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Reacts with human CD59, a 20 kDa glycosyl phosphatidyl-inositol (GPI)-anchored cell surface protein. CD59 regulates complement-mediated cell lysis, and it is involved in lymphocyte signal transduction. This protein is a potent inhibitor of the complement membrane attack complex, whereby it binds complement C8 and/or C9 during the assembly of this complex, thereby inhibiting the incorporation of multiple copies of C9 into the complex, which is necessary for osmolytic pore formation. CD59 is widely distributed on cells in all tissues. It inhibits formation of MAC, thus protecting cells from complement-mediated lysis. The expression of CD59 on erythrocytes is important for their survival. Genetic defects in GPI-anchor attachment, that cause a reduction or loss of CD59 and CD55 on erythrocytes produce the symptoms of the disease paroxysmal hemoglobinuria (PNH). It is useful for study on GPI-anchored proteins, PNH and CD59 functions.

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Recognises a protein of 12 kDa, identified as beta-2 microglobulin. Major histocompatibility complex (MHC) class 1 molecules bind to antigens for presentation on the surface of cells. The proteasome is responsible for producing these antigens from the components of foreign pathogens. MHC class 1 molecules consist of an alpha heavy chain that contains three subdomains (alpha1, alpha2, alpha3) and a non-covalent associating light chain, known as beta-2-Microglobulin. Beta-2-Microglobulin associates with the alpha3 subdomain of the alpha heavy chain and forms an immunoglobulin domain-like structure that mediates proper folding and expression of MHC class 1 molecules. The alpha1 and alpha2 domains of the alpha heavy chain form the peptide antigen-binding cleft. Mutations in the beta-2-Microglobulin gene can enhance the progression of malignant melanoma phenotypes.

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CD45RA is an isoform of the human leukocyte common antigen (CD45). Human CD45 contains three exons which encode peptide segments designated A, B and C, respectively. The differential splicing of the exons generates at least five isoforms, ABC, AB, BC, B and O. This antibody reacts with ABC and BC isoforms. CD45RA is expressed on 40-50% of peripheral CD4+ T-cells, 50% of peripheral CD8+ T-cells, B-cells, and leukemic B-cell lines. T-cells expressing CD45RA are naive or virgin T-cells. T-cells expressing CD45RO are memory T-cells. CD45RA and CD45RO define complementary, predominantly non-overlapping populations of resting peripheral T-cells. This MAb is useful in study on the subpopulation of CD4+ or CD8+ T-cells. It can especially be used to differentiate T-cell lymphomas (CD45RO +ve) from B cell lymphomas (CD45RA +ve).

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CD45RA is an isoform of the human leukocyte common antigen (CD45). Human CD45 contains three exons which encode peptide segments designated A, B and C, respectively. The differential splicing of the exons generates at least five isoforms, ABC, AB, BC, B and O. This antibody reacts with ABC and BC isoforms. CD45RA is expressed on 40-50% of peripheral CD4+ T-cells, 50% of peripheral CD8+ T-cells, B-cells, and leukemic B-cell lines. T-cells expressing CD45RA are naive or virgin T-cells. T-cells expressing CD45RO are memory T-cells. CD45RA and CD45RO define complementary, predominantly non-overlapping populations of resting peripheral T-cells. This MAb is useful in study on the subpopulation of CD4+ or CD8+ T-cells. It can especially be used to differentiate T-cell lymphomas (CD45RO +ve) from B cell lymphomas (CD45RA +ve).

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Cytokeratin 8 (CK8) belongs to the type II (or B or basic) subfamily of high molecular weight cytokeratins and exists in combination with cytokeratin 18 (CK18). CK8 is primarily found in the non-squamous epithelia and is present in majority of adenocarcinomas and ductal carcinomas. It is absent in squamous cell carcinomas. Hepatocellular carcinomas are defined by the use of antibodies that recognize only cytokeratin 8 and 18. CK8 exists on several types of normal and neoplastic epithelia, including many ductal and glandular epithelia such as colon, stomach, small intestine, trachea, and esophagus as well as in transitional epithelium. Anti-CK8 does not react with skeletal muscle or nerve cells. Epithelioid sarcoma, chordoma, and adamantinoma show strong positivity corresponding to that of simple epithelia (with antibodies against CK8, CK18 and CK19). Reportedly, anti-CK8 is useful for the differentiation of lobular ('ring-like, perinuclear') from ductal ('peripheral-predominant') carcinoma of the breast.

