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ZAP70 is a 70 kDa protein tyrosine kinase found in T-cells and natural killer cells. Control of this protein translation is via the IgVH gene.In Western blotting of whole cell lysates of normal peripheral blood mononuclear cells, the antibody labels a band corresponding to ZAP70. In Western blotting of whole cell lysates of CD19-positive purified leukemia cells from patients with Ig-unmutated and Ig-mutated CLL, the antibody labels a band corresponding to ZAP70 in the Ig-unmutated CLL samples, whereas no band is observed in the Ig-mutated CLL samples. In Western blotting of cell lysates of Jurkat cells (T-lymphoblastic cell line), the antibody labels a band of 70 kDa protein. In Western blotting of cell lysates of A431 cells (carcinoma cell line), no band is observed. ZAP70 protein is expressed in leukemic cells of approximately 25% of chronic lymphocytic leukemia (CLL) cases as well. Anti-ZAP70 expression is an excellent surrogate marker for the distinction between the Ig-mutated (anti-ZAP70 negative) and Ig-unmutated (anti-ZAP70 positive) CLL subtypes and can identify patient groups with divergent clinical courses. The anti-ZAP70 positive Ig-unmutated CLL cases have been shown to have a poorer prognosis.

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Recognizes a protein of 40 kDa, identified as cytokeratin-19 (CK19), which is expressed in sweat gland, mammary gland ductal and secretory cells, bile ducts, gastrointestinal tract, bladder urothelium, oral epithelia, esophagus, and ectocervical epithelium. Anti-CK19 reacts with a wide variety of epithelial malignancies including adenocarcinomas of the colon, stomach, pancreas, biliary tract, liver, and breast. Perhaps the most useful application is the identification of thyroid carcinoma of the papillary type, although 50%-60% of follicular carcinomas are also labeled. Anti-CK19 is a useful marker for detection of tumor cells in lymph nodes, peripheral blood, bone marrow and breast cancer.

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Recognizes a protein of 40 kDa, identified as CD7, a member of the immunoglobulin gene superfamily. Its N-terminal amino acids 1-107 are highly homologous to Ig kappa-L chains whereas the carboxyl-terminal region of the extracellular domain is proline-rich and has been postulated to form a stalk from which the Ig domain projects. CD7 is expressed on the majority of immature and mature T-lymphocytes, and T cell leukemia. It is also found on natural killer cells, a small subpopulation of normal B cells and on malignant B cells. Cross-linking surface CD7 positively modulates T cell and NK cell activity as measured by calcium fluxes, expression of adhesion molecules, cytokine secretion and proliferation. CD7 associates directly with phosphoinositol 3'-kinase. CD7 ligation induces production of D-3 phosphoinositides and tyrosine phosphorylation.

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This MAb recognizes protein of 26 kDa-60 kDa, which is identified as CD63. Its epitope is different from that of MAb LAMP3/529. The tetraspanins are integral membrane proteins expressed on cell surface and granular membranes of hematopoietic cells and are components of multi-molecular complexes with specific integrins. The tetraspanin CD63 is a lysosomal membrane glycoprotein that translocates to the plasma membrane after platelet activation. CD63 is expressed on activated platelets, monocytes and macrophages, and is weakly expressed on granulocytes, T cell and B cells. It is located on the basophilic granule membranes and on the plasma membranes of lymphocytes and granulocytes. CD63 is a member of the TM4 superfamily of leukocyte glycoproteins that includes CD9, CD37 and CD53, which contain four transmembrane regions. CD63 may play a role in phagocytic and intracellular lysosome-phagosome fusion events. CD63 deficiency is associated with Hermansky-Pudlak syndrome and is strongly expressed during the early stages of melanoma progression.

