Src Antibody [L10F23] Datasheet

Biological Description

Specificity	Src Antibody [L10F23] detects endogenous levels of total Src protein.
Background	Src belongs to the Src family of non-receptor tyrosine kinases, which regulate cell growth, adhesion, and differentiation through diverse signalling cascades. Src organizes an SH3 domain clamping a polyproline linker to an SH2 domain that binds phosphotyrosine alongside a bilobal kinase domain featuring a regulatory activation loop and C-terminal tyrosine tail. Phosphorylation at Tyr416 within the activation loop stabilizes an open conformation where the loop aligns catalytic aspartate and arginine residues for substrate coordination, while dephosphorylation or mutation permits transient active states even in closed conformations stabilized by C-terminal Tyr527 phosphorylation via Csk kinase. Intermolecular autophosphorylation at Tyr416 occurs through dimerization that juxtaposes kinase domains, with Src subsequently phosphorylating substrates like FAK at focal adhesions to activate paxillin and p130Cas for Rac1-mediated lamellipodia extension during migration. Src further engages EGFR and PDGFR through direct transphosphorylation that amplifies MAPK/ERK and PI3K/AKT pathways, while Csk-mediated Tyr527 phosphorylation recruits SH2-domain phosphatases like PTP1B to reset autoinhibition through tail clamping across the SH2 domain. Src coordinates osteoclast bone resorption via αvβ3 integrin signaling and neuronal synaptic plasticity through NMDA receptor modulation, with ubiquitous expression calibrated by membrane localization via myristoylation and palmitoylation.

Specificity

Src Antibody [L10F23] detects endogenous levels of total Src protein.

Background

Src belongs to the Src family of non-receptor tyrosine kinases, which regulate cell growth, adhesion, and differentiation through diverse signalling cascades. Src organizes an SH3 domain clamping a polyproline linker to an SH2 domain that binds phosphotyrosine alongside a bilobal kinase domain featuring a regulatory activation loop and C-terminal tyrosine tail. Phosphorylation at Tyr416 within the activation loop stabilizes an open conformation where the loop aligns catalytic aspartate and arginine residues for substrate coordination, while dephosphorylation or mutation permits transient active states even in closed conformations stabilized by C-terminal Tyr527 phosphorylation via Csk kinase. Intermolecular autophosphorylation at Tyr416 occurs through dimerization that juxtaposes kinase domains, with Src subsequently phosphorylating substrates like FAK at focal adhesions to activate paxillin and p130Cas for Rac1-mediated lamellipodia extension during migration. Src further engages EGFR and PDGFR through direct transphosphorylation that amplifies MAPK/ERK and PI3K/AKT pathways, while Csk-mediated Tyr527 phosphorylation recruits SH2-domain phosphatases like PTP1B to reset autoinhibition through tail clamping across the SH2 domain. Src coordinates osteoclast bone resorption via αvβ3 integrin signaling and neuronal synaptic plasticity through NMDA receptor modulation, with ubiquitous expression calibrated by membrane localization via myristoylation and palmitoylation.

Usage Information

Application

WB, IP

Dilution

WB	IP
1:1000	1:50

Reactivity

Human, Mouse, Rat, Monkey

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

References

https://pubmed.ncbi.nlm.nih.gov/37848415/
https://pubmed.ncbi.nlm.nih.gov/24103328/

Application Data

WB

Validated by Selleck

Lane 1: A431, Lane 2: Hela, Lane 3: Jurkat, Lane 4: RD