ARG10351

anti-MUC16 / CA125 antibody [X325]

anti-MUC16 / CA125 antibody [X325] for ELISA,IHC-Formalin-fixed paraffin-embedded sections,Western blot and Human

Cancer antibody; Controls and Markers antibody; Signaling Transduction antibody

Overview

Product Description Mouse Monoclonal antibody [X325] recognizes MUC16 / CA125
Tested Reactivity Hu
Tested Application ELISA, IHC-P, WB
Host Mouse
Clonality Monoclonal
Clone X325
Isotype IgG1
Target Name MUC16 / CA125
Antigen Species Human
Immunogen MUC16 / CA125 antigen purified from human ovarian carcinoma
Conjugation Un-conjugated
Alternate Names Mucin-16; MUC-16; Ovarian carcinoma antigen CA125; CA125; Ovarian cancer-related tumor marker CA125; CA-125

Application Instructions

Application Suggestion
Tested Application Dilution
ELISAAssay-dependent
IHC-PAssay-dependent
WB1:300
Application Note Sandwich ELISA (Capture antibody - Detection antibody):
ARG10156 - ARG10351
ARG10351 - ARG10156
ARG10534 - ARG10351

* The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist.

Properties

Form Liquid
Purification Ion exchange chromatography.
Buffer 10 mM Tris (pH 7.5), 0.15 M NaCl and 0.05% Sodium azide
Preservative 0.05% Sodium azide
Concentration 1.0-2.0 mg/ml
Storage Instruction For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C or below. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use.
Note For laboratory research only, not for drug, diagnostic or other use.

Bioinformation

Database Links

GeneID: 94025 Human MUC16

Swiss-port # Q8WXI7 Human Mucin-16

Gene Symbol MUC16
Gene Full Name mucin 16, cell surface associated
Background CA125 is a tumor antigen widely used in monitoring ovarian cancer. Using a rabbit polyclonal antibody produced to purified CA125 antigen to screen cells from an ovarian cancer cell (OVCAR-3) cDNA library in E. coli, Yin and Lloyd (2001) cloned a long partial cDNA, which they designated MUC16, corresponding to the CA125 antigen. The deduced 1,890-amino acid protein contains characteristic features of a mucin-type molecule, including a high serine, threonine, and proline content in an N-terminal region of 9 partially conserved tandem repeats and a C-terminal region nontandem repeat sequence containing a possible transmembrane region and a potential tyrosine phosphorylation site. MUC16 also has a high leucine content. Northern blot analysis showed that the level of MUC16 mRNA correlated with the expression of CA125 in a panel of cell lines. [Provide by OMIN]
Function Thought to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces. [UniProt]
Research Area Cancer antibody; Controls and Markers antibody; Signaling Transduction antibody
Calculated MW 1519 kDa
PTM Heavily O-glycosylated; expresses both type 1 and type 2 core glycans.
Heavily N-glycosylated; expresses primarily high mannose and complex bisecting type N-linked glycans.
May be phosphorylated. Phosphorylation of the intracellular C-terminal domain may induce proteolytic cleavage and the liberation of the extracellular domain into the extracellular space.
May contain numerous disulfide bridges. Association of several molecules of the secreted form may occur through interchain disulfide bridges providing an extraordinarily large gel-like matrix in the extracellular space or in the lumen of secretory ducts.

Clone References

Molecular organization of the mucins and glycocalyx underlying mucus transport over mucosal surfaces of the airways.

Kesimer M et al.
Mucosal Immunol.,  (2013)

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Coexpression of MUC16 and mesothelin is related to the invasion process in pancreatic ductal adenocarcinoma.

Shimizu A et al.
Cancer Sci.,  (2012)

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The prevalence and nature of glycan alterations on specific proteins in pancreatic cancer patients revealed using antibody-lectin sandwich arrays.

Yue T et al.
Mol Cell Proteomics.,  (2009)

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