Product nameAnti-ErbB2 Affibody® Molecule (Biotin)
See all ErbB 2 affibody® molecule
Conjugation notesThis molecule is biotinylated at the unique C-terminal cysteine using a maleimide-biotin reagent.
Tested applicationsSuitable for: IHC-Fr, ICC/IF, Flow Cytmore details
Species reactivityReacts with: Human
This product is a recombinant protein produced in E.coli.
What are Affibody Molecules?
Affibody® affinity ligands are unique research reagents, produced using innovative protein-engineering technologies. They are small, simple proteins composed of a three-helix bundle based on the scaffold of one of the IgG-binding domains of Protein A. Protein A is a surface protein from the bacterium Staphylococcus aureus. This scaffold has excellent features as an affinity ligand and can be designed to bind with high affinity to any given target protein. The domain consists of 58 amino acids, 13 of which are randomized to generate Affibody® libraries with a large number of ligand variants. Thus, the libraries consist of a multitude of protein ligands with an identical backbone and variable surface-binding properties. In function, Affibody® Molecules mimic monoclonal antibodies. Compared to antibodies, the most striking dissimilarity of Affibody® Molecules is the small size. Affibody® Molecules have a molecular weight of 6kDa, compared to the molecular weight of antibodies, which is 150kDa. In spite of its small size, the binding site of Affibody® Molecules is similar to that of an antibody. The advantages of Affibody® Molcules over antibodies are: -their small size -the simple structure of the molecules -its robust physical properties; able to withstand a broad range of analytical conditions, including extreme pH and elevated temperature -its ability to fold correctly intracellularly -the fast and cost effective production in bacteria -the potential to couple Affibody® Molecules in multimeric constructs Affibody® Molecules have highly competitive properties for applications within affinity purification, sample preparation, protein detection and in vitro diagnostics.
Storage instructionsShipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C long term. Store In the Dark.
Storage bufferpH: 7.20
Preservative: 0.02% Sodium azide
Constituents: 0.328% Sodium phosphate, 0.87% Sodium chloride
Concentration information loading...
Purification notesThe purity of this product is >98% as determined by RP-HPLC analysis.
FunctionProtein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization.
In the nucleus is involved in transcriptional regulation. Associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter and activates its transcription. Implicated in transcriptional activation of CDKN1A; the function involves STAT3 and SRC. Involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell growth.
Tissue specificityExpressed in a variety of tumor tissues including primary breast tumors and tumors from small bowel, esophagus, kidney and mouth.
Involvement in diseaseHereditary diffuse gastric cancer
Chromosomal aberrations involving ERBB2 may be a cause gastric cancer. Deletions within 17q12 region producing fusion transcripts with CDK12, leading to CDK12-ERBB2 fusion leading to truncated CDK12 protein not in-frame with ERBB2.
Sequence similaritiesBelongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily.
Contains 1 protein kinase domain.
modificationsAutophosphorylated. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit (Probable). Ligand-binding increases phosphorylation on tyrosine residues (PubMed:27134172). Signaling via SEMA4C promotes phosphorylation at Tyr-1248 (PubMed:17554007). Dephosphorylated by PTPN12 (PubMed:27134172).
Cellular localizationCytoplasm. Nucleus and Cell membrane. Cytoplasm, perinuclear region. Nucleus. Translocation to the nucleus requires endocytosis, probably endosomal sorting and is mediated by importin beta-1/KPNB1.
- Information by UniProt
- Verb b2 erythroblastic leukemia viral oncogene homolog 2, neuro/glioblastoma derived oncogene homolog
- C erb B2/neu protein
Our Abpromise guarantee covers the use of ab31890 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|IHC-Fr||Use at an assay dependent dilution.
Staining of paraffin embedded tissues is not recommended. AFFIBODY® MOLECULES ARE PROTOCOL SPECIFIC. PLEASE REFER TO THE "PROTOCOLS" SECTION.
|ICC/IF||Use at an assay dependent dilution.|
|Flow Cyt||Use at an assay dependent dilution.|
Cells of the human mammary gland cell line SK-BR3 were stained with biotin conjugated Anti-ErbB2 Affibody® molecule (ab31890). The staining was localized to the membrane of the ErbB2 expressing human mammary gland cells. Nuclei were counter stained with DAPI (blue fluorescence).
The SK-BR3 cells were stained for 30 minutes at a concentration of 1-5ug Affibody® molecule/ml.