Glial fibrillary acidic protein (GFAP) is an intermediate filament protein of 52kD reported to be expressed in glial cells, for example, astrocytes and ependymal cells. In the peripheral nervous system, GFAP has been reported to be expressed in Schwann cells, enteric glial cells and satellite cells of human sensory ganglia and in neoplastic tissues GFAP has been reported to be expressed in astrocytomas and ependymomas. When using GFAP-GA5 the heat induced epitope retrieval (HIER) technique may improve staining in some cases.
Antibody Isotype:
IgG1
Monosan Range:
MONXtra
Clone:
GA5
Concentration:
Greater than or equal to 70 mg/L
Storage buffer:
Tissue culture supernatant with sodium azide
Storage:
2-8°C
References 1:
Louis ED et al. Brain 7. 2007; 130:3297-3307
References 2:
Barresi V et al. Archives of Pathology and Laboratory 8. Medicine 2006; 130:1208-1211
References 3:
Biondo B et al. Acta Neuropathologica 2004; 108:309-318
The HMB45 antigen has also been identified in retinal pigment epithelium (RPE) but is reported to be reactive only with the transient prenatal and infantile RPE. No reaction is reported to be observed with intradermal nevi and normal adult melanocytes and non-melanocytic cells. Tumor cells of epithelial, lymphoid, glial and mesenchymal origin are reported to be negative. This clone is well described in the literature. It is indicated to label an intracytoplasmic antigen in the majority of melanomas and other tumors demonstrating melanoma/melanocytic differentiation. The clone is also reported to react with junctional and blue nevus cells. (Bacchi CE et al., A Review. Applied Immunohistochemistry. 4:73-85 (1996)).
Antibody Isotype:
IgG1, kappa
Monosan Range:
MONXtra
Clone:
HMB45
Concentration:
Greater than or equal to 10.8 mg/L
Storage buffer:
Tissue culture supernatant with Sodium azide
Storage:
2-8°C
References 1:
Swetter SM et al. Archives of Dermatology. 2004; 140:99-103
References 2:
Kapur RP et al. The Journal of Histochemistry and Cytochemistry. 1992; 40(2):207-212
References 3:
Gown AM et al. American Journal of Pathology. 1986; 123(2):195-203
Epidermal growth factor receptor (EGFR) is a transmembrane protein receptor of 170 kD with tyrosine kinase activity. Increased levels of EGFR are reported to be linked with malignant transformation of squamous cells eg in squamous cell carcinoma of the lung, head, neck, skin, cervix and esophagus. EGFR may also play a role in the development and progression of hepatocellular carcinomas where recurrence rates are higher in EGFR-positive cases. This correlation has similarly been reported in colorectal cancers where EGFR, produced by tumor cells, plays an important role in the invasiveness and proliferation of colorectal cancers. The majority of published studies of EGFR expression in human breast cancer has similarly shown an association with EGFR expression where it is inversely related to estrogen receptor status.
Antibody Isotype:
IgG2a
Monosan Range:
MONXtra
Clone:
EGFR.113
Concentration:
Greater than or equal to 26 mg/L
Storage buffer:
Tissue culture supernatant with Sodium azide
Storage:
2-8°C
References 1:
Lodge AJ et al. Journal of Clinical Pathology. 2003; 56(4):300304
References 2:
Sriplakich S et al. BJU Int. 1999; 83(4):498503
References 3:
Inoue K et al. Acta Med Okayama 1998; 52(6):305310
References 4:
Tungekar MF and Linehan J. Journal of Clinical Pathology. 1998; 51:583587
Mouse anti-Progesterone Receptor (A/B Forms), clone16 and SAN27
Antibody Type:
Monoclonal
Host Animal:
Mouse
Species Reactivity:
human
Immunogen:
Prokaryotic recombinant protein corresponding to the N-terminal region of the A form of the human progesterone receptor generating clone 16 and a prokaryotic recombinant protein corresponding to the 164 amino acid N-terminal region unique to the B form of the progesterone receptor generating clone SAN27.
