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Mouse Anti-FLT1 Monoclonal Antibody (6D1-G11) (CBMAB-1268-YC)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
6D1-G11
Antibody Isotype
IgG1
Application
ELISA

Basic Information

Immunogen
Extracellular domain of human VEGFR-1 (106 kD)
Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Purity
>95%, as determined by SDS-PAGE analysis
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Fms Related Tyrosine Kinase 1
Introduction
FLT1 is a member of the vascular endothelial growth factor receptor (VEGFR) family, which binds to VEGFR-A, VEGFR-B and placental growth factor and plays an important role in angiogenesis and vasculogenesis. FLT1 is found in vascular endothelial cells, placental trophoblast cells and peripheral blood monocytes.
Entrez Gene ID
2321
UniProt ID
P17948
Alternative Names
FLT; FLT-1; VEGFR1; VEGFR-1
Function
Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFB and PGF, and plays an essential role in the development of embryonic vasculature, the regulation of angiogenesis, cell survival, cell migration, macrophage function, chemotaxis, and cancer cell invasion. Acts as a positive regulator of postnatal retinal hyaloid vessel regression (Ref. 11). May play an essential role as a negative regulator of embryonic angiogenesis by inhibiting excessive proliferation of endothelial cells. Can promote endothelial cell proliferation, survival and angiogenesis in adulthood. Its function in promoting cell proliferation seems to be cell-type specific. Promotes PGF-mediated proliferation of endothelial cells, proliferation of some types of cancer cells, but does not promote proliferation of normal fibroblasts (in vitro). Has very high affinity for VEGFA and relatively low protein kinase activity; may function as a negative regulator of VEGFA signaling by limiting the amount of free VEGFA and preventing its binding to KDR. Modulates KDR signaling by forming heterodimers with KDR. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leading to activation of phosphatidylinositol kinase and the downstream signaling pathway. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Phosphorylates SRC and YES1, and may also phosphorylate CBL. Promotes phosphorylation of AKT1 at 'Ser-473'. Promotes phosphorylation of PTK2/FAK1 (PubMed:16685275).

Isoform 1:
Phosphorylates PLCG.

Isoform 2&3&4:
May function as decoy receptor for VEGFA.

Isoform 7:
Has a truncated kinase domain; it increases phosphorylation of SRC at 'Tyr-418' by unknown means and promotes tumor cell invasion.
Biological Process
Angiogenesis Source: UniProtKB-KW
Blood vessel morphogenesis Source: UniProtKB
Cell migration Source: UniProtKB
Cellular response to vascular endothelial growth factor stimulus Source: UniProtKB
Embryonic morphogenesis Source: UniProtKB
Hematopoietic progenitor cell differentiation Source: GO_Central
Hyaloid vascular plexus regression Source: UniProtKB
Monocyte chemotaxis Source: UniProtKB
Negative regulation of vascular endothelial cell proliferation Source: BHF-UCL
Peptidyl-tyrosine phosphorylation Source: UniProtKB
Positive regulation of angiogenesis Source: UniProtKB
Positive regulation of cell migration Source: UniProtKB
Positive regulation of cell population proliferation Source: ProtInc
Positive regulation of kinase activity Source: GO_Central
Positive regulation of MAPK cascade Source: UniProtKB
Positive regulation of MAP kinase activity Source: UniProtKB
Positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
Positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
Positive regulation of phospholipase C activity Source: UniProtKB
Protein autophosphorylation Source: UniProtKB
Transmembrane receptor protein tyrosine kinase signaling pathway Source: GO_Central
Vascular endothelial growth factor receptor-1 signaling pathway Source: UniProtKB
Vascular endothelial growth factor receptor signaling pathway Source: UniProtKB
Cellular Location
Isoform 1: Endosome; Cell membrane. Autophosphorylation promotes ubiquitination and endocytosis.
Isoform 2&3&4&5: Secreted
Isoform 5&6&7: Cytoplasm
Involvement in disease
Can contribute to cancer cell survival, proliferation, migration, and invasion, and tumor angiogenesis and metastasis. May contribute to cancer pathogenesis by promoting inflammatory responses and recruitment of tumor-infiltrating macrophages.
Abnormally high expression of soluble isoforms (isoform 2, isoform 3 or isoform 4) may be a cause of preeclampsia.
Topology
Extracellular: 27-758
Helical: 759-780
Cytoplasmic: 781-1338
PTM
N-glycosylated.
Ubiquitinated after VEGFA-mediated autophosphorylation, leading to proteolytic degradation.
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 at Tyr-1169 is important for interaction with PLCG. Phosphorylation at Tyr-1213 is important for interaction with PIK3R1, PTPN11, GRB2, and PLCG. Phosphorylation at Tyr-1333 is important for endocytosis and for interaction with CBL, NCK1 and CRK. Is probably dephosphorylated by PTPRB.
More Infomation

