Phospho-DDR1/DDR2 (Tyr796/740) Antibody (Mouse mAb) [M16G11]

Application: Reactivity: Human

Usage Information

Dilution
WB1:5000

Application
WB

Reactivity
Human

Source
Mouse Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
97 kDa 120-130 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
Phospho-DDR1/DDR2 (Tyr796/740) Antibody (Mouse mAb) [M16G11] detects endogenous levels of total DDR1/DDR2 protein only when it is phosphorylated at Tyr796/740.

Clone
M16G11

Synonym(s)
6030432F18;AI323681;CAK;CD167;CD167a;DDR;DDR1;Drd1;EDDR1;HGK2;MCK10;Mpk6;NEP;NTRK4;PTK3;PTK3A;PTK3D;RTK6;TRKE

Background
Phospho‑DDR1/DDR2 (Tyr796/740) refers to the activated forms of the collagen receptors DDR1 and DDR2, two discoidin domain receptor tyrosine kinases that integrate extracellular matrix cues with intracellular signaling controlling adhesion, migration, and matrix remodeling. DDR1 carries a discoidin‑like collagen‑binding domain, a single transmembrane segment, a juxtamembrane region, and an intracellular kinase domain whose activation loop contains Tyr796; collagen engagement induces slow but sustained receptor autophosphorylation on multiple tyrosines, and antibodies specific for phospho‑Tyr796 detect DDR1 only in this ligand‐activated state, marking the productive kinase conformation that propagates downstream signaling. DDR2 shares a similar domain layout and is likewise activated by fibrillar collagens, but Tyr740 sits within its activation loop as a regulatory site that is phosphorylated not only during receptor autophosphorylation but also directly by Src family kinases, creating a key control point for DDR2 signaling output. Biochemical dissection of DDR2 shows that Src targets three activation‑loop residues (Tyr736, Tyr740, Tyr741); phosphorylation at Tyr740 stimulates intramolecular DDR2 autophosphorylation on additional cytoplasmic tyrosines, which then serve as docking sites for the adaptor Shc and assembly of DDR2–Shc signaling complexes, linking collagen engagement to Ras–MAPK and other Shc‑dependent pathways. Mutation of Tyr740 to phenylalanine relieves an inhibitory constraint within the activation loop, producing a receptor that displays collagen‑independent autophosphorylation and constitutive signaling, indicating that the unphosphorylated Tyr740 side chain restrains kinase activity and that its modification or substitution shifts DDR2 toward an active conformation. Across DDR1 and DDR2, phosphorylation at Tyr796 and Tyr740 therefore defines collagen‑ and Src‑responsive activation loop states that control receptor autophosphorylation, adaptor recruitment, and signal propagation into pathways regulating cell–matrix adhesion, motility, and tissue remodeling, and assays that specifically quantify phospho‑DDR1 (Tyr796) and phospho‑DDR2 (Tyr740) in lysates provide a direct biochemical readout of discoidin receptor engagement by collagen and of Src‑dependent tuning of DDR2 activity in physiological and pathological contexts.

Background

Phospho‑DDR1/DDR2 (Tyr796/740) refers to the activated forms of the collagen receptors DDR1 and DDR2, two discoidin domain receptor tyrosine kinases that integrate extracellular matrix cues with intracellular signaling controlling adhesion, migration, and matrix remodeling. DDR1 carries a discoidin‑like collagen‑binding domain, a single transmembrane segment, a juxtamembrane region, and an intracellular kinase domain whose activation loop contains Tyr796; collagen engagement induces slow but sustained receptor autophosphorylation on multiple tyrosines, and antibodies specific for phospho‑Tyr796 detect DDR1 only in this ligand‐activated state, marking the productive kinase conformation that propagates downstream signaling. DDR2 shares a similar domain layout and is likewise activated by fibrillar collagens, but Tyr740 sits within its activation loop as a regulatory site that is phosphorylated not only during receptor autophosphorylation but also directly by Src family kinases, creating a key control point for DDR2 signaling output. Biochemical dissection of DDR2 shows that Src targets three activation‑loop residues (Tyr736, Tyr740, Tyr741); phosphorylation at Tyr740 stimulates intramolecular DDR2 autophosphorylation on additional cytoplasmic tyrosines, which then serve as docking sites for the adaptor Shc and assembly of DDR2–Shc signaling complexes, linking collagen engagement to Ras–MAPK and other Shc‑dependent pathways. Mutation of Tyr740 to phenylalanine relieves an inhibitory constraint within the activation loop, producing a receptor that displays collagen‑independent autophosphorylation and constitutive signaling, indicating that the unphosphorylated Tyr740 side chain restrains kinase activity and that its modification or substitution shifts DDR2 toward an active conformation. Across DDR1 and DDR2, phosphorylation at Tyr796 and Tyr740 therefore defines collagen‑ and Src‑responsive activation loop states that control receptor autophosphorylation, adaptor recruitment, and signal propagation into pathways regulating cell–matrix adhesion, motility, and tissue remodeling, and assays that specifically quantify phospho‑DDR1 (Tyr796) and phospho‑DDR2 (Tyr740) in lysates provide a direct biochemical readout of discoidin receptor engagement by collagen and of Src‑dependent tuning of DDR2 activity in physiological and pathological contexts.

References
https://pubmed.ncbi.nlm.nih.gov/16186108/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%