Phospho-HER3/ErbB3 (Tyr1289) Antibody - #AF3802
Product: | Phospho-HER3/ErbB3 (Tyr1289) Antibody |
Catalog: | AF3802 |
Description: | Rabbit polyclonal antibody to Phospho-HER3/ErbB3 (Tyr1289) |
Application: | ELISA(peptide) |
Reactivity: | Human, Mouse, Rat |
Mol.Wt.: | 148kD(Calculated). |
Uniprot: | P21860 |
RRID: | AB_2847116 |
Product Info
*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
Cite Format: Affinity Biosciences Cat# AF3802, RRID:AB_2847116.
Fold/Unfold
c erbB 3; c erbB3; Erb b2 receptor tyrosine kinase 3; ErbB 3; ERBB3; ERBB3 protein; erbB3 S; ERBB3_HUMAN; Glial growth factor receptor; HER 3; HER3; Human epidermal growth factor receptor 3; LCCS2; MDA BF 1; MGC88033; p180 ErbB3; p45 sErbB3; p85 sErbB3; proto-oncogene-like protein c ErbB 3; proto-oncogene-like protein c ErbB3; Proto-oncogene-like protein c-ErbB-3; Receptor tyrosine protein kinase erbB 3; Receptor tyrosine protein kinase erbB3; Receptor tyrosine-protein kinase erbB-3; Tyrosine kinase type cell surface receptor HER3; Tyrosine kinase-type cell surface receptor HER3; v erb b2 avian erythroblastic leukemia viral oncogene homolog 3; v erb b2 erythroblastic leukemia viral oncogene homolog 3 (avian); v erb b2 erythroblastic leukemia viral oncogene homolog 3;
Immunogens
A synthesized peptide derived from human HER3/ErbB3 around the phosphorylation site of Tyr1289.
- P21860 ERBB3_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MRANDALQVLGLLFSLARGSEVGNSQAVCPGTLNGLSVTGDAENQYQTLYKLYERCEVVMGNLEIVLTGHNADLSFLQWIREVTGYVLVAMNEFSTLPLPNLRVVRGTQVYDGKFAIFVMLNYNTNSSHALRQLRLTQLTEILSGGVYIEKNDKLCHMDTIDWRDIVRDRDAEIVVKDNGRSCPPCHEVCKGRCWGPGSEDCQTLTKTICAPQCNGHCFGPNPNQCCHDECAGGCSGPQDTDCFACRHFNDSGACVPRCPQPLVYNKLTFQLEPNPHTKYQYGGVCVASCPHNFVVDQTSCVRACPPDKMEVDKNGLKMCEPCGGLCPKACEGTGSGSRFQTVDSSNIDGFVNCTKILGNLDFLITGLNGDPWHKIPALDPEKLNVFRTVREITGYLNIQSWPPHMHNFSVFSNLTTIGGRSLYNRGFSLLIMKNLNVTSLGFRSLKEISAGRIYISANRQLCYHHSLNWTKVLRGPTEERLDIKHNRPRRDCVAEGKVCDPLCSSGGCWGPGPGQCLSCRNYSRGGVCVTHCNFLNGEPREFAHEAECFSCHPECQPMEGTATCNGSGSDTCAQCAHFRDGPHCVSSCPHGVLGAKGPIYKYPDVQNECRPCHENCTQGCKGPELQDCLGQTLVLIGKTHLTMALTVIAGLVVIFMMLGGTFLYWRGRRIQNKRAMRRYLERGESIEPLDPSEKANKVLARIFKETELRKLKVLGSGVFGTVHKGVWIPEGESIKIPVCIKVIEDKSGRQSFQAVTDHMLAIGSLDHAHIVRLLGLCPGSSLQLVTQYLPLGSLLDHVRQHRGALGPQLLLNWGVQIAKGMYYLEEHGMVHRNLAARNVLLKSPSQVQVADFGVADLLPPDDKQLLYSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWELMTFGAEPYAGLRLAEVPDLLEKGERLAQPQICTIDVYMVMVKCWMIDENIRPTFKELANEFTRMARDPPRYLVIKRESGPGIAPGPEPHGLTNKKLEEVELEPELDLDLDLEAEEDNLATTTLGSALSLPVGTLNRPRGSQSLLSPSSGYMPMNQGNLGESCQESAVSGSSERCPRPVSLHPMPRGCLASESSEGHVTGSEAELQEKVSMCRSRSRSRSPRPRGDSAYHSQRHSLLTPVTPLSPPGLEEEDVNGYVMPDTHLKGTPSSREGTLSSVGLSSVLGTEEEDEDEEYEYMNRRRRHSPPHPPRPSSLEELGYEYMDVGSDLSASLGSTQSCPLHPVPIMPTAGTTPDEDYEYMNRQRDGGGPGGDYAAMGACPASEQGYEEMRAFQGPGHQAPHVHYARLKTLRSLEATDSAFDNPDYWHSRLFPKANAQRT
PTMs - P21860 As Substrate
Site | PTM Type | Enzyme | Source |
---|---|---|---|
S15 | Phosphorylation | Uniprot | |
N250 | N-Glycosylation | Uniprot | |
N353 | N-Glycosylation | Uniprot | |
N408 | N-Glycosylation | Uniprot | |
N414 | N-Glycosylation | Uniprot | |
N437 | N-Glycosylation | Uniprot | |
N469 | N-Glycosylation | Uniprot | |
N522 | N-Glycosylation | Uniprot | |
N566 | N-Glycosylation | Uniprot | |
T640 | Phosphorylation | Uniprot | |
