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Thomsen-Friedenreich Antigen Antibody (SPM320), Novus Biologicals™

Mouse Monoclonal Antibody

Marca:  Novus Biologicals NBP2-45282-0.1MG

 vedi altre versioni di questo prodotto

Codice prodotto. 18171559

  • 583.00€ / 0.10mg

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Descrizione

Descrizione

Ensure accurate, reproducible results in Immunohistochemistry (Paraffin), Immunofluorescence

Thomsen-Friedenreich Antigen Monoclonal specifically detects Thomsen-Friedenreich Antigen in Human, Mouse, Rat samples. It is validated for Flow Cytometry, Immunohistochemistry, Immunocytochemistry/Immunofluorescence, Immunohistochemistry-Paraffin, Immunofluorescence.
TRUSTED_SUSTAINABILITY
Specifica

Specifica

Thomsen-Friedenreich Antigen
Monoclonal
0.2 mg/mL
Immunohistochemistry-Paraffin 0.5 - 1.0 ug/ml, Immunofluorescence 0.5 - 1.0 ug/ml
Mouse
Protein A or G purified
RUO
Recognizes a disaccharide epitope, Gal1-3GalNAc, of Thomsen-Friedenreich (TF) antigen. It is specific for both anomeric forms of the disaccharide (TF and TF, including related structures on the glycolipid) and shows no cross-reactivity with sialylated glycophorin. The Thomsen-Friedenreich antigen acts as an oncofetal antigen, with low expression in normal adult tissues but increasing to fetal levels of expression in hyperplasia or malignancy. It is considered as a pan-carcinoma marker. This MAb is capable to agglutinate desialylated red blood cells. During metastasis, the ability of malignant cells to form multicellular aggregates via homotypic or heterotypic aggregation and their adhesion to the endothelium are critical. The tumor-associated carbohydrate Thomsen-Friedenreich antigen (Gal-GalNAc) is involved in tumor cell adhesion and tissue invasion. It also causes an immune response, and overexpression of the antigen causes cancer cells to be more sensitive to natural killer cell lysis. The Thomsen-Friedenreich antigen is suppressed in normal healthy cells and represents one of the few chemically well-defined antigens associated with tumor malignancy. The presence of the Thomsen-Friedenreich antigen on the surface of cancer cells may result from a divergence from the normal pathway for O-linked glycosylation in these cells, most likely caused by inappropriate localization of the enzymes involved in synthesis of the disaccharide.
Store at 4C.
IgM κ
Immunohistochemistry (Paraffin), Immunofluorescence
SPM320
Unconjugated
10mM PBS and 0.05% BSA with 0.05% Sodium Azide
Neuraminidase-treated human red blood cells
0.1 mg
Primary
Human, Mouse, Rat
Purified
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