Biosensis Neurological Disease Research
New Antibodies for Neurological Disease research: Presenilins, Nicastrin, DJ-1 & beta-Synuclein proteins - a little nip, a little tuck and a whole lot of research lies ahead!
 

Dear Doctor    

Welcome to our August edition of e-antibody solutions. Biosensis is a leading supplier of top quality products for your Neuroscience research. In this newsletter Biosensis is pleased to introduce you to some of our new, largely published antibodies for neurological disease research.    

 

To learn more about our products visit us at www.biosensis.com

Presenilin
Presenilin proteins play a critical role in both health and potentially in disease as well. As part of the catalytic engine of gamma secretase, and critical for the proper functioning of various signaling pathways from the developmental Notch receptor signaling to synaptic function and LTP, research into Presenilin 1 and Presenilin 2 is at the cutting edge of neuroscience research. Biosensis is pleased to introduce three new purified and published rabbit polyclonal antibodies for Presenilin research.


Description  
Catalog No 
Price (USD) 
Rabbit polyclonal antibody to Presenilin 1 (1-20): IgG R-1605-500 $287.00 
Rabbit polyclonal antibody to Presenilin 1 loop region: IgG R-1680-500 $287.00 
Rabbit polyclonal antibody to Presenilin 2 loop region: IgG R-1681-500 $287.00 
 
R-1605-500 Image: Western Immunoblotting of human and mouse Presenilin 1 protein in mouse cell line extracts and mouse and human brain. Membrane protein load 20μg. Crude anti-PS1 N-terminal (NT) used at 1:2000. Catalog No: R-1605-500
            
References:  
1. M.X. Silveyra et al (2008) Presenilin-1 interacts with acetylcholinesterase and alters its enzymatic activity and glycosylation. Mol. Cell Biol. 210, 788-792.

2. J.G. Culvenor et al (2004) Characterization of Presenilin complexes from mouse and human brain using Blue Native gel
electrophoresis reveals high expression in embryonic brain and minimal change in complex mobility with pathogenic presenilin mutations. Eur. J. Biochem. 271, 375-385.

3. N.T. Ilaya et al (2004) Nicastrin expression in mouse peripheral tissues is not co-ordinated with Presenilin and is high in muscle. J. Neurochem. 91, 230-237.

4. D. Beher et al (2003) In vitro Characterization of the Presenilin-dependent gamma-secretase complex using a novel affinity ligand. Biochem. 42, 8133-8142.

5. G. Evin et al (2002) Alternative transcripts of Presenilin-1 associated with Frontotemporal  Dementia. NeuroReport 13, 917-921.

6. G. Evin et at (2001) Aspartyl protease inhibitor pepstatin binds to the presenilins of Alzheimer's disease. Biochem. 40, 8359-8368.

These new antibodies complement our already existing line of Presenilin antibodies and should allow researchers an even wider choice for their single and double labeling research efforts.  
 
Nicastrin 
Nicastrin is also a component of gamma secretase and appears to be important not only for the maintenance of gamma secretase but also acts as its receptor for substrates and is critical for proper substrate binding and recruitment. Biosensis is pleased to introduce three new published and purified rabbit polyclonal antibodies for your Nicastrin research. An N-terminal specific (Catalog number R-1686-500), a C-terminal specific (Catalog number R-1684-500) and a total protein (Catalog number R-1685-500) purified rabbit polyclonal antibody for Nicastrin. The antibodies have been successfully tested in western blot and immunoprecipitation on human and rodent samples and should provide researchers with very useful antibody reagents for continuing research into the expression and function of Nicastrin.


 Description
Catalog No 
Price (USD)  
Rabbit polyclonal antibody to Nicastrin, C-terminal domain:
IgG
 R-1684-500  $287.00
Rabbit polyclonal antibody to Nicastrin, central region: IgG R-1685-500  $287.00
Rabbit polyclonal antibody to Nicastrin, N-terminal domain:
IgG
 R-1686-500  $287.00
  

R-1684-500 Image: Western Immunoblotting of mouse and human Nicastrin protein in tissues and a human cell line (SHSY5Y). Membrane proteins were prepared and loaded as 20 μg protein per lane. Catalog No: R-1684-500

References:
1. J.G. Culvenor et al (2004) Characterization of Presenilin complexes from mouse and human brain using Blue Native gel electrophoresis reveals high expression in embryonic brain and minimal change in complex mobility with pathogenic Presenilin mutations. Eur. J. Biochem. 271, 375-385.  

2. N.T. Ilaya et al (2004) Nicastrin expression in mouse peripheral tissues is not co-ordinated with Presenilin and is high in muscle. J. Neurochem. 91, 230-237.