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This antibody recognises a 60 kDa protein, identified as the heat shock protein 60. The antibody's epitope is localized between amino acids 383-447 of human HSP60. A wide variety of environmental and pathophysiological stressful conditions trigger the synthesis of a family of proteins known as heat shock proteins (hsp’s), more appropriately called as stress response proteins (srp’s). HSP60 is a potential antigen in a number of autoimmune diseases. In human arthritis and in experimentally induced arthritis in animals, disease development coincides with the development of immune reactivity directed against not only bacterial HSP60, but also against its mammalian homolog. Clone LK1 antibody, unlike LK2 antibody, recognises only the mammalian (not bacterial) HSP60 and is useful in distinguishing HSP60 from mammals and bacteria.

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Thyroglobulin is a 660 kDa dimeric pre-protein with mutiple glycosylation sites, detected at ~300 kDa in western blot. It is produced by and processed within the thyroid gland to produce the hormone thyroxine and triiodothyronine. Prior to forming dimers, thyroglobulin monomers undergo conformational maturation in the endoplasmic reticulation. The vast majority of follicular carcinomas of the thyroid will give positive immunoreactivity for thyroglobulin antibody even though sometimes only focally. Poorly differentiated carcinomas of the thyroid are frequently thyroglobulin antibody negative. Adenocarcinomas of other-than-thyroid origin do not react with this antibody. This antibody is useful in identification of thyroid carcinoma of the papillary and follicular types. Presence of thyroglobulin in metastatic lesions establishes the thyroid origin of tumor. Thyroglobulin antibody, combined with calcitonin antibody, can identify medullary carcinomas of the thyroid. Furthermore, thyroglobulin antibody, combined with TTF1 antibody, can be a reliable marker to differentiate between primary thyroid and lung neoplasms.

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Pax genes contain paired domains with strong homology to genes in Drosophila, which are involved in programming early development. Lesions in the Pax-6 gene account for most cases of aniridia, a congenital malformation of the eye, chiefly characterised by iris hypoplasia, which can cause blindness. Pax-6 is involved in other anterior segment malformations besides aniridia, such as Peters anomaly, a major error in the embryonic development of the eye with corneal clouding with variable iridolenticulocorneal adhesions. The Pax-6 gene encodes a transcriptional regulator that recognises target genes through its paired-type DNA-binding domain. The paired domain is composed of two distinct DNA-binding subdomains, the amino-terminal subdomain and the carboxy-terminal subdomain, which bind respective consensus DNA sequences. The human Pax-6 gene produces two alternatively spliced isoforms that have the distinct structure of the paired domain.

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Recognises a protein of 47-55 kDa, which is identified as FOXP3. Its precise epitope is not known, but it has been mapped to the N-terminal portion of the protein. The FOX family of transcription factors is a large group of proteins that share a common DNA binding domain termed a winged-helix or forkhead domain. During early development, FOXP1 and FOXP2 are expressed abundantly in the lung, with lower levels of expression in neural, intestinal and cardiovascular tissues, where they act as transcription repressors. FOXP1 is widely expressed in adult tissues, while neoplastic cells often exhibit a dramatic change in expression level or localization of FOXP1. Mutations in FOXP3 gene cause IPEX, a fatal, X-linked inherited disorder characterised by immune dysregulation. The FOXP3 protein is essential for normal immune homeostasis. Specifically, FOXP3 represses transcription through a DNA binding forkhead domain, thereby regulating T cell activation.

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This mAb recognises granulocyte-colony stimulating factor (G-CSF) in the cytoplasm of mature granulocytes. It shows no reactivity with any other cell types. Markers of myeloid cells are useful in the identification of different levels of cellular differentiation. It reacts with early precursor and mature forms of myeloid cells. It is useful for the detection of myeloid leukemias and granulocytic sarcomas. It can be used as a marker of granulocytes in normal tissues or inflammatory processes.G-CSF is a pleiotropic cytokine that influences differentiation, proliferation and activation of the neutrophilic granulocyte lineage. The human G-CSF cDNA encodes a 207 amino acid precursor containing a 29 amino acid signal peptide that is proteolytically cleaved to form a 178 amino acid residue mature protein. Two G-CSF's, which are identical except for a three amino acid deletion in the amino-terminus of one form of the protein have been isolated from human cells. Murine and human G-CSF's share 73% sequence identity at the amino acid level.

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At least five CD1 genes (CD1a, b, c, d, and e) are identified. CD1 proteins have been demonstrated to restrict T cell response to non-peptide lipid and glycolipid antigens and play a role in non-classical antigen presentation. CD1a is a non-polymorphic MHC Class 1 related cell surface glycoprotein, expressed in association with Beta-2 microglobulin. CD1a antibody labels Langerhans cell histiocytosis (Histiocytosis X), extranodal histiocytic sarcoma, a subset of T-lymphoblastic lymphoma/leukemia, and interdigitating dendritic cell sarcoma of the lymph node. When combined with antibody against TTF-1 and CD5, CD1a antibody is useful in distinguishing between pulmonary and thymic neoplasms since CD1a is consistently expressed in thymic lymphocytes in both typical and atypical thymomas, but only focally in 1/6 of thymic carcinomas and not in lymphocytes in pulmonary neoplasms. antibody to CD1a is reported to be a new marker for perivascular epithelial cell tumor (PEComa).

