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MAB5208

Sigma-Aldrich

Anti-Amyloid Antibody, β 1-16, clone AB10

clone AB10, Chemicon®, from mouse

Sinónimos:

Anti-AAA, Anti-ABPP, Anti-AD1, Anti-APPI, Anti-CTFgamma, Anti-CVAP, Anti-PN-II, Anti-PN2, Anti-alpha-sAPP, Anti-preA4

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

mouse

Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

AB10, monoclonal

species reactivity

human, monkey, bovine

manufacturer/tradename

Chemicon®

technique(s)

ELISA: suitable
immunocytochemistry: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable

isotype

IgG1

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... APP(351)

Specificity

Amyloid-beta 1-16.

Immunogen

Amyloid-beta 1-16 conjugated to KLH

Application

Anti-Amyloid Antibody, β 1-16, clone AB10 detects level of Amyloid & has been published & validated for use in ELISA, IP, WB, IC, IH.
Research Category
Neuroscience
Research Sub Category
Neurodegenerative Diseases
Western blot: 1-5 µg/mL
Immunohistochemistry: 5-10 µg/mL
Immunocytochemistry: 5-10 µg/mL
ELISA: 0.2-1.0 µg/mL
Immunoprecipitation

Optimal working dilutions must be determined by end user.

Physical form

Format: Purified
Purified immunoglobulin. Liquid in TRIS-buffered saline containing 1 mg/mL bovine serum albumin and 0.01% sodium azide.

Storage and Stability

Maintain frozen at -20°C in undiluted aliquots for up to 12 months after date of receipt. Avoid repeated freeze/thaw cycles.

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Legal Information

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Huey-Jen Tsay et al.
International journal of molecular sciences, 22(19) (2021-10-14)
Alzheimer's disease (AD) is characterized by the deposition of β-amyloid peptide (Aβ). There are currently no drugs that can successfully treat this disease. This study first explored the anti-inflammatory activity of seven components isolated from Antrodia cinnamonmea in BV2 cells
Amanda B Chai et al.
International journal of molecular sciences, 22(1) (2021-01-02)
Defective clearance mechanisms lead to the accumulation of amyloid-beta (Aβ) peptides in the Alzheimer's brain. Though predominantly generated in neurons, little is known about how these hydrophobic, aggregation-prone, and tightly membrane-associated peptides exit into the extracellular space where they deposit
Tsai-Teng Tzeng et al.
International journal of molecular sciences, 19(2) (2018-02-22)
Hericium erinaceus was used in traditional Chinese medicine for physiologically beneficial medicines. Recently, it has become a candidate in causing positive brain health-related activities. We previously reported that Hericium erinaceus mycelium ameliorates Alzheimer's disease (AD)-related pathologies. To reveal the role
Yung-Cheng Huang et al.
PloS one, 17(1), e0260966-e0260966 (2022-01-25)
Diabetes is a risk factor for Alzheimer's disease (AD), a chronic neurodegenerative disease. We and others have shown prediabetes, including hyperglycemia and obesity induced by high fat and high sucrose diets, is associated with exacerbated amyloid beta (Aβ) accumulation and

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