. coli. The expressed protein consists of 65 amino acids with a predicted molecular weight of approximately 7 kDa.

Application

Proliferation Studies

Biochem/physiol Actions

EC₅₀ ~20-40 ng/ml as determined by a cell proliferation assay using breast carcinoma cell line SK-BR-3 or in a serum-free cell proliferation assay using the human cell line MCF7.

Physical form

Lyophilized from PBS, 50 µg BSA/µg cytokine.

Preparation Note

Store lyophilized protein dessicated at -20°C. Lyophilized product should be reconstituted in sterile PBS containing at least 0.1% human serum albumin or bovine serum albumin to prepare a stock solution of no less than 50 µg/ml. Following initial thaw, aliquot and freeze (-20°C).

Other Notes

It is recommended that the protein be titrated for optimal results in individual systems.
Riese, D.J., et al. 1996. J. Biol. Chem.271, 20047.
Holmes, W.E., et al. 1992. Science256, 1205.
Karey, K.P., et al. 1988. Cancer Res.48, 4083.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

Toxicity: Standard Handling (A)


Storage Class

11 - Combustible Solids

wgk

WGK 3


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.

US1PF048-EACH: + PF048-50UG: + PF048-UG:

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Rachel R Besser et al.
Biomaterials science, 8(2), 591-606 (2019-12-21)
We report a water-soluble and non-toxic method to incorporate additional extracellular matrix proteins into gelatin hydrogels, while obviating the use of chemical crosslinkers such as glutaraldehyde. Gelatin hydrogels were fabricated using a range of gelatin concentrations (4%-10%) that corresponded to