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Recognizes a protein of 40 kDa, identified as CD7, a member of the immunoglobulin gene superfamily. Its N-terminal amino acids 1-107 are highly homologous to Ig kappa-L chains whereas the carboxyl-terminal region of the extracellular domain is proline-rich and has been postulated to form a stalk from which the Ig domain projects. CD7 is expressed on the majority of immature and mature T-lymphocytes, and T cell leukemia. It is also found on natural killer cells, a small subpopulation of normal B cells and on malignant B cells. Cross-linking surface CD7 positively modulates T cell and NK cell activity as measured by calcium fluxes, expression of adhesion molecules, cytokine secretion and proliferation. CD7 associates directly with phosphoinositol 3'-kinase. CD7 ligation induces production of D-3 phosphoinositides and tyrosine phosphorylation.

Supplier: Biotium

Recognizes a protein of 40 kDa, identified as CD7, a member of the immunoglobulin gene superfamily. Its N-terminal amino acids 1-107 are highly homologous to Ig kappa-L chains whereas the carboxyl-terminal region of the extracellular domain is proline-rich and has been postulated to form a stalk from which the Ig domain projects. CD7 is expressed on the majority of immature and mature T-lymphocytes, and T cell leukemia. It is also found on natural killer cells, a small subpopulation of normal B cells and on malignant B cells. Cross-linking surface CD7 positively modulates T cell and NK cell activity as measured by calcium fluxes, expression of adhesion molecules, cytokine secretion and proliferation. CD7 associates directly with phosphoinositol 3'-kinase. CD7 ligation induces production of D-3 phosphoinositides and tyrosine phosphorylation.

Supplier: Biotium

ZAP70 is a 70 kDa protein tyrosine kinase found in T-cells and natural killer cells.Control of this protein translation is via the IgVH gene. ZAP70 protein is expressed in leukemic cells of approximately 25% of chronic lymphocytic leukemia (CLL) cases as well.Anti-ZAP70 expression is an excellent surrogate marker for the distinction between the Ig-mutated (anti-ZAP70 negative) and Ig-unmutated (anti-ZAP70 positive) CLL subtypes and can identify patient groups with divergent clinical courses. The anti-ZAP70 positive Ig-unmutated CLL cases have been shown to have a poorer prognosis.

Supplier: Biotium

This antibody recognizes a 45 kDa protein, which is identified as isocitrate dehydrogenase (IDH1). It belongs to the isocitrate and isopropylmalate dehydrogenases family. IDH1 catalyzes the third step of the citric acid cycle, which involves the oxidative decarboxylation of isocitrate, formingalpha-ketoglutarate and CO2 in a two-step reaction. The first step involves the oxidation of isocitrate to the intermediate oxalosuccinate, while the second step involves the production ofalpha-ketoglutarate. During this process, either NADH or NADPH is produced along with CO2. Recently, an inactivating mutation of IDH1 has been implicated in glioblastoma. IDH1 appears to function as a tumor suppressor that, when mutationally inactivated, contributes to tumorigenesis in part through induction of the HIF-1 pathway.

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HLA-B belongs to the HLA class I heavy chain paralogues. This class I molecule is a heterodimer consisting of a heavy chain and a light chain (beta-2 microglobulin). The heavy chain is anchored in the membrane. Class I molecules play a central role in the immune system by presenting peptides derived from the endoplasmic reticulum lumen. They are expressed in nearly all cells. The heavy chain is approximately 45 kDa and its gene contains 8 exons. Exon 1 encodes the leader peptide, exon 2 and 3 encode the alpha1 and alpha2 domains, which both bind the peptide, exon 4 encodes the alpha3 domain, exon 5 encodes the transmembrane region and exons 6 and 7 encode the cytoplasmic tail. Polymorphisms within exon 2 and exon 3 are responsible for the peptide binding specificity of each class one molecule. Typing for these polymorphisms is routinely done for bone marrow and kidney transplantation. Hundreds of HLA-B alleles have been described.

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Cytokeratin 7 is a basic cytokeratin, which is found in most glandular and transitional epithelia but not in the stratified squamous epithelia. Keratin 7 is expressed in the epithelial cells of ovary, lung, and breast but not of colon, prostate, or gastrointestinal tract. Antibody to cytokeratin is useful in distinguishing ovarian carcinomas (keratin 7 ) from colon carcinomas (keratin 7-).

