Recombinant Human NRG2 protein (ab152998)
Key features and details
- Expression system: Wheat germ
- Tags: GST tag N-Terminus
- Suitable for: WB, ELISA
Description
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Product name
Recombinant Human NRG2 protein
See all NRG2 proteins and peptides -
Expression system
Wheat germ -
Protein length
Protein fragment -
Animal free
No -
Nature
Recombinant -
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Species
Human -
Sequence
SLKSVQDQAYKAPVVVEGKVQGLVPAGGSSSNSTREPPASGRVALVKVLD KWPLRSGGLQREQVISVGSCVPLERNQRYIFFLEPTEQPLVFKTAFAPLD -
Amino acids
116 to 215 -
Tags
GST tag N-Terminus
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Specifications
Our Abpromise guarantee covers the use of ab152998 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
Western blot
ELISA
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Form
Liquid -
Additional notes
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Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
pH: 8.00
Constituents: 0.31% Glutathione, 0.79% Tris HCl
General Info
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Alternative names
- Divergent of neuregulin 1
- Divergent of neuregulin-1
- Don 1
see all -
Function
Direct ligand for ERBB3 and ERBB4 tyrosine kinase receptors. Concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. May also promote the heterodimerization with the EGF receptor. -
Tissue specificity
Restricted to the cerebellum in the adult. -
Sequence similarities
Belongs to the neuregulin family.
Contains 1 EGF-like domain.
Contains 1 Ig-like C2-type (immunoglobulin-like) domain. -
Domain
The cytoplasmic domain may be involved in the regulation of trafficking and proteolytic processing. Regulation of the proteolytic processing involves initial intracellular domain dimerization.
ERBB receptor binding is elicited entirely by the EGF-like domain. -
Post-translational
modificationsProteolytic cleavage close to the plasma membrane on the external face leads to the release of the soluble growth factor form.
Extensive glycosylation precedes the proteolytic cleavage. -
Cellular localization
Secreted and Cell membrane. Does not seem to be active. - Information by UniProt
Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
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Datasheet download
References (0)
ab152998 has not yet been referenced specifically in any publications.