Product Detail
Product NameAngiopoietin-2 Antibody
Clone No.4A2
Host SpeciesMouse
ClonalityMonoclonal
PurificationProA affinity purified
ApplicationsWB, IP, IF, IHC
Species ReactivityHu, Ms, Rt
Immunogen Descpeptide
ConjugateUnconjugated
Other NamesAGPT 2 antibody Agpt2 antibody ANG 2 antibody ANG-2 antibody ANG2 antibody Angiopoietin 2a antibody Angiopoietin 2B antibody Angiopoietin-2 antibody Angiopoietin2 antibody ANGP2_HUMAN antibody ANGPT 2 antibody Angpt2 antibody Tie2 ligand antibody
Accession NoSwiss-Prot#:O15123
Uniprot
O15123
Gene ID
285;
Calculated MW62-70kDa
Formulation1*TBS (pH7.4), 1%BSA, 40%Glycerol. Preservative: 0.05% Sodium Azide.
StorageStore at -20˚C
Application Details
WB: 1:100-1:1,000
IHC: 1:50-500
IP: 1-2 μg per 100-500 μg of total protein(1 ml of cell lysate)
Western Blot analysis of Ang-2 expression in HUV-EC-C (A) and TF-1 (B) whole cell lysates.
Immunoperoxidase staining of formalin fixed, paraffin-embedded human placenta tissue showing cytoplasmic staining of trophoblastic cells at low (A) and high (B) magnification.
Tie-1 and Tie-2 (also designated Tek) are novel cell surface receptor tyrosine kinases. The extracellular domain of Tie-1 has an unusual multidomain structure consisting of a cluster of three epidermal growth factor homology motifs localized between two immunoglobulin-like loops, which are followed by three Fibronectin type III repeats next to the transmembrane region. Angiopoietin-1 (Ang-1) is a secreted ligand for Tie-2. Preliminary biochemical analyses of Ang-1 reveal a potential Fibrinogen-like domain at the carboxy-terminus and coiled-coil regions in the amino-terminus. Ang-1 is an angiogenic factor that is thought to be involved in endothelial development. A related protein, angiopoietin-2 (Ang-2), has been identified as a naturally occurring antagonist of Ang-1 activation of Tie-2. In adult tissue, Ang-2 expression seems to be restricted to sites of vascular remodeling.
If you have published an article using product 48274, please notify us so that we can cite your literature.