Phospho-VEGFR3 (Tyr1230) Antibody - #AF3676
Product: | Phospho-VEGFR3 (Tyr1230) Antibody |
Catalog: | AF3676 |
Description: | Rabbit polyclonal antibody to Phospho-VEGFR3 (Tyr1230) |
Application: | IHC IF/ICC |
Reactivity: | Human, Mouse, Rat |
Mol.Wt.: | 153kD(Calculated). |
Uniprot: | P35916 |
RRID: | AB_2846990 |
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# AF3676, RRID:AB_2846990.
Fold/Unfold
EC 2.7.10.1; flt 4; FLT-4; FLT4; FLT41; Fms related tyrosine kinase 4; Fms-like tyrosine kinase 4; LMPH1A; PCL; Soluble VEGFR3 variant 1; Soluble VEGFR3 variant 2; Soluble VEGFR3 variant 3; Tyrosine protein kinase receptor FLT4; Tyrosine-protein kinase receptor FLT4; Vascular endothelial growth factor receptor 3; Vascular endothelial growth factor receptor 3 precursor; VEGF R3; VEGFR 3; VEGFR-3; VEGFR3; VGFR3_HUMAN;
Immunogens
A synthesized peptide derived from human VEGFR3 around the phosphorylation site of Tyr1230.
Detected in endothelial cells (at protein level). Widely expressed. Detected in fetal spleen, lung and brain. Detected in adult liver, muscle, thymus, placenta, lung, testis, ovary, prostate, heart, and kidney.
- P35916 VGFR3_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MQRGAALCLRLWLCLGLLDGLVSGYSMTPPTLNITEESHVIDTGDSLSISCRGQHPLEWAWPGAQEAPATGDKDSEDTGVVRDCEGTDARPYCKVLLLHEVHANDTGSYVCYYKYIKARIEGTTAASSYVFVRDFEQPFINKPDTLLVNRKDAMWVPCLVSIPGLNVTLRSQSSVLWPDGQEVVWDDRRGMLVSTPLLHDALYLQCETTWGDQDFLSNPFLVHITGNELYDIQLLPRKSLELLVGEKLVLNCTVWAEFNSGVTFDWDYPGKQAERGKWVPERRSQQTHTELSSILTIHNVSQHDLGSYVCKANNGIQRFRESTEVIVHENPFISVEWLKGPILEATAGDELVKLPVKLAAYPPPEFQWYKDGKALSGRHSPHALVLKEVTEASTGTYTLALWNSAAGLRRNISLELVVNVPPQIHEKEASSPSIYSRHSRQALTCTAYGVPLPLSIQWHWRPWTPCKMFAQRSLRRRQQQDLMPQCRDWRAVTTQDAVNPIESLDTWTEFVEGKNKTVSKLVIQNANVSAMYKCVVSNKVGQDERLIYFYVTTIPDGFTIESKPSEELLEGQPVLLSCQADSYKYEHLRWYRLNLSTLHDAHGNPLLLDCKNVHLFATPLAASLEEVAPGARHATLSLSIPRVAPEHEGHYVCEVQDRRSHDKHCHKKYLSVQALEAPRLTQNLTDLLVNVSDSLEMQCLVAGAHAPSIVWYKDERLLEEKSGVDLADSNQKLSIQRVREEDAGRYLCSVCNAKGCVNSSASVAVEGSEDKGSMEIVILVGTGVIAVFFWVLLLLIFCNMRRPAHADIKTGYLSIIMDPGEVPLEEQCEYLSYDASQWEFPRERLHLGRVLGYGAFGKVVEASAFGIHKGSSCDTVAVKMLKEGATASEHRALMSELKILIHIGNHLNVVNLLGACTKPQGPLMVIVEFCKYGNLSNFLRAKRDAFSPCAEKSPEQRGRFRAMVELARLDRRRPGSSDRVLFARFSKTEGGARRASPDQEAEDLWLSPLTMEDLVCYSFQVARGMEFLASRKCIHRDLAARNILLSESDVVKICDFGLARDIYKDPDYVRKGSARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGVQINEEFCQRLRDGTRMRAPELATPAIRRIMLNCWSGDPKARPAFSELVEILGDLLQGRGLQEEEEVCMAPRSSQSSEEGSFSQVSTMALHIAQADAEDSPPSLQRHSLAARYYNWVSFPGCLARGAETRGSSRMKTFEEFPMTPTTYKGSVDNQTDSGMVLASEEFEQIESRHRQESGFSCKGPGQNVAVTRAHPDSQGRRRRPERGARGGQVFYNSEYGELSEPSEEDHCSPSARVTFFTDNSY
PTMs - P35916 As Substrate
Site | PTM Type | Enzyme | Source |
---|---|---|---|
N33 | N-Glycosylation | Uniprot | |
N104 | N-Glycosylation | Uniprot | |
N411 | N-Glycosylation | Uniprot | |
N515 | N-Glycosylation | Uniprot | |
T517 | Phosphorylation | Uniprot | |
N527 | N-Glycosylation | Uniprot | |