Y680 | Phosphorylation | Uniprot | |
S686 | Phosphorylation | Uniprot | |
S693 | Phosphorylation | Uniprot | |
S717 | Phosphorylation | Uniprot | |
K736 | Methylation | Uniprot | |
S844 | Phosphorylation | Uniprot | |
S846 | Phosphorylation | Uniprot | |
Y868 | Phosphorylation | Uniprot | |
S869 | Phosphorylation | Uniprot | |
S982 | Phosphorylation | Uniprot | |
T996 | Phosphorylation | Uniprot | |
Y1054 | Phosphorylation | Uniprot | |
S1083 | Phosphorylation | Uniprot | |
S1094 | Phosphorylation | Uniprot | |
S1104 | Phosphorylation | Uniprot | |
S1113 | Phosphorylation | Uniprot | |
Y1132 | Phosphorylation | Uniprot | |
S1147 | Phosphorylation | Uniprot | |
Y1159 | Phosphorylation | Uniprot | |
T1164 | Phosphorylation | Uniprot | |
Y1197 | Phosphorylation | Uniprot | |
Y1199 | Phosphorylation | Uniprot | |
S1207 | Phosphorylation | Uniprot | |
S1215 | Phosphorylation | Uniprot | |
Y1222 | Phosphorylation | Uniprot | |
Y1260 | Phosphorylation | Uniprot | |
Y1262 | Phosphorylation | Uniprot | |
Y1276 | Phosphorylation | P00533 (EGFR) | Uniprot |
S1285 | Phosphorylation | Uniprot | |
Y1289 | Phosphorylation | P00533 (EGFR) | Uniprot |
Y1307 | Phosphorylation | Q01973 (ROR1) | Uniprot |
T1312 | Phosphorylation | Uniprot | |
S1315 | Phosphorylation | Uniprot | |
T1319 | Phosphorylation | Uniprot | |
Y1328 | Phosphorylation | Uniprot | |
S1331 | Phosphorylation | Uniprot |
Research Backgrounds
Tyrosine-protein kinase that plays an essential role as cell surface receptor for neuregulins. Binds to neuregulin-1 (NRG1) and is activated by it; ligand-binding increases phosphorylation on tyrosine residues and promotes its association with the p85 subunit of phosphatidylinositol 3-kinase. May also be activated by CSPG5. Involved in the regulation of myeloid cell differentiation.
Autophosphorylated. Ligand-binding increases phosphorylation on tyrosine residues and promotes its association with the p85 subunit of phosphatidylinositol 3-kinase.
Cell membrane>Single-pass type I membrane protein.
Secreted.
Epithelial tissues and brain.
Monomer and homodimer. Heterodimer with each of the other ERBB receptors (Potential). Interacts with CSPG5. Interacts with GRB7. Interacts with MUC1. Interacts with MYOC (By similarity). Interacts with isoform 2 of PA2G4. Found in a ternary complex with NRG1 and ITGAV:ITGB3 or ITGA6:ITGB4.
The cytoplasmic part of the receptor may interact with the SH2 or SH3 domains of many signal-transducing proteins.
Belongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily.
Research Fields
· Environmental Information Processing > Signal transduction > MAPK signaling pathway. (View pathway)
· Environmental Information Processing > Signal transduction > ErbB signaling pathway. (View pathway)
· Environmental Information Processing > Signal transduction > Calcium signaling pathway. (View pathway)
· Environmental Information Processing > Signal transduction > PI3K-Akt signaling pathway. (View pathway)
· Human Diseases > Drug resistance: Antineoplastic > EGFR tyrosine kinase inhibitor resistance.
· Human Diseases > Cancers: Overview > Proteoglycans in cancer.
· Human Diseases > Cancers: Overview > MicroRNAs in cancer.
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