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ABS219

Sigma-Aldrich

Anti-phospho-Tie2 (Ser1119) Antibody

from rabbit, purified by affinity chromatography

Synonym(s):

Angiopoietin-1 receptor, Tunica interna endothelial cell kinase, Tyrosine-protein kinase receptor TEK, Tyrosine-protein kinase receptor TIE-2, hTIE2, p140 TEK, CD202b

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

rabbit

Quality Level

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

purified by

affinity chromatography

species reactivity

human

species reactivity (predicted by homology)

mouse (based on 100% sequence homology), rat (based on 100% sequence homology), bovine (based on 100% sequence homology)

technique(s)

western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

phosphorylation (pSer1119)

Gene Information

human ... TEK(7010)

General description

TIE2 (tyrosine kinase with Ig and EGF homology domains 2) is expressed almost exclusively in endothelial cells in mice, rats and humans. This receptor possesses a unique extracellular domain containing two immunoglobulin-like loops separated by three epidermal growth factor-like repeats that are connected to three fibronectin type III-like repeats. The ligand for the receptor is Angiopoietin 1. Defects in TIE2 are associated with inherited venous malformations; the TIE2 signaling pathway appears to be critical for endothelial cell-smooth muscle cell communication in venous morphogenesis.

Specificity

This antibody recognizes Tie2 phosphorylated at Ser1119.

Immunogen

Epitope: Phosphorylated Ser1119
KLH-conjugated linear peptide corresponding to human Tie2 phosphorylated at Ser1119.

Application

Anti-phospho-Tie2 (Ser1119) Antibody is an antibody against phospho-Tie2 (Ser1119) for use in WB.
Research Category
Signaling
Research Sub Category
Kinases & Phosphatases

Quality

Evaluated by Western Blot in HEK293T overexpressing Tie2 protein.

Western Blot Analysis: A 1:500 dilution detected Tie2 on 10 µg of HEK293T overexpressing Tie2 protein.

Target description

~160 kDa observed. Uniprot gives a calculated molecular weight of 126 kDa, but has been observed at ~160 kDa due to glycosolation. A non-modified specific band appears at ~52 kDa in some lysates.

Physical form

Affinity purified
Purified rabbit polyclonal in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Storage and Stability

Stable for 1 year at 2-8°C from date of receipt.

Analysis Note

Control
HEK293T overexpressing Tie2 protein

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Sunil K Chauhan et al.
Arteriosclerosis, thrombosis, and vascular biology, 35(7), 1606-1615 (2015-05-23)
In angiogenesis, circulating mononuclear cells are recruited to vascular lesions; however, the underlying mechanisms are poorly understood. Here, we characterize the functional role of protein tyrosine kinase 7 (PTK7)-expressing CD11b(+) mononuclear cells in vitro and in vivo using a mouse
Tatiana Y Besschetnova et al.
Matrix biology : journal of the International Society for Matrix Biology, 42, 56-73 (2015-01-13)
It is well known that angiogenesis is linked to fibrotic processes in fibroproliferative diseases, but insights into pathophysiological processes are limited, due to lack of understanding of molecular mechanisms controlling endothelial and fibroblastic homeostasis. We demonstrate here that the matrix

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