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Merck
CN

MABC200

Anti-APC Antibody, clone CC-1

clone CC-1, from mouse

Synonym(s):

Adenomatous polyposis coli protein, APC, Deleted in polyposis 2.5

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About This Item

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

Anti-APC Antibody, clone CC-1, clone CC-1, from mouse

biological source

mouse

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

CC-1, monoclonal

species reactivity

human

technique(s)

immunohistochemistry: suitable

isotype

IgG2bκ

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Quality Level

Gene Information

human ... APC(324)

Analysis Note

Immunohistochemistry Analysis: A 1:5 dilution from a representative lot detected APC in human colorectal cancer tissue, human smooth muscle tissue, and human colon tissue.

Application

Anti-APC Antibody, clone CC-1 detects levels of APC proteins & has been published & validated for use in IHC.
Immunohistochemistry Analysis: A representative lot from an independent laboratory detected APC in human brain tissue containing multiple schlerosis lesions (Saikali, P. et al. (2007). J Neurosci. 27(5):1220-1228.).

Immunohistochemistry Analysis: A representative lot from an independent laboratory detected APC in rat spinal cord injury tissue (McTique, D. M., et al. (2001). J Neurosci. 21(10):3392-3400.).

General description

311 kDa calculated
Adenomatous polyposis coli protein (APC) is a ubiquitous multidomain protein that has a well documented role as a tumor suppressor. The mechanism of APC-mediated tumor suppression is still an area of active investigation; however, several studies suggest that APC is a negative regulator of the Wnt signaling pathway as it downregulates β-catenin via interactions with Axin/GSK3-β complex, thereby preventing transcription of genes such as MYC that contribute to cell proliferation. Defective APC proteins contribute to the initiation and proliferation of various types of cancers, including familial adenomatous polyposis. However, other studies have shown that APC interacts with a range of other proteins such as the EB1 microtubule-binding proteins, to regulate other processes such as cell migration.

Immunogen

Recombinant protein corresponding to human APC.

Physical form

Format: Purified

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Storage Class

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Emily G Baxi et al.
Glia, 62(9), 1513-1529 (2014-05-28)
Nerve conduction within the mammalian central nervous system is made efficient by oligodendrocyte-derived myelin. Historically, thyroid hormones have a well described role in regulating oligodendrocyte differentiation and myelination during development; however, it remains unclear which thyroid hormone receptors are required
Jasmin Steudler et al.
Glia, 70(11), 2045-2061 (2022-06-29)
Oligodendrocytes (ODCs) are myelinating cells of the central nervous system (CNS) supporting neuronal survival. Oxidants and mitochondrial dysfunction have been suggested as the main causes of ODC damage during neuroinflammation as observed in multiple sclerosis (MS). Nonetheless, the dynamics of
Maria Traka et al.
Brain : a journal of neurology, 133(10), 3017-3029 (2010-09-21)
Adult-onset demyelinating disorders of the central nervous system represent the most common neurological abnormalities in young adults. Nevertheless, our understanding of disease pathogenesis and recovery in demyelinating disorders remains incomplete. To facilitate investigation into these processes, we have developed a
Bastian G Brinkmann et al.
Neuron, 59(4), 581-595 (2008-09-02)
Understanding the control of myelin formation by oligodendrocytes is essential for treating demyelinating diseases. Neuregulin-1 (NRG1) type III, an EGF-like growth factor, is essential for myelination in the PNS. It is thus thought that NRG1/ErbB signaling also regulates CNS myelination
Qi-Yan Cai et al.
Anatomical record (Hoboken, N.J. : 2007), 292(4), 498-512 (2009-01-15)
The tumor suppressor phosphatase and tensin homologue (PTEN) is a protein and lipid phosphatase. PTEN mutations have been associated with a large number of human cancers. To understand the physiological role of PTEN in the brain and its relationship to

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