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Description:
This MAb recognizes a protein of 134 kDa, which binds fibroblast growth factor and E-selectin (cell-adhesion lectin on endothelial cells mediating the binding of neutrophils). Fucosylation is essential for binding to E-selectin. It contains sialic acid residues and 16 Cys-rich GLG1 repeats. This MAb can be used to stain the Golgi complex in cell or tissue preparations and can be used as a Golgi marker in subcellular fractions. It produces a diffuse staining pattern of the Golgi zone in normal and malignant cells. This MAb is an excellent marker for human cells in xenographic model research. It reacts specifically with human cells. The Golgi apparatus is an organelle present in all eukaryotic cells that forms a part of the endomembrane system. The primary function of the Golgi apparatus is to process and package macromolecules synthesized by the cell for exocytosis or use within the cell. The Golgi is made up of a stack of flattened, membrane-bound sacs known as cisternae, with three functional regions: the cis face, medial region and trans face. Each region consists of various enzymes that selectively modify the macromolecules passing though them, depending on where they are destined to reside. Several spherical vesicles that have budded off of the Golgi are present surrounding the main cisternae. The Golgi tends to be more pronounced and numerous in cells that make and secrete many substances such as plasma B cells.
Description:
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.
Description:
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.
Description:
Recognizes a single protein of 33-34 kDa, identified as the prostate specific antigen (PSA). This MAb is highly specific to PSA and stains prostatic secretory and ductal epithelium in both normal and neoplastic tissues. PSA is a chymotrypsin-like serine protease (kallikrein family) exclusively produced by the prostate epithelium, and abundant in seminal fluid. PSA can be detected in the sera of patients with prostatic carcinoma. It is predominantly complexed to a liver-derived serine protease inhibitor, alpha-1-antichymotrypsin (ACT). A higher proportion of serum PSA is complexed to ACT in prostate cancer than in benign prostate hyperplasia. This MAb makes an excellent pair with MAb 1A7G6B6 for PSA tests.
Description:
Recognizes a protein of 130-140 kDa, identified as CD22 (also known as BL-CAM). CD22 expression is restricted to normal and neoplastic B cells and is absent from other haemopoietic cell types. In B-cell ontogeny, CD22 is first expressed in the cytoplasm of pro-B and pre-B cells, and on the surface as B cells mature to become IgD . It is not expressed by plasma cells, CD22 is found highly expressed in follicular mantle and marginal zone B-cells, and while germinal center B-cells are relatively weak. CD22 is a member of the immunoglobulin superfamily and serves as an adhesion receptor for sialic acid-bearing ligands expressed on erythrocytes and all leukocyte classes. It also associates with tyrosine kinases and play a role in signal transduction and B-cell activation.
Description:
MAb VU-2G7 reacts with MUC1, a large transmembrane glycoprotein expressed on the ductal surface of normal glandular epithelia. The dominant epitope of VU-2G7 has not been established with epitope fingerprinting. The extracellular domain of MUC1 largely consists of a highly conserved, O-glycosylated 20 amino acids tandem repeat which can occur 30-100 times per molecule depending on the length of the allele involved. In the vast majority of human carcinomas this protein is up regulated and poorly glycosylated and appears on the cell surface in a non-polarized fashion.
Description:
MAb VU-2G7 reacts with MUC1, a large transmembrane glycoprotein expressed on the ductal surface of normal glandular epithelia. The dominant epitope of VU-2G7 has not been established with epitope fingerprinting. The extracellular domain of MUC1 largely consists of a highly conserved, O-glycosylated 20 amino acids tandem repeat which can occur 30-100 times per molecule depending on the length of the allele involved. In the vast majority of human carcinomas this protein is up regulated and poorly glycosylated and appears on the cell surface in a non-polarized fashion.
Description:
Recognizes a phosphor-protein of 45 kDa, identified as MyoD1. This MAb does not cross react with myogenin, Myf5, or Myf6. Antibody to MyoD1 labels the nuclei of myoblasts in developing muscle tissues. MyoD1 is not detected in normal adult tissue, but is highly expressed in the tumor cell nuclei of rhabdomyosarcomas. Occasionally nuclear expression of MyoD1 is seen in ectomesenchymoma and a subset of Wilm s tumors. Weak cytoplasmic staining is observed in several non-muscle tissues, including glandular epithelium and also in rhabdomyosarcomas, neuroblastomas, Ewing s sarcomas and alveolar soft part sarcomas.
Description:
Recognizes 183 kDa protein with DNA-binding characteristics, which is identified as a myeloid specific antigen. It reacts with myeloid precursor cells and granulocytes in bone marrow. Its antigen appears to be restricted to M2 and M3 acute myelogenous leukemia (AML) subtypes. Markers of myeloid cells are useful in the identification of different levels of cellular differentiation. This MAb reacts with early precursor and mature forms of human myeloid cells. It is useful in the identification of myelogenous leukemias, distinguishing granulocytic sarcomas from lymphoid malignancies and also in the study of differentiation and transformation of human myeloid cells. The biological function of this antigen is not clear, although it has been proposed that it may play a role in the differentiation of myeloid cells.
