Product Focus: Advantages Of Recombinant Beta-Amyloid Peptides

rPeptide provide high quality Peptides, Reagents, Proteins, Antibodies, and more, with a focus on Alzheimer’s and Parkinson’s disease research. Their proprietary platform vector technology enables the recombinant expression of historically difficult peptides/ proteins as soluble peptides/proteins in E. coli.

Accumulation of beta-amyloid as plaques between neurons in the brain is a primary pathological feature of Alzheimer’s disease.  Amyloid is a general term for protein fragments produced normally by the body.  Beta-amyloid is a protein fragment snipped from an amyloid precursor protein (APP). In a healthy brain these protein fragments are broken down and eliminated, but in Alzheimer’s disease the fragments accumulate to form hard, insoluble plaques. These plaques have been correlated with neurotoxicity and the cognitive decline associated with the disease.

Reliable, consistent sources of ‘artificial‘ beta-amyloid are essential to scientists researching the role of this peptide in its various forms, in relation to Alzheimer’s disease.  The most common artificial beta-amyloid is chemically synthesised, but does have disadvantages to the researcher.

When a synthetic beta-amyloid is made, the final full length peptide is in a crude prep mixture. Beta-amyloid is a highly hydrophobic peptide and binds non-specifically to impurities like heavy metals, which are not detectable on HPLC or Mass Spec, but could alter the biological properties of the peptide. In every synthetic preparation this will vary, leading to variability in the biological properties from lot to lot.

rPeptide’s recombinant beta-amyloid peptides are prepared as a very soluble (proprietary) fusion, to significantly reduce the non-specific binding in an impure prep. This soluble fusion is purified to >90% purity and then cleaved to give the final beta-amyloid peptides, which are further purified to >97% purity.  As a result, rPeptide’s recombinant beta-amyloids offer greater batch to batch reproducibility.

Benefits:

• Batch to Batch Consistency: of Physical, Chemical and Biological Properties.  This is THE biggest problem with synthetic beta-amyloid peptides and is not found with recombinant beta-amyloids.
• Purity: Consistently >97%
• Oxidation: No oxidation of the 35Met. A mutant 35Met-Valine, is available to study the effect of oxidation of methionine.
• Chemical Modifications: None (like racemerisation).
• Uniformly full length peptides: No n-1, n-2 subspecies in each lot.
• Uniformly Labelled Peptides: Can economically and uniformly label with 15N, 13C and 15N+13C
• Net Peptide Content: Recombinant Beta-amyloid is sold as “net” peptide content rather than ‘total’ content.  Peptides sold as ‘total’ content often include  20%-40% salt.
• Available in a range of salts allowing you to choose the optimal format for your research (HCl, NaOH, HFIP, TFA)

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Where can I find more information about rPeptide?

Visit the manufacturer page at www.stratech.co.uk/rpeptide, email info@stratech.co.uk or call  +44 (0) 1638 782600.

Stratech Scientific is a distributor of high quality, competitively priced, reliable products for research laboratories throughout the UK and Europe. Please contact us to find out which ranges we can supply in your country.

Product Focus: Amylo-Glo RTD Amyloid Plaque Stain Reagent

Amylo-Glo® RTD™ “Ready to Dilute” Staining reagent is designed to stain amyloid plaques in tissue sections. This novel marker has several advantages over other conventional markers such as Thioflavin S and Congo Red because of its unique chemical and spectral properties. (L. Schmued et al. (2012) J.Neuroscience Methods 209:120– 126).

Using Amylo-Glo® results in a very bright blue UV excitable stain under physiological conditions that will not bleed through when illuminated with other filters. Its brightness makes it ideal for low magnification quantification studies, while its unique excitation/emission profile and mild staining conditions makes it ideal for combination for multiple immunofluorescent labeling studies. Amylo-Glo® RTD™ is compatible with fresh, frozen, and formalin-fixed immunohistochemistry or cytochemistry, and it is particularly good for confocal and multiple labeling because of its high fluorescent intensity and high resistance to photo-bleaching. Moreover because Amylo-Glo® fluoresces in the UV channel, double and triple labeling experiments can be performed very easily (protocol).

