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Mouse Anti-APCS Recombinant Antibody (CBYC-P017) (CBMAB-P0066-YC)

Provided herein is a Mouse monoclonal antibody against Human Amyloid P Component, Serum. The antibody can be used for immunoassay techniques, such as WB.
See all APCS antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBYC-P017
Antibody Isotype
IgG2b
Application
WB, IHC-P

Basic Information

Immunogen
Serum amyloid P component Fusion Protein Ag14957 (20-223 aa).
Host Species
Mouse
Specificity
Human
Antibody Isotype
IgG2b
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:500-1:2,000
IHC-P1:20-1:200

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, pH 7.3, 50% glycerol
Preservative
0.02% sodium azide
Concentration
Batch dependent
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at-20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
amyloid P component, serum
Introduction
APCS is a glycoprotein, belonging to the pentraxin family of proteins, which has a characteristic pentameric organization. These family members have considerable sequence homology which is thought to be the result of gene duplication. The binding of the encoded protein to proteins in the pathological amyloid cross-beta fold suggests its possible role as a chaperone. This protein is also thought to control the degradation of chromatin. It has been demonstrated that this protein binds to apoptotic cells at an early stage, which raises the possibility that it is involved in dealing with apoptotic cells in vivo.
Entrez Gene ID
Human325
Mouse29339
UniProt ID
HumanP02743
MouseP23680
Alternative Names
PTX2; SAP; HEL-S-92n; Sap
Function
Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. May also function as a calcium-dependent lectin.
Biological Process
Acute-phase response Source: ProtInc
Amyloid fibril formation Source: Reactome
Chaperone-mediated protein complex assembly Source: ProtInc
Complement activation, classical pathway Source: GO_Central
Innate immune response Source: BHF-UCL
Negative regulation by host of viral exo-alpha-sialidase activity Source: BHF-UCL
Negative regulation by host of viral glycoprotein metabolic process Source: BHF-UCL
Negative regulation by host of viral process Source: GO_Central
Negative regulation of acute inflammatory response Source: BHF-UCL
Negative regulation of exo-alpha-sialidase activity Source: BHF-UCL
Negative regulation of glycoprotein metabolic process Source: BHF-UCL
Negative regulation of monocyte differentiation Source: BHF-UCL
Negative regulation of viral entry into host cell Source: BHF-UCL
Negative regulation of viral process Source: BHF-UCL
Negative regulation of wound healing Source: BHF-UCL
Protein folding Source: ProtInc
Cellular Location
Secreted
PTM
N-glycosylated with a complex biantennary oligosaccharide chain with a sialic acid at the end (disialo-SAP). Monosialo-SAP as well as asioalo-SAP are also detected (PubMed:15174148).

Doni, A., Parente, R., Laface, I., Magrini, E., Cunha, C., Colombo, F. S., ... & Mantovani, A. (2021). Serum amyloid P component is an essential element of resistance against Aspergillus fumigatus. Nature Communications, 12(1), 1-15.

Karhadkar, T. R., Pilling, D., & Gomer, R. H. (2021). Serum Amyloid P inhibits single stranded RNA-induced lung inflammation, lung damage, and cytokine storm in mice. Plos one, 16(1), e0245924.

Ma, J., Liu, Q., & White, J. R. (2021). Novel methods to determine complement activation in human serum induced by the complex of Dezamizumab and serum amyloid P. Journal of Biological Chemistry, 101136.

Larsen, C. P., Sharma, S. G., Caza, T. N., Kenan, D. J., Storey, A. J., Edmondson, R. D., ... & Arthur, J. M. (2020). Serum amyloid P deposition is a sensitive and specific feature of membranous-like glomerulopathy with masked IgG kappa deposits. Kidney international, 97(3), 602-608.

Scarale, M. G., Copetti, M., Garofolo, M., Fontana, A., Salvemini, L., De Cosmo, S., ... & Menzaghi, C. (2020). The synergic association of hs-CRP and serum amyloid P component in predicting all-cause mortality in patients with type 2 diabetes. Diabetes care, 43(5), 1025-1032.

Pilling, D., Cox, N., Thomson, M. A., Karhadkar, T. R., & Gomer, R. H. (2019). Serum Amyloid P and a Dendritic Cell–Specific Intercellular Adhesion Molecule-3–Grabbing Nonintegrin Ligand Inhibit High-Fat Diet–Induced Adipose Tissue and Liver Inflammation and Steatosis in Mice. The American journal of pathology, 189(12), 2400-2413.

Borthwick, N. J., Lane, T., Moyo, N., Crook, A., Shim, J. M., Baines, I., ... & Pepys, M. B. (2018). Randomized phase I trial HIV-CORE 003: Depletion of serum amyloid P component and immunogenicity of DNA vaccination against HIV-1. PloS one, 13(5), e0197299.

Pilling, D., & Gomer, R. H. (2018). The development of serum amyloid P as a possible therapeutic. Frontiers in immunology, 9, 2328.

Nagatoshi, A., Ueda, M., Ueda, A., Tasaki, M., Inoue, Y., Ma, Y., ... & Ando, Y. (2017). Serum amyloid P component: a novel potential player in vessel degeneration in CADASIL. Journal of the neurological sciences, 379, 69-76.

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For research use only. Not intended for any clinical use.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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