Src Antibody [L10F23]

Catalog No.: F4132

Application: Reactivity: Human, Mouse, Rat, Monkey

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

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代表番号: 045-509-1970|電子メール：sales@selleck.co.jp

使用情報

Dilution
WB1:1000 IP1:50

Application
WB, IP

Source
Rabbit Monoclonal Antibody

Reactivity
Human, Mouse, Rat, Monkey

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
60 kDa

Datasheet & SDS

生物学的記述

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

Clone
L10F23

Synonym(s)
Proto-oncogene tyrosine-protein kinase Src; Proto-oncogene c-Src; pp60c-src; SRC

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.

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.

References
[1] Cuesta-Hernández HN, et al. Nat Commun. 2023 Oct 17;14(1):6548. [2] Meng Y, et al. J Mol Biol. 2014 Jan 23;426(2):423-35.

PVDFメンブレン孔径参考表

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%