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In Western blotting, this antibody recognizes proteins in MW range of 265-400 kDa, identified as different glycoforms of EMA. The α subunit has cell adhesive properties. It can act both as an adhesion and an anti-adhesion protein. EMA may provide a protective layer on epithelial cells against bacterial and enzyme attack. The β subunit contains a C-terminal domain, which is involved in cell signaling, through phosphorylations and protein-protein interactions. In immunohistochemical assays, it superbly stains routine formalin/paraffin carcinoma tissues. Antibody to EMA is useful as a pan-epithelial marker for detecting early metastatic loci of carcinoma in bone marrow or liver.

Supplier: Biotium

In Western blotting, this antibody recognizes proteins in MW range of 265-400 kDa, identified as different glycoforms of EMA. The α subunit has cell adhesive properties. It can act both as an adhesion and an anti-adhesion protein. EMA may provide a protective layer on epithelial cells against bacterial and enzyme attack. The β subunit contains a C-terminal domain, which is involved in cell signaling, through phosphorylations and protein-protein interactions. In immunohistochemical assays, it superbly stains routine formalin/paraffin carcinoma tissues. Antibody to EMA is useful as a pan-epithelial marker for detecting early metastatic loci of carcinoma in bone marrow or liver.

Supplier: Biotium

This antibody recognizes an antigen associated with the nuclear membrane in human cells. It can be used to stain the nuclear membrane in cell or tissue preparations and can be used as a marker of the nuclear membrane in subcellular fractions. It produces a ring pattern around the nucleus of cells of normal and malignant cells and may be used to stain the nuclear membrane of cells in fixed or frozen tissue sections. It can be used with paraformaldehyde fixed frozen tissue or cell preparations and formalin fixed, paraffin-embedded tissue sections.,The nuclear envelope (also known as the perinuclear envelope, nuclear membrane, nucleolemma or karyotheca) is the double membrane of the nucleus that encloses genetic material in eukaryotic cells. It separates the contents of the nucleus (DNA in particular) from the cytosol (cytoplasm). Numerous nuclear pores are present on the nuclear envelope to facilitate and regulate the exchange of materials (for example, proteins and RNA) between the nucleus and the cytoplasm. The space between the two membranes that make up the nuclear envelope is called the perinuclear space (also called the perinuclear cisterna), and is usually about 20 - 40 nm wide. Each of the two membranes is composed of a lipid bilayer. The outer membrane is continuous with the rough endoplasmic reticulum. The inner membrane is erected upon the nuclear lamina, a network of intermediate filaments made of lamin, that plays a role in mitosis and meiosis. The type of lamins present are A, B1, B2, and C. The nuclear envelope may also play a role in the disposition of chromatin inside the nucleus. The lamina acts as a site of attachment for chromosomes. It also acts like a shield for the nucleus. During prophase in mitosis, the chromatids begin condensing to form chromosomes, and the nuclear envelope begins to disintegrate. During metaphase, the nuclear envelope is completely disintegrated, and the chromosomes can be pulled apart as chromatids by the spindle fibers.

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Recognizes a protein of 32 kDa, identified as CD8a (also known as CD8 chain, T cell co-receptor, Leu2, and T8). CD8 molecule consists of two chains, termed and chain, which are expressed as a disulphide-linked heterodimer or as an homodimer. CD8 is expressed on T cell subset (cytotoxic/suppressor T cells), thymocytes and NK cells. The majority of CD8 T-cells expresses CD8 as heterodimer. Some subpopulation of CD8 T cells as well as NK cells may express homodimer. CD8 functions as a co-receptor in concert with TCR for binding the MHC class I/peptide complex. The HIV-2 envelope glycoprotein binds CD8 chain (but not chain). The cytoplasmic domain of CD8 associates with p56lck tyrosine kinase.

