Src Antibody [M13K12] | Primary Antibodies

Application: Reactivity: Avian

Lane 1: DF-1

Usage Information

Dilution

Application
WB, IP, IF

Reactivity
Avian

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
60 kDa

Positive Control	CEF cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
Src Antibody [M13K12] detects endogenous levels of total Src protein.

Clone
M13K12

Synonym(s)
Proto-oncogene tyrosine-protein kinase Src; Proto-oncogene c-Src; pp60c-src (p60-Src); SRC; SRC1

Background
c-Src, the prototypical proto-oncogenic non-receptor tyrosine kinase and cellular counterpart to v-Src from Rous sarcoma virus, is the founding member of the Src family kinases (SFKs) that orchestrates cell proliferation, survival, migration, adhesion, and cytoskeletal remodeling in multicellular organisms. c-Src contains an N-terminal myristoylated SH4 domain for plasma membrane localization, a unique domain allowing SFK-specific interactions, an SH3 domain that binds proline-rich PxxP motifs, an SH2 domain recognizing phosphotyrosine (pTyr) residues, a catalytic SH1 kinase domain with an ATP-binding site and an activation loop containing the Tyr419 autophosphorylation site, and a C-terminal regulatory tail with the inhibitory Tyr527. c-Src integrates signals from integrins, receptor tyrosine kinases (RTKs), and G-protein-coupled receptors (GPCRs), phosphorylating over 100 substrates in pathways such as FAK-Src-p130Cas for adhesion turnover, Ras/ERK/PI3K for cell growth and survival, and cortactin/FAK for invadopodia formation in metastasis. Its autoinhibition is enforced by CSK-catalyzed phosphorylation of Tyr527, which binds the SH2 domain, while the SH3 domain grips the SH2-kinase linker to block substrate access, maintaining c-Src in a compact, inactive conformation. Activation requires precise reversal of these interactions via dephosphorylation by PTP1B or CD45, displacement of Csk-binding protein, or clustering-induced autophosphorylation at Tyr419, resulting in up to a 1000-fold increase in kinase activity. Dysregulation of c-Src, through C-terminal tail truncation (as in v-Src), CSK suppression, or overexpression, is observed in human cancers (including colon, breast, prostate, and pancreatic cancers).

Background

c-Src, the prototypical proto-oncogenic non-receptor tyrosine kinase and cellular counterpart to v-Src from Rous sarcoma virus, is the founding member of the Src family kinases (SFKs) that orchestrates cell proliferation, survival, migration, adhesion, and cytoskeletal remodeling in multicellular organisms. c-Src contains an N-terminal myristoylated SH4 domain for plasma membrane localization, a unique domain allowing SFK-specific interactions, an SH3 domain that binds proline-rich PxxP motifs, an SH2 domain recognizing phosphotyrosine (pTyr) residues, a catalytic SH1 kinase domain with an ATP-binding site and an activation loop containing the Tyr419 autophosphorylation site, and a C-terminal regulatory tail with the inhibitory Tyr527. c-Src integrates signals from integrins, receptor tyrosine kinases (RTKs), and G-protein-coupled receptors (GPCRs), phosphorylating over 100 substrates in pathways such as FAK-Src-p130Cas for adhesion turnover, Ras/ERK/PI3K for cell growth and survival, and cortactin/FAK for invadopodia formation in metastasis. Its autoinhibition is enforced by CSK-catalyzed phosphorylation of Tyr527, which binds the SH2 domain, while the SH3 domain grips the SH2-kinase linker to block substrate access, maintaining c-Src in a compact, inactive conformation. Activation requires precise reversal of these interactions via dephosphorylation by PTP1B or CD45, displacement of Csk-binding protein, or clustering-induced autophosphorylation at Tyr419, resulting in up to a 1000-fold increase in kinase activity. Dysregulation of c-Src, through C-terminal tail truncation (as in v-Src), CSK suppression, or overexpression, is observed in human cancers (including colon, breast, prostate, and pancreatic cancers).

References
https://pubmed.ncbi.nlm.nih.gov/36936693/ https://pubmed.ncbi.nlm.nih.gov/9024657/

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%