Catalogue No.	TR-300-AG
Related products	Amylo-Glo / EB kit catalog number TR-400-AG
Compound Name	Compound: Amylo-Glo; Classification: Styrylbenzene derivative; Appearance: Yellow solution; Molecular Weight: 392; Filter system for visualizing: UV
Purity	Thin layer chromatography using alumina plates and a solvent system of ethanol and water (3:1) revealed the presence of two fluorescent isomers. No amount of starting material was detected.
Biol. activity	Excitation Peak: 334; Emission Peak: 533 nm – unbound, 438 nm when bound to amyloid
Applications	Staining of amyloid plaques in human and animal tissues, see included protocol
Specificity	amyloid plaques both intraneuronal and vascular
Reconstitution	Ready to dilute per protocol; 100X
Storage	The stock solution can be stored for up to 12 months at 4°C protected from light. No preservatives. Use sterile technique when handling and proper laboratory procedures.
Expiry Date	one year from date of purchase
General References	L. Schmued et al. (2012) J.Neuroscience Methods 209:120– 126
Kit Components	5 mL of 100X Amylo-Glo RTD™ (A-G RTD™) solution
Reagent Kit protocol	TR-300-AG Protocol

PDF Data Sheet	Data Sheet
MSDS	MSDS

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Where can I find more information about Biosensis?

Visit the manufacturer page at www.stratech.co.uk/biosensis, email info@stratech.co.uk or call +44 (0) 1638 782600

Stratech Scientific is a distributor of high quality, competitively priced, reliable products for research laboratories throughout the UK and Europe. Please contact us to find out which ranges we can supply in your country.

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Product Focus: Monoclonal Antibody to Amyloid beta peptide (A beta 40/42)

The amyloid beta peptide is derived from the cleavage of the Amyloid precursor protein (APP) and varies in length from 39 to 43 amino acids. However, the form(s) of amyloid-beta peptide (Aβ) associated with the pathology characteristic of Alzheimer’s disease (AD) remains unclear. In particular, the neurotoxicity of intraneuronal Aβ accumulation is an area of considerable research and controversy principally because antibodies thought to be specific for Aβ have been shown to actually detect intraneuronal APP and not Aβ exclusively.

Boisensis MOAB-2 (mouse IgG2b) antibody is a pan-specific, high-titer antibody to Aβ residues 1-4 as demonstrated by biochemical and immunohistochemical analyses (IHC), and is highly specific just to amyloid beta peptide.

Experimental Data
Using IHC on 5xFAD brain tissue, MOAB-2 immunoreactivity co-localized with C-terminal antibodies specific for Aβ40 and Aβ42. MOAB-2 did not co-localize with either N- or C-terminal antibodies to APP. In addition, no MOAB-2-immunreactivity was observed in the brains of 5xFAD/BACE-/- mice, although significant amounts of APP were detected by N- and C-terminal antibodies to APP, as well as by 6E10.

In both 5xFAD and 3xTg mouse brain tissue, MOAB-2 co-localized with cathepsin-D, a marker for acidic organelles, further evidence for intraneuronal Aβ, distinct from Aβ associated with the cell membrane. MOAB-2 demonstrated strong intraneuronal and extra-cellular immunoreactivity in 5xFAD and 3xTg mouse brain tissues.

The MOAB-2 antibody does not detect APP or APP-CTFs in cell culture media/lysates (HEK-APPSwe or HEK APPSwe/BACE1) or in brain homogenates from transgenic mice expressing 5 familial AD (FAD) mutation (5xFAD mice).