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CD19 is a transmembrane glycoprotein that contains two extracellular immunoglobulin-like domains. CD19 is present in both benign and malignant B-cells and is considered to be the most reliable surface marker of this lineage over a wide range of maturational stages. In normal lymphoid tissue, CD19 is observed in germinal centers, in mantle zone cells, and in scattered cells of the inter-follicular areas. Anti-CD19 exhibits an overall immunoreactivity pattern similar to those of the antibodies against CD20 and CD22. However, in contrast to CD20, expression of CD19 is continuous throughout B-cell development and through terminal differentiation of B-cells into plasma cells. Anti-CD19 positivity is seen in the vast majority of B-cell neoplasms commonly at a lower intensity than normal B-cell counterparts. Plasma cell neoplasms are nearly always negative, as are T-cell neoplasms.

Supplier: Biotium

Recognizes a protein of 95 kDa, identified as CD19. CD19 is a transmembrane glycoprotein that contains two extracellular immunoglobulin-like domains. CD19 is present in both benign and malignant B-cells and is considered to be the most reliable surface marker of this lineage over a wide range of maturational stages. In normal lymphoid tissue, CD19 is observed in germinal centers, in mantle zone cells, and in scattered cells of the inter-follicular areas. Anti-CD19 exhibits an overall immunoreactivity pattern similar to those of the antibodies against CD20 and CD22. However, in contrast to CD20, expression of CD19 is continuous throughout B-cell development and through terminal differentiation of B-cells into plasma cells. Anti-CD19 positivity is seen in the vast majority of B-cell neoplasms commonly at a lower intensity than normal B-cell counterparts. Plasma cell neoplasms are nearly always negative, as are T-cell neoplasms.

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JC-1 dye is used for fluorescence-based measurement of mitochondrial membrane potential changes in cells, a key measure of cell viability.

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IL-6 is a potent lymphoid cell growth factor that stimulates the growth and survivability of certain B-cells and T-cells. IL-6 plays a role in host defense, acute phase reactions, immune responses, and hematopoiesis. IL-6 is expressed by T-cells, B-cells, monocytes, fibroblasts, hepatocytes, endothelial cells and keratinocytes.

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The family of EF-hand type Ca2 -binding proteins includes calbindin, S-100 alpha and beta, calgranulins, B and C, and the parvalbumin family members, including parvalbumin alpha and parvalbumin beta. The S-100 protein is involved in the regulation of cellular processes such as cell cycle progression and differentiation. S-100 protein may function in the activation of Ca2 induced Ca2 release, inhibition of microtubule assembly and inhibition of protein kinase C mediated phosphorylation. Two S-100 subunits, sharing 60% sequence identity, have been described as S-100 alpha chain and S-100 beta chain. Three S-100 dimeric forms have been characterized, differing in their subunit composition of two alpha chains, two beta chains or one alpha and one beta chain. S-100 localizes to the cytoplasm and nuclei of astrocytes, Schwann s cells, ependymomas and astrogliomas. S-100 is also detected in almost all benign naevi, malignant melanocytic tumours and in Langerhans cells in the skin. Calbindin, S-100 proteins and parvalbumin proteins are each expressed in neural tissues. In addition, S-100 alpha and beta are present in a variety of other tissues and calbindin is present in intestine and kidney.

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This MAb stains the cytoplasm of macrophages and histiocytes in hematopoietic organs, Kupffer's cells of the liver and Langerhan's cells of the skin. It also stains the mantle zone B-lymphocytes of the lymph node and spleen, spermatogonia, and chief cells of the stomach. S100A9 is expressed by macrophages in acutely inflamed tissues and in chronic inflammation. It is detected in peripheral blood leukocytes, in neutrophils and granulocytes. It is present at sites of vascular inflammation. S100A9 is also expressed in epithelial cells constitutively or induced during dermatoses. S100A9 is a Calcium-binding protein. It has antimicrobial activity towards bacteria and fungi. It is important for resistance to invasion by pathogenic bacteria. It up-regulates transcription of genes that are under the control of NF-kappa-B. S100A9 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide (LPS). It promotes tubulin polymerization when unphosphorylated. It also promotes phagocyte migration and infiltration of granulocytes at sites of wounding. It plays a role as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.

