Thermo Fisher Scientific Angiopoietin 2 Monoclonal Antibody (OTI3H7)

Applications

Tested Dilution

Publications

Western Blot (WB)

1:500

-

Immunohistochemistry (Paraffin) (IHC (P))

1:150

-

Product Specifications

Species Reactivity

Human

Host/Isotype

Mouse / IgG1

Class

Monoclonal

Type

Antibody

Clone

OTI3H7

Immunogen

Human recombinant protein fragment corresponding to amino acids 19-496 of ANGPT2 produced in E.coli if (typeof window.$mangular === undefined || !window.$mangular) { window.$mangular = {}; } $mangular.antigenJson = \[{targetFamily:Angiopoietin 2,uniProtId:O15123-1,ncbiNodeId:9606,antigenRange:19-496,antigenLength:496,antigenImageFileName:MA5-26781_Angiopoietin_2_O15123-1_House_mouse.svg,antigenImageFileNamePDP:MA5-26781_Angiopoietin_2_O15123-1_House_mouse_PDP.jpeg,sortOrder:1}\]; $mangular.isB2BCMGT = false; $mangular.isEpitopesModalImageMultiSizeEnabled = true;

View immunogen .st0{fill:#FFFFFF;} .st1{fill:#1E8AE7;}

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Liquid

Concentration

1 mg/mL

Purification

Affinity Chromatography

Storage buffer

PBS, pH 7.3, with 1% BSA, 50% glycerol

Contains

0.02% sodium azide

Storage conditions

-20° C, Avoid Freeze/Thaw Cycles

Shipping conditions

Ambient (domestic); Wet ice (international)

RRID

AB_2723872

Target Information

ANG-2 binds to the endothelial cell specific receptor Tie-2, but, in contrast to ANG-1, does not induce tyrosine phosphorylation. Consequently, ANG-2 modulates ANG-1 activation of Tie-2 and, depending on the physiological and biochemical environment, can act either as an agonist or antagonist of Tie-2 induced angiogenesis. The signaling interactions of ANG-1, ANG-2 and Tie-2, along with less characterized ANG-3 and ANG-4, are required for embryonic and adult angiogenesis. Physiologically, ANG-1 and ANG-2 are associated with sprouting, tube formation, and structural integrity of newly formed blood vessels. Mature human ANG-2 is a secreted protein containing 480 amino acid residues. ANG-2 is composed of an alpha-helix-rich coiled coil N-terminal domain and fibrinogen-like C-terminal domain. ANG-2 exists predominantly in the form of a disulfide-linked dimer.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.