The human progesterone receptor (PR) is expressed as two isoforms, PRA (94 kD) and PRB (114 kD), which function as ligand-activated transcription factors. In vitro studies have indicated that PRA and PRB can activate different target genes and that PRA, in some circumstances, may act as a dominant inhibitor of the function of PRB and other steroid hormone receptors. PRA and PRB are both expressed in normal breast. Most endometrial carcinomas, however, are reported to express only one isoform with either PRA or PRB being expressed. The cocktail has been formulated using two clones, clone 16, specific for PRA, and SAN27, specific for PRB.
Terminal deoxynucleotidyl transferase (TdT) is a DNA polymerase of 58 kD located in the cell nucleus which catalyzes the polymerization of deoxynucleotides at the 3' hydroxyl ends of oligo or polydeoxynucleotide initiators and functions without a template. TdT is reported to be expressed in primitive T and B lymphocytes of the normal thymus and bone marrow. The identification of TdT-positive cell populations in primary and secondary lymphoid organs during maturation of the immune system is one area of interest but it is the reported occurrence of high levels of enzyme activity in white blood cells and bone marrow in certain leukemias which is of particular interest.
Antibody Isotype:
IgG2a
Monosan Range:
MONXtra
Clone:
SEN28
Concentration:
Greater than or equal to 30 mg/L
Storage buffer:
Tissue culture supernatant with sodium azide
Storage:
2-8°C
References 1:
Tai YC and Peh SC. FSingapore Medical Journal. 2003; 44(5):250-255
CD33 antigen is reported to appear on myelomonocytic precursor cells after CD34 antigen expression. It then continues to be expressed on both the myeloid and monocyte lineages, although it is reported to be absent on granulocytes. It has been reported that expression of CD33 is restricted to monocytes, premyelocytes, myeloid blasts, some acute undifferentiated leukemias and acute lymphoblastic leukemias.
Antibody Isotype:
IgG2b
Monosan Range:
MONXtra
Clone:
PWS44
Concentration:
Greater than or equal to 417 mg/L
Storage buffer:
Tissue culture supernatant with sodium azide
Storage:
2-8°C
References 1:
Bradshaw EM et al. Nature Neuroscience. 2013, 16(7): 848 852
References 2:
Hoyer JD et al. American Journal of Clinical Pathology. 2008; 129(2): 316 323.
ZAP-70 is a member of the syk family of proteins. It is expressed on T cells and NK cells and is required for the T cell receptor activation that triggers an immune response. CLL B cells that express the non-mutated immunoglobulin VH genes express levels of ZAP-70 protein that are comparable to those found in the blood T cells of healthy adults. Leukemic cells that express mutated Ig VH genes generally do not express detectable levels of ZAP-70 protein and this is correlated with the high level expression of CD38.
Antibody Isotype:
IgG2b, kappa
Monosan Range:
MONXtra
Clone:
L453R
Concentration:
Greater than or equal to 449 mg/L
Storage buffer:
PBS with sodium azide
Storage:
2-8°C
References 1:
Orchard J et al. Leukaemia and Lymphoma 2005; 46(12):16891698
References 2:
Wang J et al. Applied Immunohistochemistry and Molecular Morphology 2005; 13(4):323332
References 3:
Mustelin T and Tasken K.Biochemical Journal 2003; 371:1527
References 4:
Van Oers N and Weiss A. Seminars in Immunology 1995; 7:227236
CD31 antigen (PECAM-1) is a single chain transmembrane glycoprotein with a molecular weight of 130 to 140 kD. The CD31 molecule is expressed on the surface of platelets, monocytes, granulocytes, B cells and at the endothelial intracellular junction. The molecule has an extracellular domain that contains six Ig-like homology units of C2 subclass, typical of cell to cell adhesion molecules. This domain mediates endothelial cell to cell adhesion, plays a role in endothelial contact and may serve to stabilize the endothelial cell monolayer. The CD31 molecule also has a cytoplasmic domain with potential sites for phosphorylation after cellular activation. The properties of CD31 antigen suggest that it is involved in interactive events during angiogenesis, thrombosis and wound healing. Angiogenesis is essential for tumor growth and metastases.
