Overview

  • Product name
    Recombinant Human NRG2 protein
  • Protein length
    Protein fragment

Description

  • Nature
    Recombinant
  • Source
    Wheat germ
  • Amino Acid Sequence
    • Species
      Human
    • Sequence
      SLKSVQDQAYKAPVVVEGKVQGLVPAGGSSSNSTREPPASGRVALVKVLD KWPLRSGGLQREQVISVGSCVPLERNQRYIFFLEPTEQPLVFKTAFAPLD
    • Amino acids
      116 to 215
    • Tags
      proprietary tag N-Terminus

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.

  • Applications

    Western blot

    ELISA

  • Form
    Liquid
  • Additional notes
    Protein concentration is above or equal to 0.05 mg/ml.
  • Concentration information loading...

Preparation and Storage

  • 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

  • Alternative names
    • Divergent of neuregulin 1
    • Divergent of neuregulin-1
    • Don 1
    • DON-1
    • Neural- and thymus-derived activator for ERBB kinases
    • Neuregulin 2
    • Neuregulin-2
    • NRG-2
    • Nrg2
    • NRG2_HUMAN
    • NTAK
    • Pro NRG2
    • Pro-NRG2
    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
    modifications
    Proteolytic 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

Images

  • ab152998 on a 12.5% SDS-PAGE stained with Coomassie Blue.

References

ab152998 has not yet been referenced specifically in any publications.

Customer reviews and Q&As

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Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"

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