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Recognizes the -chain of CD3, which consists of five different polypeptide chains (designated as γ, δ, ε, ζ, and η) with MW ranging from 16-28 kDa. The CD3 complex is closely associated at the lymphocyte cell surface with the T cell antigen receptor (TCR). Reportedly, CD3 complex is involved in signal transduction to the T cell interior following antigen recognition. The CD3 antigen is first detectable in early thymocytes and probably represents one of the earliest signs of commitment to the T cell lineage. In cortical thymocytes, CD3 is predominantly intra-cytoplasmic. However, in medullary thymocytes, it appears on the T cell surface. CD3 antigen is a highly specific marker for T cells, and is present in majority of T cell neoplasms.

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Recognizes a protein of 185 kDa, which is identified as c-erbB-2/HER-2/neu. Its epitope is localized in the extracellular domain. C-erbB-2/HER-2 is a member of the EGFR family. This MAb is specific and shows minimal cross-reaction with other members of the EGFR-family. Receptors of this family are located on the plasma membrane and consist of an extracellular ligand-binding domain that is connected to a large intracellular domain by a single transmembrane sequence. c-erbB-2/HER-2 protein is over-expressed in a variety of carcinomas especially those of breast and ovary.

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Recognizes a protein of 185 kDa, which is identified as c-erbB-2/HER-2/neu. Its epitope is localized in the extracellular domain. C-erbB-2/HER-2 is a member of the EGFR family. This MAb is specific and shows minimal cross-reaction with other members of the EGFR-family. Receptors of this family are located on the plasma membrane and consist of an extracellular ligand-binding domain that is connected to a large intracellular domain by a single transmembrane sequence. c-erbB-2/HER-2 protein is over-expressed in a variety of carcinomas especially those of breast and ovary.

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This MAb stains the cytoplasm of macrophages and histiocytes in hematopoietic organs, Kupffer's cells of the liver and Langerhan's cells of the skin. It also stains the mantle zone B-lymphocytes of the lymph node and spleen, spermatogonia, and chief cells of the stomach. S100A9 is expressed by macrophages in acutely inflamed tissues and in chronic inflammation. It is detected in peripheral blood leukocytes, in neutrophils and granulocytes. It is present at sites of vascular inflammation. S100A9 is also expressed in epithelial cells constitutively or induced during dermatoses. S100A9 is a Calcium-binding protein. It has antimicrobial activity towards bacteria and fungi. It is important for resistance to invasion by pathogenic bacteria. It up-regulates transcription of genes that are under the control of NF-kappa-B. S100A9 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide (LPS). It promotes tubulin polymerization when unphosphorylated. It also promotes phagocyte migration and infiltration of granulocytes at sites of wounding. It plays a role as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.

Supplier: Biotium

This MAb stains the cytoplasm of macrophages and histiocytes in hematopoietic organs, Kupffer's cells of the liver and Langerhan's cells of the skin. It also stains the mantle zone B-lymphocytes of the lymph node and spleen, spermatogonia, and chief cells of the stomach. S100A9 is expressed by macrophages in acutely inflamed tissues and in chronic inflammation. It is detected in peripheral blood leukocytes, in neutrophils and granulocytes. It is present at sites of vascular inflammation. S100A9 is also expressed in epithelial cells constitutively or induced during dermatoses. S100A9 is a Calcium-binding protein. It has antimicrobial activity towards bacteria and fungi. It is important for resistance to invasion by pathogenic bacteria. It up-regulates transcription of genes that are under the control of NF-kappa-B. S100A9 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide (LPS). It promotes tubulin polymerization when unphosphorylated. It also promotes phagocyte migration and infiltration of granulocytes at sites of wounding. It plays a role as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.