Antibody Isotype:
IgG1
Monosan Range:
MONXtra
Clone:
JC70A
Concentration:
Greater than or equal to 31 mg/L
Storage buffer:
Tissue culture supernatant with sodium azide
Storage:
2-8°C
References 1:
DeYoung BR et al. Journal of Clinical Pathology 1995; 22: 215-222
References 2:
Parums DV et al. Journal of Clinical Pathology 1990; 43: 752-757
References 3:
Fox SB et al. Journal of the National Cancer Institute 1997; 89: 1044-1049
References 4:
Engel CJ et al. American Journal of Surgical Pathology 1996; 20: 1260-1265
References 5:
Giatromanolaki A et al. Journal of Pathology 1996; 179: 80-88
CD10 antigen, also called neprilysin, is a 100 kD cell surface metalloendopeptidase which inactivates a variety of biologically active peptides. It was initially identified as the common acute lymphoblastic leukemia antigen (CALLA) and was thought to be tumor-specific. Subsequent studies, however, have shown that CD10 antigen is expressed on the surface of a wide variety of normal and neoplastic cells. In other lymphoid malignancies, CD10 antigen is reported to be expressed on cells of lymphoblastic, Burkitt's and follicular lymphomas. CD10 antigen has been identified on the surface of normal early lymphoid progenitor cells, immature B cells within adult bone marrow and germinal center B cells within lymphoid tissue. It is also expressed in various non-lymphoid cells and tissues, such as breast myoepithelial cells, bile canaliculi, fibroblasts, with especially high expression on the brush border of kidney and gut epithelial cells. (G. McIntosh et al. American Journal of Pathology. 154(1): 77-82 (1999)).
Antibody Isotype:
IgG1
Monosan Range:
MONXtra
Clone:
56C6
Concentration:
n/a
Storage buffer:
Tissue culture supernatant with sodium azide
Storage:
2-8°C
References 1:
Millar EK et al. Journal of Clinical Pathology 1999 52, 849-850
References 2:
McIntosh GG et al. American Journal of Pathology 1999 154(1), 7782
References 3:
Kaufmann O et al. American Journal of Clinical Pathology 1999 111(1), 117-122
References 4:
Endoh Y et al. Human Pathology 1999 30(7), 826-832
References 5:
Chu P and Arber DA. American Journal of Clinical Pathology 2000 113(3), 374382
The CD163 molecule is a type I membrane protein also known as M130 antigen, Ber-Mac3, Ki-M8 or SM4. CD163 protein is restricted in its expression to the monocytic/macrophage lineage. It is reported to be present on all circulating monocytes and most tissue macrophages except those found in the mantle zone and germinal centers of lymphoid follicles, interdigitating reticulum cells and Langerhans cells. In addition, multi-nucleated cells within inflammatory lesions are reported not to express CD163 protein. The protein is upregulated by glucocorticoids and downregulated by the immunosuppressant cyclosporin A and by phorbol esters, while lipopolysaccharide, an inflammatory mediator, has no influence on expression. It has been proposed that a specific release mechanism of soluble CD163 antigen by human monocytes may play an important role in modulating inflammatory processes.
Antibody Isotype:
IgG1
Monosan Range:
MONXtra
Clone:
10D6
Concentration:
Greater than or equal to 49 mg/L
Storage buffer:
Tissue culture supernatant with sodium azide
Storage:
2-8°C
References 1:
Bronkhorst IH et al. Investigative Ophthalmology and Visual Science. 2011; 52(2):643-650
References 2:
Lau SK et al. American Journal of Clinical Pathology. 2004; 122(5):794-801
CD11c is a member of the leukocyte integrin family of adhesion proteins. It is reported to be expressed in normal tissues, mainly on myeloid cells, for example, in bone marrow myelocytes, premyelocytes, metamyelocytes, non-segmented and segmented neutrophils with high levels reported on tissue macrophages and monocytes and with lowest levels in granulocytes. It is also reported to be expressed on NK cells, activated T cells, lymphoid cell lines, including hairy cell leukemias and a proportion of interdigitating dendritic cells.
Antibody Isotype:
IgG2a
Monosan Range:
MONXtra
Clone:
5D11
Concentration:
Greater than or equal to 30 mg/L
Storage buffer:
Tissue culture supernatant with sodium azide
Storage:
2-8°C
References 1:
Barth TFE et al. Journal of Pathology. 2007; 211:305-313
References 2:
Venkatraman L et al. Modern Pathology. 2005; 18: 255A-256A 1183 Supplement 1
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