Microtubule associated protein rich fraction: porcine brain

Microtubule associated protein rich fraction: porcine brain
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Product Uses Include

  • Positive control for the study of microtubule binding proteins
  • Investigation of the the effect of MAPs on microtubule dynamics
  • Substrate for many protein kinases

Material
A microtubule associated protein (MAP) fraction has been isolated from porcine brain by temperature induced tubulin polymerization followed by ionic exchange chromatography over a phosphocellulose matrix and salt elution (1, 2). The MAP fraction protein is supplied as a white lyophilized powder

Purity
Protein purity is determined by scanning densitometry of Coomassie Blue stained protein on a 12% polyacrylamide gel. MAP2 constitutes 70% of the total protein (see Figure 1).

mapfgel

Figure 1: Microtubule associated protein fraction purity determination. A 10 µg sample of MAPF was separated by electrophoresis in a 12% SDS-PAGE system, and stained with Coomassie Blue.

Biological Activity
The biological activity of the MAP fraction is determined by the ability of 0.1 mg/ml MAP fraction to enhance the polymerization rate (Vmax) of purified bovine brain tubulin (Cat. # TL238in vitro. Stringent quality control ensures that the MAP fraction protein will stimulate tubulin polymerization at least five fold when compared to tubulin polymerization without MAP fraction.

mapffig2

Figure 2: Tubulin polymerization in the presence and absence of microtubule associated protein fraction. Tubulin polymerization reactions were carried out as in BK006 with 5% glycerol containing 2 mg/ml of pure bovine brain tubulin (Cat. # TL238) being polymerized in the presence and absence of 0.1 mg/ml MAP fraction protein.

References

  1. Vallee, R. B. 1982. J. Cell Biol. 92, 435-442
  2. Kuznetsov S. A., et al. 1981. FEBS Lett. 135, 241-244

For product Datasheets and MSDSs please click on the PDF links below.   For additional information, click on the FAQs tab above or contact our Technical Support department at tservice@cytoskeleton.com

AuthorTitleJournalYearArticle Link
Ait-Bouziad, Nadine et al.Phosphorylation of the overlooked tyrosine 310 regulates the structure, aggregation, and microtubule- And lipid-binding properties of TauJournal of Biological Chemistry2020ISSN 1083-351X
Liang, Hong et al.The microtubule-associated protein IQ67 DOMAIN5 modulates microtubule dynamics and pavement cell shapePlant Physiology2018ISSN 1532-2548
Zhang, Xiang et al.Palladin is a novel microtubule-associated protein responsible for spindle orientationScientific Reports2017ISSN 2045-2322
Gumy, Laura F. et al.MAP2 Defines a Pre-axonal Filtering Zone to Regulate KIF1- versus KIF5-Dependent Cargo Transport in Sensory NeuronsNeuron2017ISSN 1097-4199
Kesten, Christopher et al.In vitro Microtubule Binding Assay and Dissociation Constant EstimationBio-Protocol2016ISSN 2331--8325
Endler, Anne et al.A Mechanism for Sustained Cellulose Synthesis during Salt StressCell2015ISSN 1097-4172
He, Ze et al.Cytoplasmic retention of a nucleocytoplasmic protein TBC1D3 by microtubule network is required for enhanced EGFR signalingPLoS ONE2014ISSN 1932-6203
Wu, Jianchun et al.Caspase-mediated cleavage of C53/LZAP protein causes abnormal microtubule bundling and rupture of the nuclear envelopeCell Research2013ISSN 1001-0602
Zhu, Mei et al.MISP is a novel Plk1 substrate required for proper spindle orientation and mitotic progressionJournal of Cell Biology2013ISSN 0021-9525
De La Mora-Rey, Teresa et al.The structure of the TOG-like domain of Drosophila melanogaster Mast/OrbitActa Crystallographica Section F: Structural Biology and Crystallization Communications2013ISSN 1744-3091
Mei, Yu et al.The Arabidopsis ARCP protein, CSI1, which is required for microtubule stability, is necessary for root and anther developmentPlant Cell2012ISSN 1532-298X
Tu-Sekine, Becky et al.Dual regulation of diacylglycerol kinase (DGK)-θ: Polybasic proteins promote activation by phospholipids and increase substrate affinityJournal of Biological Chemistry2012ISSN 0021-9258
Azakir, Bilal A. et al.Dysferlin interacts with tubulin and microtubules in mouse skeletal musclePLoS ONE2010ISSN 1932-6203
Smith, Jason G. et al.Neutralizing Antibody Blocks Adenovirus Infection by Arresting Microtubule-Dependent Cytoplasmic TransportJournal of Virology2008ISSN 0022--538X
Sackett, Dan L. et al.Intracellular proadrenomedullin-derived peptides decorate the microtubules and contribute to cytoskeleton functionEndocrinology2008ISSN 0013-7227
Farooqui, Akhlaq A. et al.Inhibitors of brain phospholipase A2 activity: Their neuropharmacological effects and therapeutic importance for the treatment of neurologic disordersPharmacological Reviews2006ISSN 0031-6997
Cho, Hyekyung P. et al.The dual-specificity phosphatase CDC14B bundles and stabilizes microtubulesMolecular and cellular biology2005ISSN 0270--7306
Satish, Latha et al.Interferon-Inducible Protein 9 (CXCL11)-Induced Cell Motility in Keratinocytes Requires Calcium Flux-Dependent Activation of μ-CalpainMolecular and Cellular Biology2005ISSN 0270--7306
Teckchandani, Anjali M. et al.The multidomain protooncogenic protein c-Cbl binds to tubulin and stabilizes microtubulesExperimental cell research2005ISSN 0014--4827
Mamoune, Asmaa et al.DU145 human prostate carcinoma invasiveness is modulated by urokinase receptor (uPAR) downstream of epidermal growth factor receptor (EGFR) signaling.Experimental cell research2004ISSN 0014--4827
Sato, Hiromi et al.The mechanism of action of the Pseudomonas aeruginosa-encoded type III cytotoxin, ExoUEMBO Journal2003ISSN 0261-4189
Nielsen, Finn C. et al.Cytoplasmic trafficking of IGF-II mRNA-binding protein by conserved KH domainsJournal of Cell Science2002ISSN 0021-9533

 

Question 1: What proteins comprise the microtubule-associated protein fraction?

Answer 1:  The MAPF is comprised of a mixture of MAP1, MAP2 and tau proteins.

 

Question 2:  Has the MAPF product been shown to significantly affect tubulin polymerization?

Answer 2:  Yes, the biological activity of the MAPF can be determined by the ability of 0.1 mg/ml MAPF to enhance the polymerization rate (Vmax) of purified porcine brain tubulin in vitro.  Stringent quality control ensures that the MAPF proteins will stimulate tubulin polymerization approximately five fold when compared to tubulin polymerization without MAPF proteins.

 

 

If you have any questions concerning this product, please contact our Technical Service department at tservice@cytoskeleton.com