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Catalogue No.	M-1586-100
Unit size	100 µg
Antigen	Recombinant human amyloid beta protein 42 (Aβ42): DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA
Antigen Location	Epitope maps to residues 1-4 of human amyloid beta peptide 40/42
Antigen Length	42 amino acids
Antibody Type	Monoclonal
Isotype	IgG2b
Clone	MOAB-2
Other Names	Beta-APP42; Beta-APP40; Beta-amyloid protein 42; Beta-amyloid protein 40; ABPP; APPI; Amyloid beta A4 protein;MOAB2;MOAB-2; Alzheimer’s antibody;AB40;AB42;abeta
Accession	P05067 A4_HUMAN;
Produced in	Mouse
Molecular Weight	With Formic acid extractions and strandard reduced western procedures beta-amyloid peptide migrates between 3-6 kDa (see figure 1).
Purity	This product is a Protein A purified mouse IgGb in 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, 0.01% sodium azide, pH 7.2.
Applications	Western Blotting (WB), Immunohistochemistry (IH), Immunohistochemistry/paraffin embedded IH(P), Immunoprecipitation (IP), Immunofluorescence (IF), ELISA. Antibody has been tested in WB using purified synthetic beta-amyloid preparations and from transgenic mouse brain formic acid extracts (see figure 1). Formic acid extraction/concentration is required for western blot detection from extracts. MOAB-2 antibody is specific for beta-amyloid and does not detect APP. Suggested dilution of 1:2000-1:5,000 for WB, standard ECL detection systems. Tissue samples for the detection of beta-amyloid should be prepared as detailed in K.L. Youmans et al. {Journal of Neuroscience Methods 196 (2011) 51–59} for best results. Detection of beta-amyloid 40/42 in direct westerns can be difficult; Dot-blots of prepared samples are recommended as detailed in Youmans. KL et al 2012. IR or fluorescent detection systems not yet tested, they but are expected to work well with higher primary antibody dilutions because of the increased sensitivity of the detection methods. Suggested dilutions for IHC are 1:50-1:1,000. Fresh frozen, 4% paraformaldehyde fixed frozen, or formalin fixed paraffin embedded tissues are all suitable. Optimal dilutions must be determined by the end user. Antigen retrieval is required in fixed tissues for optimal staining. Antibody was tested on 4% paraformaldehyde/0.1% glutaraldehyde fixed frozen tissue from 3xTg and 5xFAD mice. MOAB-2 antibody detects intraneuronal and extracellular beta-amyloid in IHC and does not detect APP {Youmans KL et al 2012}. The antibody also reacts with archival formalin-fixed, paraffin-embedded tissue samples with antigen Heat Induced Epitope Retrieval (HIER): Recommended Citrate, pH 6.0 buffer for HIER. Signal was weak without antigen retrieval. Immunoreactively was expressed in intraneural-amyloid deposition (plaque) in Alzheimer’s brain. MoAB-2 was found to be extremely clean and with an excellent signal to noise ratio with no neuro-cellular diffusive staining. In addition MOAB-2 demonstrated no significant differences in Aβ detection using paraffin fixed, free-floating sections {Youmans KL et al 2012}. Formic acid (FA) treatment resulted in optimal detection of both intraneuronal and extracellular Aβ compared to without FA (incubated in 88% FA 8 min, Youmans KL et al 2012). Free floating tissue sections were permeabilized in TBS containing 0.25% Triton X-100 (TBSX; 3 × 10 min), blocked with 3% horse serum in TBSX (3 × 10 min) followed by 1% horse serum in TBSX (2 ×10 min) and incubated with appropriate primary antibodies diluted in TBSX containing 1% horse serum overnight. See Youmans KL et al 2012 for full IH(P) protocol and method details. For IF, suggested dilution is 1:100-1:500. The antibody was tested on 4% PFA fixed frozen tissue. Fixed tissues were washed in TBS (3 × 10 min), then incubated in 88% FA (8 min), and then permeabilized in TBSX (3 × 10 min), and blocked in TBSX containing 5% bovine serum albumin (BSA; 1 hr). Sections were subsequently incubated with appropriate primary antibodies diluted in TBSX containing 2% BSA overnight on an oscillatory rotator. Detection was via fluorescently labelled absorbed secondary antibodies {Youmans KL et al 2012}. For IP, the suggested dilution is 1:200 to 1:1,000 for labeled beta-amyloid using Protein A/G conjugated beads as the capture vehicle {Youmans KL et al 2012}. In an ELISA, a dilution of 1:50-1:1000 is suggested. The antibody has been tested in ELISAs on synthetic beta-amyloid and tissue homogenates from beta-amyloid-Tg mice. Biosensis recommends optimal dilutions/concentrations should be determined by the end user for all applications. Dilutions provided are only meant to serve as a basic guide.
Specificity	MOAB-2 detects preparations enriched in U-, O-, F-Aβ42, and U-Aβ40 by dot-blot, and is thus a pan-specific Aβ antibody. However, MOAB-2 is selective for the more neurotoxic Aβ42 compared to Aβ40. Indeed, MOAB-2 demonstrated a titration against antigen concentration, and detects Aβ40 at 2.5 pmol but U-, O- and FAβb42 at antigen concentrations as low as ~ 0.1 pmol {Youmans. KL et al 2012}. MOAB-2 does not detect APP (Amyloid precursor protein).
Species Against	Human
Antibody Against	Human
Cross-reactivity	Human, Rat, other species not yet tested. By Dot blot, MOAB-2 detected rat Aβ40 and human Aβ40, albeit with less affinity than for Aβ42. {Youmans. KL et al 2012}
Form	Lyophilized, from a Protein A purified preparation in 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, 0.01% sodium azide, pH 7.2; contains 0.01% sodium azide as a preservative.
Appearance	dry powder
Reconstitution	Reconstitute in 100 µl of sterile water. Centrifuge to remove any insoluble material. Final buffer is 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, 0.01% sodium azide, pH 7.2.
Storage	After reconstitution keep aliquots at -20° to -70C for a higher stability. At 4°C keep up to one week, insulated, protected from light; use sterile methods and pipettes. Highly purified glycerol (1:1) may be added for an additional stability. Avoid repetitive freeze/thaw cycles. Keep tightly closed when not in use and protected from light.
Expiry Date	12 months after purchase
Specific References	1. K.L. Youmans et al (2012) Intraneuronal Abeta detection in 5xFAD mice by a new Abeta-specific antibody Mol Neurodegener. 2012 Mar 16;7(1):8.
General References	1. K.L. Youmans et al (2011) Amyloid-β42 alters apolipoprotein E solubility in brains of mice with five familial AD mutations J Neurosci Methods. 2011 Mar 15;196(1):51-9.