Zhao, L., Xin, S., Wu, Y., Huang, S., Xu, K., Xu, Y., ... & He, X. (2022). Global DNA and protein interactomes of FLT1P1 (Fms-related tyrosine kinase 1 pseudogene 1) revealed its molecular regulatory functions associated with preeclampsia. Molecular Biology Reports, 1-13.

Armistead, B., Kadam, L., Siegwald, E., McCarthy, F. P., Kingdom, J. C., Kohan-Ghadr, H. R., & Drewlo, S. (2021). Induction of the PPARγ (peroxisome proliferator-activated receptor γ)-GCM1 (glial cell missing 1) syncytialization axis reduces sFLT1 (soluble fms-like tyrosine kinase 1) in the preeclamptic placenta. Hypertension, 78(1), 230-240.

Chi, Z., Sun, Y., Yu, Z., Zhou, F., Wang, H., & Zhang, M. (2021). Pseudogene fms-related tyrosine kinase 1 pseudogene 1 (FLT1P1) cooperates with RNA binding protein dyskeratosis congenita 1 (DKC1) to restrain trophoblast cell proliferation and angiogenesis by targeting fms-related tyrosine kinase 1 (FLT1) in preeclampsia. Bioengineered, 12(1), 8885-8897.

M Dave, K., Kaur, L., Randhir, K. N., Mehendale, S. S., Sundrani, D. P., Chandak, G. R., & Joshi, S. R. (2021). Placental growth factor and Fms related tyrosine kinase-1 are hypomethylated in preeclampsia placentae. Epigenomics, 13(04), 257-269.

Creeden, J. F., Alganem, K., Imami, A. S., Brunicardi, F. C., Liu, S. H., Shukla, R., ... & McCullumsmith, R. E. (2020). Kinome array profiling of patient-derived pancreatic ductal adenocarcinoma identifies differentially active protein tyrosine kinases. International journal of molecular sciences, 21(22), 8679.

Kikas, T., Inno, R., Ratnik, K., Rull, K., & Laan, M. (2020). C-allele of rs4769613 near FLT1 represents a High-Confidence placental risk factor for preeclampsia. Hypertension, 76(3), 884-891.

Austdal, M., Silva, G. B., Bowe, S., Thomsen, L. C. V., Tangerås, L. H., Bjørge, L., ... & Iversen, A. C. (2019). Metabolomics identifies placental dysfunction and confirms Flt-1 (FMS-like tyrosine kinase receptor 1) biomarker specificity. Hypertension, 74(5), 1136-1143.

Shashar, M., Zubkov, A., Chernichovski, T., Hershkovitz, R., Hoffman, E., Grupper, A., ... & Schwartz, I. F. (2019). Profound decrease in glomerular arginine transport by CAT (cationic amino acid transporter)-1 contributes to the FLT-1 (FMS-like tyrosine kinase 1) induced preeclampsia in the pregnant mice. Hypertension, 73(4), 878-884.

Ji, S., Xin, H., Li, Y., & Su, E. J. (2018). FMS-like tyrosine kinase 1 (FLT1) is a key regulator of fetoplacental endothelial cell migration and angiogenesis. Placenta, 70, 7-14.

Greco, M., Palumbo, C., Sicuro, F., & Lobreglio, G. (2018). Soluble Fms-like tyrosine kinase-1 is a marker of endothelial dysfunction during sepsis. Journal of Clinical Medicine Research, 10(9), 700.

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For research use only. Not intended for any clinical use.

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