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H0786

Heregulin-β, EGF Domain human

≥80% (SDS-PAGE), recombinant, expressed in E. coli, buffered aqueous glycerol solution

Synonym(s):

HRG-β

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100 μG

$821.00

$821.00


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About This Item

MDL number:
UNSPSC Code:
12352202
NACRES:
NA.32

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biological source

human

Quality Level

recombinant

expressed in E. coli

assay

≥80% (SDS-PAGE)

form

buffered aqueous glycerol solution

mol wt

185 kDa

packaging

pkg of 100 μg

storage condition

avoid repeated freeze/thaw cycles

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

Gene Information

human ... NRG1(3084)

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This Item
H7660SRP3018SRP4633
biological source

human

biological source

human

biological source

human

biological source

human

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in E. coli

assay

≥80% (SDS-PAGE)

assay

≥98% (SDS-PAGE)

assay

≥98% (HPLC), ≥98% (SDS-PAGE)

assay

≥90% (SDS-PAGE)

Quality Level

200

Quality Level

200

Quality Level

-

Quality Level

-

form

buffered aqueous glycerol solution

form

lyophilized powder

form

lyophilized

form

lyophilized

mol wt

185 kDa

mol wt

predicted mol wt 8 kDa

mol wt

13.5 kDa

mol wt

15-16 kDa

General description

Truncated human sequence (amino acids 178-241) corresponding to the EGF domain and purified as a GST-fusion protein, cleaved with thrombin.

Biochem/physiol Actions

Growth factor ligand for ErbB3 and ErbB4 receptor tyrosine kinases.
Growth factor ligand for ErbB3 and ErbB4 receptor tyrosine kinases. The binding of HRG results in receptor dimerization and receptor trans-autophosphorylation. The phosphorylated receptors recruit cellular signaling proteins, initiating signaling pathways.

Physical form

Solution in phosphate buffered saline containing 30% glycerol.

Analysis Note

Stimulates tyrosine phosphorylation of the ErbB-3/HER-3 receptor.
The biological activity is measured by its ability to activate the c-ErbB3/HER-3 receptor in treated MCF-7 cells.

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Marcia R Campbell et al.
Cell reports, 38(5), 110291-110291 (2022-02-03)
Effective inactivation of the HER2-HER3 tumor driver has remained elusive because of the challenging attributes of the pseudokinase HER3. We report a structure-function study of constitutive HER2-HER3 signaling to identify opportunities for targeting. The allosteric activation of the HER2 kinase

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