Description:
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-).
Description:
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). This MAb cocktail recognizes all simple epithelia including glandular epithelium, for example thyroid, female breast, gastrointestinal tract, respiratory tract, and urogenital tract including transitional epithelium. All adenocarcinomas and most squamous carcinomas are positive but keratinizing squamous carcinomas are usually negative. This antibody is useful in demonstrating the presence of Paget cells; there is very little keratin 18 in the normal epidermis so only Paget cells are stained.Immuno-histochemical staining with this MAb is indistinguishable from that obtained with monoclonal antibody 5D3.
Description:
Recognizes a protein of 30-33 kDa, which is identified as CD20 (Workshop V; Code CD20.4). It is a non-Ig differentiation antigen of B-cells and its expression is restricted to normal and neoplastic B-cells, being absent from all other leukocytes and tissues. CD20 is expressed by pre B-cells and persists during all stages of B-cell maturation but is lost upon terminal differentiation into plasma cells. The protein passes through the membrane 4 times with both ends in cytoplasm and exposes one short and one longer loop to the external environment. CD20 is not glycosylated in resting B-cells and its cytoplasmic domains are differentially phosphorylated upon activation. It acts as calcium channel involved in B cell activation and cell cycle progression.
Description:
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.
Description:
This MAb reacts with both SUMO-2 and SUMO-3. The small ubiquitin-related modifier (SUMO) proteins, which include SUMO-1, 2 and 3, belong to the ubiquitin-like protein family. Like ubiquitin, the SUMO proteins are synthesized as precursor proteins that undergo processing before conjugation to target proteins. Also, both utilize the E1, E2 and E3 cascade enzymes for conjugation. However, SUMO and ubiquitin differ with respect to targeting. Ubiquitination predominantly targets proteins for degradation, whereas sumoylation targets proteins to a variety of cellular processing, including nuclear transport, transcriptional regulation, apoptosis and protein stability. The unconjugated SUMO-1, 2 and 3 proteins localize to the nuclear membrane, nuclear bodies and cytoplasm, respectively. SUMO-1 utilizes Ubc9 for conjugation to several target proteins, which include MDM2, p53, PML and RanGap1. SUMO-2 and 3 contribute to a greater percentage of protein modification than does SUMO-1 and unlike SUMO-1, they can form polymeric chains. In addition, SUMO-3 regulates beta-Amyloid generation and may be critical in the onset or progression of Alzheimer’s disease.
Description:
This MAb reacts with both SUMO-2 and SUMO-3. The small ubiquitin-related modifier (SUMO) proteins, which include SUMO-1, 2 and 3, belong to the ubiquitin-like protein family. Like ubiquitin, the SUMO proteins are synthesized as precursor proteins that undergo processing before conjugation to target proteins. Also, both utilize the E1, E2 and E3 cascade enzymes for conjugation. However, SUMO and ubiquitin differ with respect to targeting. Ubiquitination predominantly targets proteins for degradation, whereas sumoylation targets proteins to a variety of cellular processing, including nuclear transport, transcriptional regulation, apoptosis and protein stability. The unconjugated SUMO-1, 2 and 3 proteins localize to the nuclear membrane, nuclear bodies and cytoplasm, respectively. SUMO-1 utilizes Ubc9 for conjugation to several target proteins, which include MDM2, p53, PML and RanGap1. SUMO-2 and 3 contribute to a greater percentage of protein modification than does SUMO-1 and unlike SUMO-1, they can form polymeric chains. In addition, SUMO-3 regulates beta-Amyloid generation and may be critical in the onset or progression of Alzheimer’s disease.
Description:
This MAb reacts with both SUMO-2 and SUMO-3. The small ubiquitin-related modifier (SUMO) proteins, which include SUMO-1, 2 and 3, belong to the ubiquitin-like protein family. Like ubiquitin, the SUMO proteins are synthesized as precursor proteins that undergo processing before conjugation to target proteins. Also, both utilize the E1, E2 and E3 cascade enzymes for conjugation. However, SUMO and ubiquitin differ with respect to targeting. Ubiquitination predominantly targets proteins for degradation, whereas sumoylation targets proteins to a variety of cellular processing, including nuclear transport, transcriptional regulation, apoptosis and protein stability. The unconjugated SUMO-1, 2 and 3 proteins localize to the nuclear membrane, nuclear bodies and cytoplasm, respectively. SUMO-1 utilizes Ubc9 for conjugation to several target proteins, which include MDM2, p53, PML and RanGap1. SUMO-2 and 3 contribute to a greater percentage of protein modification than does SUMO-1 and unlike SUMO-1, they can form polymeric chains. In addition, SUMO-3 regulates beta-Amyloid generation and may be critical in the onset or progression of Alzheimer’s disease.
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