Datasheet

生物学的記述

Specificity	Phospho-Src Family (Tyr416) Antibody [D13C8] detects endogenous levels of total Src protein only when it is phosphorylated at Tyr416.
Background	Phospho-Src Family (Tyr416) designates the activated state of Src family kinases (SFKs), including Src, Lyn, Fyn, Yes, Lck, Blk, and Hck, non-receptor tyrosine kinases that regulate cell growth, differentiation, survival, and signal transduction from cell surface receptors. SFKs share a conserved architecture with an N-terminal myristoylation site for membrane anchoring, a unique domain, SH3 and SH2 domains for protein and phosphotyrosine interactions, and a C-terminal kinase (SH1) domain containing the activation loop with Tyr416 (Tyr419 in human Src). Phosphorylation at Tyr416, typically through intermolecular autophosphorylation, stabilizes the activation loop in an open, catalytically active conformation, boosting kinase activity by up to 20-fold and driving downstream substrate phosphorylation. This activating phosphorylation is counterbalanced by inhibitory phosphorylation at the C-terminal Tyr530 (Tyr527 in chicken), which promotes intramolecular SH2 binding and an inactive kinase state; dephosphorylation of Tyr530 and phosphorylation of Tyr416 together switch SFKs to their active form. In this state, phospho-Src Family (Tyr416) kinases mediate diverse cellular processes, including proliferation, cytoskeletal rearrangement for migration and adhesion, immune signaling (such as T-cell activation via Lck), and apoptosis regulation, while persistent activation through dysregulation contributes to cancer progression and sustained oncogenic signaling.

Specificity

Phospho-Src Family (Tyr416) Antibody [D13C8] detects endogenous levels of total Src protein only when it is phosphorylated at Tyr416.

Background

Phospho-Src Family (Tyr416) designates the activated state of Src family kinases (SFKs), including Src, Lyn, Fyn, Yes, Lck, Blk, and Hck, non-receptor tyrosine kinases that regulate cell growth, differentiation, survival, and signal transduction from cell surface receptors. SFKs share a conserved architecture with an N-terminal myristoylation site for membrane anchoring, a unique domain, SH3 and SH2 domains for protein and phosphotyrosine interactions, and a C-terminal kinase (SH1) domain containing the activation loop with Tyr416 (Tyr419 in human Src). Phosphorylation at Tyr416, typically through intermolecular autophosphorylation, stabilizes the activation loop in an open, catalytically active conformation, boosting kinase activity by up to 20-fold and driving downstream substrate phosphorylation. This activating phosphorylation is counterbalanced by inhibitory phosphorylation at the C-terminal Tyr530 (Tyr527 in chicken), which promotes intramolecular SH2 binding and an inactive kinase state; dephosphorylation of Tyr530 and phosphorylation of Tyr416 together switch SFKs to their active form. In this state, phospho-Src Family (Tyr416) kinases mediate diverse cellular processes, including proliferation, cytoskeletal rearrangement for migration and adhesion, immune signaling (such as T-cell activation via Lck), and apoptosis regulation, while persistent activation through dysregulation contributes to cancer progression and sustained oncogenic signaling.

使用情報

Application

WB, IP

Dilution

WB	IP
1:1000	1:100

Reactivity

Human, Mouse, Rat

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/31331936/
https://pubmed.ncbi.nlm.nih.gov/27387461/

Application Data

WB

Validated by Selleck

Lane 1: C6, Lane 2: C6 (Pervanadate, 0.5 mM, 37℃, 40 min)