3. D. Beher et al (2003) In vitro Characterization of the Presenilin-dependent gamma-secretase complex using a novel affinity ligand. Biochem. 42, 8133-8142
     
Beta-synuclein

Beta-synuclein is a protein encoded by SNCB gene and is highly homologous to alpha synuclein. However it is not found in Lewy bodies as alpha synuclein, but it is found in neurofibrillary tangles in patients with Alzheimer's disease. Beta synuclein is enriched in presynaptic terminals and appears be able to block alpha synuclein aggregation and may act as a protective chaperone in this way. Beta synuclein also protects neurons from staurosporine and 6-hydroxy-dopamine induced apoptosis and thus the protein is thought to have anti-apoptotic activity. As a partner for alpha synuclein research, Biosensis is pleased to offer a new purified and published polyclonal antibody to beta synuclein protein. Our catalog number R-1683-500 is made to the C terminal domain (aa99-113) of human beta synuclein and has been successfully tested in western blots and immunohistochemistry. The antibody is highly specific to beta synuclein and does not cross with alpha synuclein in western blots or in immunohistochemistry on Lewy bodies or normal tissue. 

 

 

Description
Catalog No
Price (USD)
Rabbit antibody to beta synuclein (C-terminal domain): IgG
$287.00

 

This new antibody complements our existing line of Beta synuclein antibodies and hopefully provides researchers with even more choices for their beta synuclein research in both health and pathological conditions.

 

R-1683-500

Image: Western Immunoblotting of human β-synuclein protein in human brain homogenate, 10 μg protein per lane. Crude anti-beta-synuclein ab (Catalog Number R-1683-100) used at 1:1000. Peptide absorption reduced antibody reactivity for expected beta-synuclein band of 17 kDa.    

 

References:

1. K.K. Ia et al (2011) Defining the substrate specificity determinants recognized by the active site of C-Terminal Src Kinase-Homologous Kinase (CHK) and identification of β-Synuclein as a potential CHK physiological substrate. Biochemistry, 50, 6667-6677.  

 

2. S. George et al (2010) α-Synuclein transgenic mice reveal compensatory increases in Parkinson's Disease-associated proteins DJ-1 and Parkin and have enhanced α-synuclein and PINK1 levels after rotenone treatment. J. Mol. Neurosci. 42, 243-254.

 

3. M.C. Quilty et al (2003) Localization of alpha-, beta-, and gamma-synuclein during neuronal development and alterations associated with the neuronal response to axonal trauma. Exp Neurol 182, 195-207.

4. Q.X. Li et al (2002) Platelet alpha- and gamma-synucleins in Parkinson's disease and normal control subjects. Journal of Alzheimer's Disease 4, 309-315.  

 

5. J.G. Culvenor et al (2002) Oligodendrocytes from neural stem cells express alpha-synuclein: Increased numbers from Presenilin 1 deficient mice. NeuroReport 13, 1305-1308.

6. J.G. Culvenor et al (1999) Non-Abeta component of Alzheimer's disease amyloid (NAC) revisited: NAC and alpha-synuclein are not associated with Abeta amyloid. Am. J. Path. 155, 1173-1181.  

 

DJ-1/PARK7 

Finally, DJ-1/PARK7 is a multi-functional peptidase that appears to operate as a transcription factor and molecular chaperone helping cells, particularly neurons, to deal with oxidative stress and cell death survivability. DJ-1 has been shown to interact with important mitochondrial uncoupling proteins, be a scavenger for hydrogen peroxide, positively augment the expression of NrF2 the primary transcription factor for the oxidative stress response as well as the co-transcription factor p65/RELA, help modulate astrocyte immune responses and even interact with alpha synuclein and prevent its aggregation. Thus with all the known functions and interactions for DJ-1/PARK7 quality reagents are a must and Biosensis is pleased to introduce a new purified anti-DJ-1/PARK7 rabbit polyclonal antibody, catalog number R-1682-500. Our antibody has been successfully used in western blot and immunohistochemistry on mouse and human samples and is made to an N-terminal domain peptide sequence that is specific to DJ-1/PARK7 protein by western blot. Our new antibody should enable researchers to continue to examine biological roles of DJ-1/PARK7 in both normal and pathological conditions. 

 

 

Description Catalog No Price (USD) 
Rabbit polyclonal antibody to DJ-1/PARK7: IgG 
$287.00 

     

Image: Western blotting for DJ-1 in extracts of primary cultured neurons. Samples resolved on 10% Tris-tricine gels and transferred to nitrocellulose membrane for blotting. Catalog No: R-1682-500.        

 

 

 

When you want the best reagents, trust Biosensis

The staff at Biosensis have many years of combined experience in manufacturing and working with antibodies and have published over 340 peer reviewed research publications in the field of neuroscience. We guarantee to provide you with the antibody information you need to get your research published.

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Each month, our Biospeak e-bulletins highlight recent progress in important research areas such as:
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  2. LRRK
  3. Insulin-like growth receptors
  4. Semaphorins
  5. Trk receptors
  6. Amyotrophic Lateral Sclerosis
  7. Motor Neuron Disease
  8. Neurotrophins 
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If you have a query on any of our products, please contact us at biospeak@biosensis.com.
 
Sincerely,
Tina  
Contact Information
Email:  tina@biosensis.com
Phone: + 61 8 8352 7711
Web:  www.biosensis.com