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This mAb recognises granulocyte-colony stimulating factor (G-CSF) in the cytoplasm of mature granulocytes. It shows no reactivity with any other cell types. Markers of myeloid cells are useful in the identification of different levels of cellular differentiation. It reacts with early precursor and mature forms of myeloid cells. It is useful for the detection of myeloid leukemias and granulocytic sarcomas. It can be used as a marker of granulocytes in normal tissues or inflammatory processes.G-CSF is a pleiotropic cytokine that influences differentiation, proliferation and activation of the neutrophilic granulocyte lineage. The human G-CSF cDNA encodes a 207 amino acid precursor containing a 29 amino acid signal peptide that is proteolytically cleaved to form a 178 amino acid residue mature protein. Two G-CSFs, which are identical except for a three amino acid deletion in the amino-terminus of one form of the protein have been isolated from human cells. Murine and human G-CSF s share 73% sequence identity at the amino acid level.

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Estrogen receptors (ER) are members of the steroid/thyroid hormone receptor superfamily of ligand-activated transcription factors. Estrogen receptors, including alpha and beta, contain DNA binding and ligand binding domains and are critically involved in regulating the normal function of reproductive tissues. They are located in the nucleus, though some estrogen receptors associate with the cell surface membrane and can be rapidly activated by exposure of cells to estrogen. ER alpha and beta are differentially activated by various ligands. Ligand interaction triggers a cascade of events, including dissociation from heat shock proteins, recepter dimerization, phosphorylation and the association of the hormone activated receptor with specific regulatory elements in target genes. Evidence suggests that ER alpha and beta may be regulated by distinct mechanisms even though they share many functional characteristics.

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Eukaryotic histones are basic and water-soluble nuclear proteins that form hetero-octameric nucleosome particles by wrapping 146 base pairs of DNA in a left-handed super-helical turn sequentially to form chromosomal fiber. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form the octamer; formed of two H2A-H2B dimers and two H3-H4 dimers, forming two nearly symmetrical halves by tertiary structure. Over 80% of nucleosomes contain the linker Histone H1, derived from an intronless gene that interacts with linker DNA between nucleosomes and mediates compaction into higher order chromatin. Histones are subject to posttranslational modification by enzymes primarily on their N-terminal tails, but also in their globular domains. Such modifications include methylation, citrullination, acetylation, phosphorylation, sumoylation, ubiquitination and ADP-ribosylation.

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Thyroglobulin is a 660 kDa dimeric pre-protein with mutiple glycosylation sites. It is produced by and processed within the thyroid gland to produce the hormone thyroxine and triiodothyronine. Prior to forming dimers, thyroglobulin monomers undergo conformational maturation in the endoplasmic reticulation. The vast majority of follicular carcinomas of the thyroid will give positive immunoreactivity for anti-thyroglobulin even though sometimes only focally. Poorly differentiated carcinomas of the thyroid are frequently anti-thyroglobulin negative. Adenocarcinomas of other-than-thyroid origin do not react with this antibody. This antibody is useful in identification of thyroid carcinoma of the papillary and follicular types. Presence of thyroglobulin in metastatic lesions establishes the thyroid origin of tumor. Anti-thyroglobulin, combined with anti-calcitonin, can identify medullary carcinomas of the thyroid. Furthermore, anti-thyroglobulin, combined with anti-TTF1, can be a reliable marker to differentiate between primary thyroid and lung neoplasms.

Supplier: ProSci Inc.

Thyroglobulin is a 660 kDa dimeric pre-protein with mutiple glycosylation sites, detected at ~300 kDa in western blot. It is produced by and processed within the thyroid gland to produce the hormone thyroxine and triiodothyronine. Prior to forming dimers, thyroglobulin monomers undergo conformational maturation in the endoplasmic reticulation. The vast majority of follicular carcinomas of the thyroid will give positive immunoreactivity for thyroglobulin antibody even though sometimes only focally. Poorly differentiated carcinomas of the thyroid are frequently thyroglobulin antibody negative. Adenocarcinomas of other-than-thyroid origin do not react with this antibody. This antibody is useful in identification of thyroid carcinoma of the papillary and follicular types. Presence of thyroglobulin in metastatic lesions establishes the thyroid origin of tumor. Thyroglobulin antibody, combined with calcitonin antibody, can identify medullary carcinomas of the thyroid. Furthermore, thyroglobulin antibody, combined with TTF1 antibody, can be a reliable marker to differentiate between primary thyroid and lung neoplasms.