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Key Documents

H5529

Sigma-Aldrich

Heregulin-α, EGF Domain human

recombinant, expressed in E. coli, lyophilized powder, suitable for cell culture, ≥97% (SDS-PAGE)

Synonyme(s) :

HRG-α

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About This Item

Numéro MDL:
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.32

Source biologique

human

Niveau de qualité

Produit recombinant

expressed in E. coli

Pureté

≥97% (SDS-PAGE)

Forme

lyophilized powder

Puissance

10-50 ng/mL

Poids mol.

protein 8 kDa (reducing conditions)
protein ~7 kDa (predicted)

Conditionnement

pkg of 50 μg

Technique(s)

cell culture | mammalian: suitable

Impuretés

endotoxin, tested

Numéro d'accès UniProt

Température de stockage

−20°C

Informations sur le gène

human ... NRG1(3084)

Actions biochimiques/physiologiques

Heregulin (HRG) is the human homologue to the neu differentiation factor (NDF) in rat. The heregulin family members contain one EGF-like motif and an IgD-like motif in the extracellular domain. They bind to ErbB-2, ErbB-3, and ErbB-4 (receptors closely related to EGFR). HRG-α and HRG-β isoforms differ slightly in the EGF domain due to alternate splicing. HRG-β isoforms are further subdivided into β1, β2, and β3 isoforms, which show identical binding and activation characteristics. Both α and β HRG isoforms bind to ErbB-3 and ErbB-4 homodimers, but not directly to ErbB-2. HRG-α binding to ErbB-3 and ErbB-4 is reported to be approximately 100-fold weaker than that of HRG-β. When ErbB-2 is combined into a heterodimer with ErbB-3 or ErbB-4, the binding affinities of both α and β isoforms are substantially improved. HRGs are mitogenic for Schwann cells in culture and weakly to moderately mitogenic for a variety of epithelial cells, including mammary, ovarian, lung, and gastric cells. HRGs inhibit proliferation and induce differentation in some tumor cell lines, such as certain mammary tumor cells, which are arrested at the G2M phase. HRGs also induce expression of acetylcholine receptors and possibly other molecules in muscle cells at newly formed neuromuscular synapses, suggesting they may play a role in neuromuscular synapse maturation and maintenance.

Forme physique

Lyophilized from a 0.2 μm filtered solution in phosphate buffered saline, pH 7.4, containing 50 μg bovine serum albumin per 1 μg as a carrier protein.

Remarque sur l'analyse

The bioactivity is tested in culture using a proliferation assay with the human cell line MCF-7.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

S Y Baek et al.
Developmental neuroscience, 20(6), 512-517 (1998-12-22)
Neu differentiation factor (NDF), a 44-kD polypeptide, is a member of the neuregulin family which also includes glial growth factor, heregulin and acetylcholine-receptor-inducing activity. Previous studies have demonstrated that NDF/glial growth factor/heregulin/acetylcholine-receptor-including activity are products of neurons and mediate proliferation
Z Aguilar et al.
Oncogene, 18(44), 6050-6062 (1999-11-11)
The heregulins are a family of ligands with ability to induce phosphorylation of the p185HER-2/neu receptor. Various investigators have reported a variety of responses of mouse and human breast and ovarian cells to this family of ligands including growth stimulation
J T Jones et al.
FEBS letters, 447(2-3), 227-231 (1999-04-24)
ErbB receptor activation is a complex process and is dependent upon the type and number of receptors expressed on a given cell. Previous studies with defined combinations of ErbB receptors expressed in mammalian cells have helped elucidate specific biological responses
Take your partners, please--signal diversification by the erbB family of receptor tyrosine kinases.
R J Daly
Growth factors (Chur, Switzerland), 16(4), 255-263 (1999-07-31)
Neu differentiation factor (NDF) and the neuregulin (NRG) family.
Yarden, Y., Wen, D. et al.
The Cytokine Handbook, 146-146 (1998)

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