Youmans, KL et al (2011) J. Neuroscience Methods 196(1):51-59.
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3049315.

Youmans, KL et al (2012) Mol. Neurodegener. 7:8.
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3355009.

PDF Data Sheet	Data Sheet
MSDS	MSDS

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Where can I find more information about Biosensis?

Visit the manufacturer page at www.stratech.co.uk/biosensis, email info@stratech.co.uk or call +44 (0) 1638 782600

Stratech Scientific is a distributor of high quality, competitively priced, reliable products for research laboratories throughout the UK and Europe. Please contact us to find out which ranges we can supply in your country.

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Product Focus: Mouse Monoclonal antibody to Amyloid beta peptide (A beta 40/42)

The amyloid beta peptide is derived from the cleavage of the Amyloid precursor protein (APP) and varies in length from 39 to 43 amino acids. However, the form(s) of amyloid-beta peptide (Aβ) associated with the pathology characteristic of Alzheimer’s disease (AD) remains unclear. In particular, the neurotoxicity of intraneuronal Aβ accumulation is an area of considerable research and controversy principally because antibodies thought to be specific for Aβ have been shown to actually detect intraneuronal APP and not Aβ exclusively.

MOAB-2 (mouse IgG2b) is a pan-specific, high-titer antibody to Aβ residues 1-4 as demonstrated by biochemical and immunohistochemical analyses (IHC), and is highly specific just to amyloid beta peptide.

MOAB-2 did not detect APP or APP-CTFs in cell culture media/lysates (HEK-APPSwe or HEK APPSwe/BACE1) or in brain homogenates from transgenic mice expressing 5 familial AD (FAD) mutation (5xFAD mice).

Using IHC on 5xFAD brain tissue, MOAB-2 immunoreactivity co-localized with C-terminal antibodies specific for Aβ40 and Aβ42. MOAB-2 did not co-localize with either N- or C-terminal antibodies to APP. In addition, no MOAB-2-immunreactivity was observed in the brains of 5xFAD/BACE-/- mice, although significant amounts of APP were detected by N- and C-terminal antibodies to APP, as well as by 6E10.

In both 5xFAD and 3xTg mouse brain tissue, MOAB-2 co-localized with cathepsin-D, a marker for acidic organelles, further evidence for intraneuronal Aβ, distinct from Aβ associated with the cell membrane. MOAB-2 demonstrated strong intraneuronal and extra-cellular immunoreactivity in 5xFAD and 3xTg mouse brain tissues.

