Home    >   Primary Antibodies

Anti-Src

Rabbit Polyclonal Antibody
Catalog No. S19-63BR




Catalog No. Pack Size Price (USD)
S19-63BR-100 100 ug $325
S19-63BR-BULK BULK Contact Us  


Overview:

Src family belongs to non-receptor tyrosine kinases. Src was originally identified as a transforming protein of the Rous sarcoma virus (RSV) that had enzymatic ability to phosphorylate tyrosine in protein substrates (1). Src is overexpressed and activated in a large number of human malignancies and has been linked to the development of cancer and progression to distant metastases (2). In addition to increasing cell proliferation, a key role of Src in cancer seems to be the ability to promote invasion and motility, functions that might contribute to tumour progression.

References:


1. Collett, M S. et al: Protein kinase activity associated with the avian sarcoma virus src gene product. Proc Natl Acad Sci U S A. 1978 Apr;75(4):2021-4.

2. Jacobs, C. et al: Expression of pp60c-src protein kinase in adult and fetal human tissue: high activities in some sarcomas and mammary carcinomas. Cancer Res. 1983 Apr;43(4):1696-702.


Specificity:

Recognizes the Src protein


Cross Reactivity:

Human, Mouse and Rat


Host / Isotype / Clone#:

Rabbit, IgG


Immunogen:

The antiserum was produced against synthesized non-phosphopeptide derived from human Src around the phosphorylation site of tyrosine 529 (P-Q-YP-Q-P).


Purification:

Affinity chromatography


Stability:

Store at 4oC (add 0.1% NaN3) for several months, and at -20oC for longer periods. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.


Sample Data:

Western Blot analysis of extracts from 293 cells using Anti-Src (Lane 1 and 2) and Anti-phospho-Src (Tyr529) (Lane 3 and 4).



Product Datasheets



 Keller N et al., Studies of the molecular mechanism of caspase-8 activation by solution NMR Cell Death and Differentiation April 2010 10.1038/cdd.2009.155

 Gupta Shalini et al., Kinase-Actuated Immunoaggregation of Peptide-Conjugated Gold Nanoparticles Small June 2010 10.1002/smll.201000099

 Huang Yongqi et al., The Activity and Stability of the Intrinsically Disordered Cip/Kip Protein Family AreRegulated by Non-Receptor Tyrosine Kinases Journal of Molecular Biology January 2015 10.1016/j.jmb.2014.11.011

 Jun Cho Hee et al., EphrinB1 Interacts with CNK1 and Promotes Cell Migration through c-Jun N-terminal Kinase (JNK) Activation Journal of Biological Chemistry May 2014 10.1074/jbc.M114.558809

 Nama Sangkil et al., Novel synthetic derivatives of the natural product berbamine inhibit Jak2/Stat3 signaling and induce apoptosis of human melanoma cells Molecular Oncology October 2012 10.1016/j.molonc.2012.05.002

 E. Salhia Hussam et al., Cardiac troponin I tyrosine 26 phosphorylation decreases myofilament Ca 2+ sensitivity and accelerates deactivation Journal of Molecular and Cellular Cardiology September 2014 10.1016/j.yjmcc.2014.09.013

 Zhou Xi et al., The CHMP4b- and Src-docking sites in the Bro1 domain are autoinhibited in the native state of Alix Biochemical Journal March 2009 10.1042/BJ20081388

 Ghadiali JE et al., Protein Kinase-Actuated Resonance Energy Transfer in Quantum Dot-Peptide Conjugates ACS Nano July 2010 10.1021/nn101293s

 Beebe Kristin et al., Post-translational modification and conformational state of Heat Shock Protein 90 differentially affect binding of chemically diverse small molecule inhibitors Oncotarget July 2013 10.18632/oncotarget.1099

 Y Jin et al., Src drives the Warburg effect and therapy resistance by inactivating pyruvate dehydrogenase through tyrosine-289 phosphorylation. Oncotarget May 2016 10.18632/oncotarget.7159

 Figel Dwyer Sheila et al., Identification of Novel Focal Adhesion Kinase Substrates: Role for FAK in NFKB Signaling International Journal of Biological Sciences February 2015 10.7150/ijbs.10273

 Kosten Jonas et al., Efficient Modification of Alpha-Synuclein Serine 129 by Protein Kinase CK1 Requires Phosphorylation of Tyrosine 125 as a Priming Event ACS Chemical Neuroscience October 2014 10.1021/cn5002254

 Martic? Sanela et al., Electrochemical investigations into Tau protein phosphorylations Analyst March 2012 10.1039/c2an35097a

 Martica Sanela et al., Probing copper/tau protein interactions electrochemically Analytical Biochemistry November 2013 10.1016/j.ab.2013.07.015


RESEARCH AREAS

Angiogenesis, Apoptosis/Autophagy, Cancer, Cytoplasmic Tyrosine Kinases, ERK/MAPK Pathway, Inflammation, Invasion/Metastasis, JAK/STAT Pathway



SIGNALCHEM BIOTECH INC.


About

Terms of Service

Privacy Policy

Get the latest resources, updates and offers in your inbox