Datasheet

生物学的記述

Specificity	Phospho-Src (Tyr419) Antibody [D21H6] detects endogenous levels of total Src protein only when it is phosphorylated at Tyr419.
Background	Phospho-Src (Tyr419), the activation loop phosphorylation marking full catalytic competence of the Src family kinase prototype, unlocks bidirectional tyrosine kinase signaling from virtually all integrin, growth factor, and GPCR stimuli across adherent cells and platelets. Dephosphorylation of inhibitory Tyr530 by CD45/PTP1B relieves SH2 domain clamping, permitting trans-autophosphorylation at Tyr419 that rigidly positions the activation loop for substrate access while relieving steric occlusion of the ATP-binding cleft; this catalyzes hierarchical phosphorylation cascades where Src primes receptor tyrosine kinases through Y1009/1101 autophosphorylation on EGFR while amplifying FAK at Y397/576/577/861 to scaffold paxillin/PI3K recruitment. Active p-Tyr419-Src drives Ras-GRF1/ERK for proliferation, STAT3/5a for survival, and cortactin/pyk2 for invadopodia maturation via sequential Arp2/3 activation; feedback engages Csk/Shp1 through C-terminal docking to restore Tyr530 phosphorylation, while PP2A/PP1 dephosphorylate the activation loop for signal termination. In platelets, shear-induced clustering at podosome-like adhesions generates local p-Tyr419 gradients that license αIIbβ3 outside-in signaling for clot retraction, while fibroblasts exploit Src for durotaxis through myosin-IIA/Y1183 feedback with tension sensors.

Specificity

Phospho-Src (Tyr419) Antibody [D21H6] detects endogenous levels of total Src protein only when it is phosphorylated at Tyr419.

Background

Phospho-Src (Tyr419), the activation loop phosphorylation marking full catalytic competence of the Src family kinase prototype, unlocks bidirectional tyrosine kinase signaling from virtually all integrin, growth factor, and GPCR stimuli across adherent cells and platelets. Dephosphorylation of inhibitory Tyr530 by CD45/PTP1B relieves SH2 domain clamping, permitting trans-autophosphorylation at Tyr419 that rigidly positions the activation loop for substrate access while relieving steric occlusion of the ATP-binding cleft; this catalyzes hierarchical phosphorylation cascades where Src primes receptor tyrosine kinases through Y1009/1101 autophosphorylation on EGFR while amplifying FAK at Y397/576/577/861 to scaffold paxillin/PI3K recruitment. Active p-Tyr419-Src drives Ras-GRF1/ERK for proliferation, STAT3/5a for survival, and cortactin/pyk2 for invadopodia maturation via sequential Arp2/3 activation; feedback engages Csk/Shp1 through C-terminal docking to restore Tyr530 phosphorylation, while PP2A/PP1 dephosphorylate the activation loop for signal termination. In platelets, shear-induced clustering at podosome-like adhesions generates local p-Tyr419 gradients that license αIIbβ3 outside-in signaling for clot retraction, while fibroblasts exploit Src for durotaxis through myosin-IIA/Y1183 feedback with tension sensors.

使用情報

Application

WB, FCM

Dilution

WB	FCM
1:5000	1:100

Reactivity

Mouse, Rat, Human

Source

Rabbit Monoclonal Antibody

MW

60 kDa

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

プロトコール

References

https://pubmed.ncbi.nlm.nih.gov/9988270/
https://pubmed.ncbi.nlm.nih.gov/23923048/

Application Data

WB

Validated by Selleck

Lane 1: A431, Lane 2: A431 (Pervanadate, 50 mM, 5 min), Lane 3: NIH/3T3, Lane 4: NIH/3T3 (Pervanadate, 50 mM, 5 min)