Specificity

MOAB-2 detects preparations enriched in U-, O-, F-Aβ42, and U-Aβ40 by dot-blot, and is thus a pan-specific Aβ antibody. However, MOAB-2 is selective for the more neurotoxic Aβ42 compared to Aβ40. Indeed, MOAB-2 demonstrated a titration against antigen concentration, and detects Aβ40 at 2.5 pmol but U-, O- and FAβb42 at antigen concentrations as low as ~ 0.1 pmol {Youmans. KL et al 2012}. MOAB-2 does not detect APP (Amyloid precursor protein).

Applications

Summary: Western Blotting (WB), Immunohistochemistry (IH), Immunohistochemistry/paraffin embedded IH(P), Immunoprecipitation (IP), Immunofluorescence (IF), ELISA. Antibody has been tested in WB using purified synthetic beta-amyloid preparations.

MOAB-2 antibody is specific for beta-amyloid and does not detect APP. Suggested dilution of 1:2000-1:5,000 for WB, standard ECL detection systems. Tissue samples for the detection of beta-amyloid should be prepared as detailed in K.L. Youmans et al. {Journal of Neuroscience Methods 196 (2011) 51–59} for best results. Detection of beta-amyloid 40/42 in direct westerns can be difficult; Dot-blots of prepared samples are recommended as detailed in Youmans. KL et al 2012. IR or fluorescent detection systems not yet tested, they but are expected to work well with higher primary antibody dilutions because of the increased sensitivity of the detection methods. Suggested dilutions for IHC are 1:50-1:1,000. Fresh frozen, 4% paraformaldehyde fixed frozen, or formalin fixed paraffin embedded tissues are all suitable. Optimal dilutions must be determined by the end user. Antigen retrieval is required in fixed tissues for optimal staining. Antibody was tested on 4% paraformaldehyde/0.1% glutaraldehyde fixed frozen tissue from 3xTg and 5xFAD mice. MOAB-2 antibody detects intraneuronal and extracellular beta-amyloid in IHC and does not detect APP {Youmans KL et al 2012}. The antibody also reacts with archival formalin-fixed, paraffin-embedded tissue samples with antigen Heat Induced Epitope Retrieval (HIER): Recommended Citrate, pH 6.0 buffer for HIER. Signal was weak without antigen retrieval. Immunoreactively was expressed in intraneural-amyloid deposition (plaque) in Alzheimer’s brain. MoAB-2 was found to be extremely clean and with an excellent signal to noise ratio with no neuro-cellular diffusive staining. In addition MOAB-2 demonstrated no significant differences in Aβ detection using paraffin fixed, free-floating sections {Youmans KL et al 2012}. Formic acid (FA) treatment resulted in optimal detection of both intraneuronal and extracellular Aβ compared to without FA (incubated in 88% FA 8 min, Youmans KL et al 2012). Free floating tissue sections were permeabilized in TBS containing 0.25% Triton X-100 (TBSX; 3 × 10 min), blocked with 3% horse serum in TBSX (3 × 10 min) followed by 1% horse serum in TBSX (2 ×10 min) and incubated with appropriate primary antibodies diluted in TBSX containing 1% horse serum overnight. See Youmans KL et al 2012 for full IH(P) protocol and method details. For IF, suggested dilution is 1:100-1:500. The antibody was tested on 4% PFA fixed frozen tissue. Fixed tissues were washed in TBS (3 × 10 min), then incubated in 88% FA (8 min), and then permeabilized in TBSX (3 × 10 min), and blocked in TBSX containing 5% bovine serum albumin (BSA; 1 hr). Sections were subsequently incubated with appropriate primary antibodies diluted in TBSX containing 2% BSA overnight on an oscillatory rotator. Detection was via fluorescently labelled absorbed secondary antibodies {Youmans KL et al 2012}. For IP, the suggested dilution is 1:200 to 1:1,000 for labeled beta-amyloid using Protein A/G conjugated beads as the capture vehicle {Youmans KL et al 2012}. In an ELISA, a dilution of 1:50-1:1000 is suggested. The antibody has been tested in ELISAs on synthetic beta-amyloid and tissue homogenates from beta-amyloid-Tg mice. Biosensis recommends optimal dilutions/concentrations should be determined by the end user for all applications. Dilutions provided are only meant to serve as a basic guide.

