ErbB 2 Blocking Peptide peptide (Phospho) (STJ504715)

SKU:
STJ504715-250

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Applications: Immunodepletion/Immunocompetition
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description: Phospho-ErbB 2 Blocking Peptide is synthetically produced from the 1100-1150 sequence and is suitable for use in western blot applications.
Storage Instruction: Store at-20°C for long term storage. Avoid freeze-thaw cycles.
Gene Symbol: ERBB2
Gene ID: 2064
Uniprot ID: ERBB2_HUMAN
Immunogen Region: 1100-1150
Immunogen: Phoshporylated synthetic peptide taken within amino acid region 1100-1150 on human HER-2 protein
Tissue Specificity Expressed in a variety of tumor tissues including primary breast tumors and tumors from small bowel, esophagus, kidney and mouth.
Post Translational Modifications Autophosphorylated. 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. Signaling via SEMA4C promotes phosphorylation at Tyr-1248. Dephosphorylated by PTPN12.
Function Protein 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.
Peptide Name Receptor Tyrosine-Protein Kinase Erbb-2
Metastatic Lymph Node Gene 19 Protein
Mln 19
Proto-Oncogene Neu
Proto-Oncogene C-Erbb-2
Tyrosine Kinase-Type Cell Surface Receptor Her2
P185erbb2
Cd Antigen Cd340
Database Links Reactome: R-HSA-1227986
Reactome: R-HSA-1250196
Reactome: R-HSA-1251932
Reactome: R-HSA-1257604
Reactome: R-HSA-1306955
Reactome: R-HSA-1358803
Reactome: R-HSA-1963640
Reactome: R-HSA-1963642
Reactome: R-HSA-2219530
Reactome: R-HSA-416572
Reactome: R-HSA-5673001
Reactome: R-HSA-6785631
Reactome: R-HSA-6811558
Reactome: R-HSA-8847993
Reactome: R-HSA-8863795
Reactome: R-HSA-8866910
Reactome: R-HSA-9634285
Reactome: R-HSA-9652282
Reactome: R-HSA-9664565
Reactome: R-HSA-9665233
Reactome: R-HSA-9665244
Reactome: R-HSA-9665245
Reactome: R-HSA-9665246
Reactome: R-HSA-9665247
Reactome: R-HSA-9665249
Reactome: R-HSA-9665250
Reactome: R-HSA-9665251
Reactome: R-HSA-9665348
Reactome: R-HSA-9665686
Reactome: R-HSA-9665737
Cellular Localisation Cell Membrane
Single-Pass Type I Membrane Protein
Cell Projection
Ruffle Membrane
Internalized From The Cell Membrane In Response To Egf Stimulation
Isoform 1: Cell Membrane
Early Endosome
Cytoplasm
Perinuclear Region
Nucleus
Translocation To The Nucleus Requires Endocytosis
Probably Endosomal Sorting And Is Mediated By Importin Beta-1/Kpnb1
Also Detected In Vps35-Positive Endosome-To-Tgn Retrograde Vesicles
Isoform 2: Cytoplasm
Isoform 3: Cytoplasm
Alternative Peptide Names Receptor Tyrosine-Protein Kinase Erbb-2 protein
Metastatic Lymph Node Gene 19 Protein protein
Mln 19 protein
Proto-Oncogene Neu protein
Proto-Oncogene C-Erbb-2 protein
Tyrosine Kinase-Type Cell Surface Receptor Her2 protein
P185erbb2 protein
Cd Antigen Cd340 protein
ERBB2 protein
HER2 protein
MLN19 protein
NEU protein
NGL protein

Information sourced from Uniprot.org

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