Key features and details
- Expression system: Sf9 cells
- Purity: >= 43% SDS-PAGE
- Active: Yes
- Tags: GST tag N-Terminus
- Suitable for: Functional Studies, SDS-PAGE
Product nameRecombinant human ErbB2 / HER2 protein (Active)
See all ErbB2 / HER2 proteins and peptides
Activity ≥40 pmole/min/µg.
Assay was done in Kinase buffer containing 2 mM DTT using Poly- (Glu:Tyr) substrate (0.2 mg/ml) and 20 µM ATP. Reaction was done at 30oC for 45 min.
Purity>= 43 % SDS-PAGE.
Expression systemSf9 cells
Protein lengthProtein fragment
SequenceQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETELRKVKVLGS GAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQ IAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYH ADGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPA REIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVSEFSR MARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLVDAEEYLVPQQ GFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPS EGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYV APLTCSPQPEYVNQPDVRPQPPSPREGPLPAARPAGATLERPKTLSPGKN GVVKDVFAFGGAVENPEYLTPQGGAAPQPHPPPAFSPAFDNLYYWDQDPP ERGAPPSTFKGTPTAENPEYLGLDVPV
Predicted molecular weight89 kDa including tags
Amino acids679 to 1255
TagsGST tag N-Terminus
Additional sequence informationNM_004448
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Preparation and Storage
Stability and Storage
Shipped on Dry Ice. Store at -80°C. Avoid freeze / thaw cycle.
Constituents: 0.63% Tris HCl, 0.64% Sodium chloride, 0.02% Potassium chloride, 20% Glycerol, 0.61% Glutathione, 0.05% DTT
This product is an active protein and may elicit a biological response in vivo, handle with caution.
- Verb b2 erythroblastic leukemia viral oncogene homolog 2, neuro/glioblastoma derived oncogene homolog
- C erb B2/neu protein
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
ab269979 has not yet been referenced specifically in any publications.