PDF Data Sheet	– Click to download the Data Sheet
MSDS	– Click to download the MSDS

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Where can I find more information about Biosensis?

Visit the manufacturer page at www.stratech.co.uk/biosensis, email info@stratech.co.uk or call +44 (0) 1638 782600

Stratech Scientific is a distributor of high quality, competitively priced, reliable products for research laboratories throughout the UK and Europe. Please contact us to find out which ranges we can supply in your country.

Product Focus: Mouse Monoclonal antibody to Amyloid beta peptide (A beta 40/42), MOAB-2, purified

The amyloid beta peptide is derived from the cleavage of the Amyloid precursor protein (APP) and varies in length from 39 to 43 amino acids. However, the form(s) of amyloid-beta peptide (Aβ) associated with the pathology characteristic of Alzheimer’s disease (AD) remains unclear. In particular, the neurotoxicity of intraneuronal Aβ accumulation is an area of considerable research and controversy principally because antibodies thought to be specific for Aβ have been shown to actually detect intraneuronal APP and not Aβ exclusively.

MOAB-2 (mouse IgG2b) is a pan-specific, high-titer antibody to Aβ residues 1-4 as demonstrated by biochemical and immunohistochemical analyses (IHC), and is highly specific just to amyloid beta peptide.

MOAB-2 does not detect APP or APP-CTFs in cell culture media/lysates (HEK-APPSwe or HEK APPSwe/BACE1) or in brain homogenates from transgenic mice expressing 5 familial AD (FAD) mutation (5xFAD mice).

Using IHC on 5xFAD brain tissue, MOAB-2 immunoreactivity co-localized with C-terminal antibodies specific for Aβ40 and Aβ42. MOAB-2 did not co-localize with either N- or C-terminal antibodies to APP. In addition, no MOAB-2-immunreactivity was observed in the brains of 5xFAD/BACE-/- mice, although significant amounts of APP were detected by N- and C-terminal antibodies to APP, as well as by 6E10.

In both 5xFAD and 3xTg mouse brain tissue, MOAB-2 co-localized with cathepsin-D, a marker for acidic organelles, further evidence for intraneuronal Aβ, distinct from Aβ associated with the cell membrane. MOAB-2 demonstrated strong intraneuronal and extra-cellular immunoreactivity in 5xFAD and 3xTg mouse brain tissues.

Specificity

MOAB-2 detects preparations enriched in U-, O-, F-Aβ42, and U-Aβ40 by dot-blot, and is thus a pan-specific Aβ antibody. However, MOAB-2 is selective for the more neurotoxic Aβ42 compared to Aβ40. Indeed, MOAB-2 demonstrated a titration against antigen concentration, and detects Aβ40 at 2.5 pmol but U-, O- and FAβb42 at antigen concentrations as low as ~ 0.1 pmol {Youmans. KL et al 2012}. MOAB-2 does not detect APP (Amyloid precursor protein).

Catalogue No.	M-1586-100
Batch No.	See product label
Unit size	100 µg
Antigen	Recombinant human amyloid beta protein 42 (Aβ42): DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA
Antigen Location	Epitope maps to residues 1-4 of human amyloid beta peptide 40/42
Antigen Length	42 amino acids
Antibody Type	Monoclonal
Isotype	IgG2b
Clone	MOAB-2
Other Names	Beta-APP42; Beta-APP40; Beta-amyloid protein 42; Beta-amyloid protein 40; ABPP; APPI; Amyloid beta A4 protein;MOAB2;MOAB-2; Alzheimer’s antibody;AB40;AB42;abeta
Accession	P05067 A4_HUMAN;
Produced in	Mouse
Purity	This product is a Protein A purified mouse IgGb in 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, 0.01% sodium azide, pH 7.2.

Data Sheet
MSDS

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Where can I find more information about Biosensis?

Visit the manufacturer page at www.stratech.co.uk/biosensis, email info@stratech.co.uk or call +44 (0) 1638 782600

Stratech Scientific is a distributor of high quality, competitively priced, reliable products for research laboratories throughout the UK and Europe. Please contact us to find out which ranges we can supply in your country.