Y830 | Phosphorylation | P12931 (SRC) | Uniprot |
Y833 | Phosphorylation | P12931 (SRC) | Uniprot |
Y853 | Phosphorylation | P12931 (SRC) | Uniprot |
S863 | Phosphorylation | Uniprot | |
S871 | Phosphorylation | Uniprot | |
T886 | Phosphorylation | Uniprot | |
S976 | Phosphorylation | Uniprot | |
S986 | Phosphorylation | Uniprot | |
Y1063 | Phosphorylation | P35916 (FLT4) , P12931 (SRC) | Uniprot |
K1064 | Ubiquitination | Uniprot | |
Y1068 | Phosphorylation | P35916 (FLT4) | Uniprot |
K1079 | Ubiquitination | Uniprot | |
S1163 | Phosphorylation | Uniprot | |
Y1230 | Phosphorylation | P35968 (KDR) , P35916 (FLT4) | Uniprot |
Y1231 | Phosphorylation | P35916 (FLT4) , P35968 (KDR) | Uniprot |
S1235 | Phosphorylation | Uniprot | |
K1253 | Ubiquitination | Uniprot | |
Y1265 | Phosphorylation | P35968 (KDR) , P35916 (FLT4) | Uniprot |
K1300 | Ubiquitination | Uniprot | |
Y1333 | Phosphorylation | P35916 (FLT4) , P35968 (KDR) , P12931 (SRC) | Uniprot |
Y1337 | Phosphorylation | P12931 (SRC) , P35916 (FLT4) | Uniprot |
Y1363 | Phosphorylation | P35916 (FLT4) | Uniprot |
PTMs - P35916 As Enzyme
Substrate | Site | Source |
---|---|---|
P29353 (SHC1) | Y349 | Uniprot |
P29353 (SHC1) | Y350 | Uniprot |
P29353 (SHC1) | Y427 | Uniprot |
P35916 (FLT4) | Y1063 | Uniprot |
P35916 (FLT4) | Y1068 | Uniprot |
P35916 (FLT4) | Y1230 | Uniprot |
P35916 (FLT4) | Y1231 | Uniprot |
P35916 (FLT4) | Y1265 | Uniprot |
P35916 (FLT4) | Y1333 | Uniprot |
P35916 (FLT4) | Y1337 | Uniprot |
P35916 (FLT4) | Y1363 | Uniprot |
P51812 (RPS6KA3) | Y707 | Uniprot |
Research Backgrounds
Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFC and VEGFD, and plays an essential role in adult lymphangiogenesis and in the development of the vascular network and the cardiovascular system during embryonic development. Promotes proliferation, survival and migration of endothelial cells, and regulates angiogenic sprouting. Signaling by activated FLT4 leads to enhanced production of VEGFC, and to a lesser degree VEGFA, thereby creating a positive feedback loop that enhances FLT4 signaling. Modulates KDR signaling by forming heterodimers. The secreted isoform 3 may function as a decoy receptor for VEGFC and/or VEGFD and play an important role as a negative regulator of VEGFC-mediated lymphangiogenesis and angiogenesis. Binding of vascular growth factors to isoform 1 or isoform 2 leads to the activation of several signaling cascades; isoform 2 seems to be less efficient in signal transduction, because it has a truncated C-terminus and therefore lacks several phosphorylation sites. Mediates activation of the MAPK1/ERK2, MAPK3/ERK1 signaling pathway, of MAPK8 and the JUN signaling pathway, and of the AKT1 signaling pathway. Phosphorylates SHC1. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase. Promotes phosphorylation of MAPK8 at 'Thr-183' and 'Tyr-185', and of AKT1 at 'Ser-473'.
Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation in response to H(2)O(2) is mediated by a process that requires SRC and PRKCD activity. Phosphorylation at Tyr-1068 is required for autophosphorylation at additional tyrosine residues. Phosphorylation at Tyr-1063 and Tyr-1337 is important for interaction with CRK and subsequent activation of MAPK8. Phosphorylation at Tyr-1230, Tyr-1231 and Tyr-1337 is important for interaction with GRB2 and subsequent activation of the AKT1 and MAPK1/ERK2 and/or MAPK3/ERK1 signaling pathways. In response to endothelial cell adhesion onto collagen, can also be phosphorylated in the absence of FLT4 kinase activity by SRC at Tyr-830, Tyr-833, Tyr-853, Tyr-1063, Tyr-1333, and Tyr-1337.
Cell membrane>Single-pass type I membrane protein. Cytoplasm. Nucleus.
Note: Ligand-mediated autophosphorylation leads to rapid internalization.
Cell membrane>Single-pass type I membrane protein.
Note: Ligand-mediated autophosphorylation leads to rapid internalization.
Cell membrane>Single-pass type I membrane protein.
Secreted. Cytoplasm.
Detected in endothelial cells (at protein level). Widely expressed. Detected in fetal spleen, lung and brain. Detected in adult liver, muscle, thymus, placenta, lung, testis, ovary, prostate, heart, and kidney.
Interacts with VEGFC and VEGFD. Monomer in the absence of bound VEGFC or VEGFD. Homodimer in the presence of bound VEGFC or VEGFD. Can also form a heterodimer with KDR. Interacts with PTPN14; the interaction is enhanced by stimulation with VEGFC. Interacts with CRK, GRB2, PTK2/FAK1, SHC1, PIK3R1 and PTPN11/SHP-2. Identified in a complex with SRC and ITGB1.
The first and second Ig-like C2-type (immunoglobulin-like) domains are sufficient for VEGFC binding (PubMed:23878260). The fourth and fifth Ig-like C2-type domains are sufficient for homodimerization (PubMed:23878260). The fifth and seventh Ig-like C2-type domains are required for autophosphorylation and further activation (PubMed:23878260).
Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.
Research Fields
· Cellular Processes > Cellular community - eukaryotes > Focal adhesion. (View pathway)
· Environmental Information Processing > Signal transduction > MAPK signaling pathway. (View pathway)
· Environmental Information Processing > Signal transduction > Ras signaling pathway. (View pathway)
· Environmental Information Processing > Signal transduction > Rap1 signaling pathway. (View pathway)
· Environmental Information Processing > Signaling molecules and interaction > Cytokine-cytokine receptor interaction. (View pathway)
· Environmental Information Processing > Signal transduction > PI3K-Akt signaling pathway. (View pathway)
· Human Diseases > Cancers: Overview > Pathways in cancer. (View pathway)
· Human Diseases > Cancers: Specific types > Breast cancer. (View pathway)
References
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