Supplier: Biotium

Recognizes a 67 kDa glycoprotein, which is identified as CD33 (HLDA IV; WS Code M-505). CD33 is a transmembrane protein of the sialic acid-binding immunoglobulin-like lectin (Siglec) family. It belongs to the immuno-receptor tyrosine-based inhibitory motif (ITIM)-containing molecules able of recruiting protein tyrosine phosphatases SHP-1 and SHP-2 to signal assemblies; these ITIMs are also used for ubiquitin-mediated removal of the receptor from the cell surface. CD33 is expressed on cells of myelomonocytic lineage, binds sialic acid residues in N- and O-glycans on cell surfaces, and is a therapeutic target for acute myeloid leukemia. CD33 is expressed on myeloid progenitors, monocytes, granulocytes, dendritic cells and mast cells. It is absent on platelets, lymphocytes, erythrocytes and hematopoietic stem cells.

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The c-Myc protein is a transcription factor, which is encoded by the c-Myc gene on human chromosome 8q24. c-Myc is commonly activated in a variety of tumor cells and plays an important role in cellular proliferation, differentiation, apoptosis and cell cycle progression. The phosphorylation of c-Myc has been investigated and previous studies have suggested a functional association between phosphorylation at Thr58/Ser62 by glycogen synthase kinase 3, cyclin dependent kinase, ERK2 and C-Jun N terminal Kinase (JNK) in cell proliferation and cell cycle regulation. Studies also have shown that c-Myc is essential for tumor cell development in vasculogenesis and angiogenesis that distribute blood throughout the cells, and which brought extensive attention in the development of new therapeutic approach for cancer treatment.

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The c-Myc protein is a transcription factor, which is encoded by the c-Myc gene on human chromosome 8q24. c-Myc is commonly activated in a variety of tumor cells and plays an important role in cellular proliferation, differentiation, apoptosis and cell cycle progression. The phosphorylation of c-Myc has been investigated and previous studies have suggested a functional association between phosphorylation at Thr58/Ser62 by glycogen synthase kinase 3, cyclin dependent kinase, ERK2 and C-Jun N terminal Kinase (JNK) in cell proliferation and cell cycle regulation. Studies also have shown that c-Myc is essential for tumor cell development in vasculogenesis and angiogenesis that distribute blood throughout the cells, and which brought extensive attention in the development of new therapeutic approach for cancer treatment.

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Anti-CD57 marks a subset of lymphocytes known as natural killer (NK) cells. Follicular center cell lymphomas often contain many NK cells within the neoplastic follicles. Anti-CD57 also stains neuroendocrine cells and their derived tumors, including carcinoid tumor and medulloblastoma. Anti-CD57 can also be useful in separating type B3 thymoma from thymic carcinoma when combined with a panel that includes antibodies against GLUT1, CD5, and CEA.

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This antibody recognizes a protein of 35 kDa, which is identified as tartrate-resistant acid phosphatase (TRAcP). It exists as two isoforms (5a and 5b). This MAb reacts with both the isoforms. Serum TRAcP 5a is secreted by macrophages and dendritic cells and increased in many patients of rheumatoid arthritis.Serum TRAcP 5b is produced from osteoclasts and elevated during bone resorption. TRAcP is an iron containing glycoprotein, which catalyzes the conversion of orthophosphoric monoester to alcohol and orthophosphate. It is the most basic of the acid phosphatases and is the only form not inhibited by L( )-tartrate. TRAcP is synthesized as a latent proenzyme and is activated by proteolytic cleavage and reduction. Normally, TRAcP is highly expressed by osteoclasts, activated macrophages, neurons and endometrium during pregnancy. Expression of TRAcP is increased in certain pathological conditions such as Leukemic Reticuloendotheliosis (Hairy Cell Leukemia), Gaucher's Disease, HIV-induced Encephalopathy, Osteoclastoma and in osteoporosis and metabolic bone diseases. Anti-TRAcP antibody labels the cells of Hairy Cell Leukemia (HCL) with a high degree of sensitivity and specificity. Other cells stained with this antibody are tissue macrophages and osteoclasts.