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mycoplasma+detection
Numéro de catalogue:
(BOSSBS-8603R-A555)
Fournisseur:
Bioss
Description:
The Hox proteins play a role in patterns of embryonic development and cellular differentiation by regulating downstream target genes. In vivo, the HoxD9 protein interacts with the autoregulatory and cross-regulatory enhancers of the murine HoxB1 and human HoxD9 genes. Specifically, the HoxD9 protein interacts with the human control region (HCR) of the HoxD9 gene, thus inducing transcription of the HoxD9 promoter. HoxD9 may be a multifunctional transcriptional regulator, as it contains different activation domains. Activation of HoxD9 depends on the structure of the target regulatory element, and results in differential cofactor interaction. The HoxD9 protein is expressed in the early stages of mouse joint development, primarily in the articular cartilage. HoxD9 transcripts are also detected in the synovial tissue of arthritic mice, but not in that of normal mice, suggesting that HoxD9 may have a role in the pathology of arthritis. Furthermore, the HoxD9 protein is highly expressed in the synoviocytes of patients with rheumatoid arthritis (RA), but not in osteoarthritis patients. The human HoxD9 protein is also differentially expressed in the human cervical cancer cell line HeLa, but is not expressed in the normal cervix and may thus play a role in tumorigenesis.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-8603R-A488)
Fournisseur:
Bioss
Description:
The Hox proteins play a role in patterns of embryonic development and cellular differentiation by regulating downstream target genes. In vivo, the HoxD9 protein interacts with the autoregulatory and cross-regulatory enhancers of the murine HoxB1 and human HoxD9 genes. Specifically, the HoxD9 protein interacts with the human control region (HCR) of the HoxD9 gene, thus inducing transcription of the HoxD9 promoter. HoxD9 may be a multifunctional transcriptional regulator, as it contains different activation domains. Activation of HoxD9 depends on the structure of the target regulatory element, and results in differential cofactor interaction. The HoxD9 protein is expressed in the early stages of mouse joint development, primarily in the articular cartilage. HoxD9 transcripts are also detected in the synovial tissue of arthritic mice, but not in that of normal mice, suggesting that HoxD9 may have a role in the pathology of arthritis. Furthermore, the HoxD9 protein is highly expressed in the synoviocytes of patients with rheumatoid arthritis (RA), but not in osteoarthritis patients. The human HoxD9 protein is also differentially expressed in the human cervical cancer cell line HeLa, but is not expressed in the normal cervix and may thus play a role in tumorigenesis.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-8603R-A680)
Fournisseur:
Bioss
Description:
The Hox proteins play a role in patterns of embryonic development and cellular differentiation by regulating downstream target genes. <i>in vivo</i>, the HoxD9 protein interacts with the autoregulatory and cross-regulatory enhancers of the murine HoxB1 and human HoxD9 genes. Specifically, the HoxD9 protein interacts with the human control region (HCR) of the HoxD9 gene, thus inducing transcription of the HoxD9 promoter. HoxD9 may be a multifunctional transcriptional regulator, as it contains different activation domains. Activation of HoxD9 depends on the structure of the target regulatory element, and results in differential cofactor interaction. The HoxD9 protein is expressed in the early stages of mouse joint development, primarily in the articular cartilage. HoxD9 transcripts are also detected in the synovial tissue of arthritic mice, but not in that of normal mice, suggesting that HoxD9 may have a role in the pathology of arthritis. Furthermore, the HoxD9 protein is highly expressed in the synoviocytes of patients with rheumatoid arthritis (RA), but not in osteoarthritis patients. The human HoxD9 protein is also differentially expressed in the human cervical cancer cell line HeLa, but is not expressed in the normal cervix and may thus play a role in tumorigenesis.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-8603R)
Fournisseur:
Bioss
Description:
The Hox proteins play a role in patterns of embryonic development and cellular differentiation by regulating downstream target genes. In vivo, the HoxD9 protein interacts with the autoregulatory and cross-regulatory enhancers of the murine HoxB1 and human HoxD9 genes. Specifically, the HoxD9 protein interacts with the human control region (HCR) of the HoxD9 gene, thus inducing transcription of the HoxD9 promoter. HoxD9 may be a multifunctional transcriptional regulator, as it contains different activation domains. Activation of HoxD9 depends on the structure of the target regulatory element, and results in differential cofactor interaction. The HoxD9 protein is expressed in the early stages of mouse joint development, primarily in the articular cartilage. HoxD9 transcripts are also detected in the synovial tissue of arthritic mice, but not in that of normal mice, suggesting that HoxD9 may have a role in the pathology of arthritis. Furthermore, the HoxD9 protein is highly expressed in the synoviocytes of patients with rheumatoid arthritis (RA), but not in osteoarthritis patients. The human HoxD9 protein is also differentially expressed in the human cervical cancer cell line HeLa, but is not expressed in the normal cervix and may thus play a role in tumorigenesis.
UOM:
1 * 100 µl
Numéro de catalogue:
(ENZOBMLFG60200100)
Fournisseur:
ENZO LIFE SCIENCES
Description:
Fibronectins are high molecular weight, disulphide-linked, dimeric cell adhesion glycoproteins found in basement membranes and in the interstitial connective tissue matrix. A single fibronectin gene is subject to alternative splicing in a cell-type-, development- and age-regulated manner which gives rise to multiple molecular forms. In addition to their prominent role in adhesion, fibronectins have been reported to mediate various aspects of cellular interaction, including migration during development and wound-healing, haemostasis, and the regulation of cell growth and differentiation. Cellular fibronectins (cFn) are found in low amounts in normal human plasma and tissues, but they are abundant in the plasma of carcinoma patients and in the stroma of various carcinomas. In contrast, a soluble form of fibronectin produced by hepatocytes is readily detectable in plasma and becomes deposited in pericellular matrices and within tissues. This form of fibronectin, referred to as ‘plasma fibronectin’ (pFn), differs from cFn by the absence of an amino acid sequence, known as extra domain A1.
UOM:
1 * 100 µl
New Product
Numéro de catalogue:
(BOSSBS-1302R-A488)
Fournisseur:
Bioss
Description:
Glutamic Acid Decarboxylase (GAD) catalyzes the conversion of L glutamate to g-aminobutyric acid (GABA), the principal inhibitory neurotransmitter in the brain, and a putative paracrine signal molecule in pancreatic islets. GAD has a restricted tissue distribution. It is highly expressed in the cytoplasm of GABAergic neurons in the central nervous system (CNS) and pancreatic beta cells. It is also present in other non-neuronal tissues such as testis, oviduct and ovary. GAD is also transiently expressed in non-GABAergic cells of the embryonic and adult nervous system, suggesting its involvement in development and plasticity. GAD exists as two isoforms, GAD65 and GAD67 (molecular masses of 65 and 67 kD, respectively) that are encoded by two different genes. GAD65 is an ampiphilic, membraneanchored protein, (585 amino acid residues) and is encoded on human chromosome 10. GAD67 is a cytoplasmic protein (594 amino acid residues) and is encoded on chromosome 2. There is 64% amino acid identity between the two isoforms, with the highest diversity located at the N terminus, which in GAD65 is required for targeting the enzyme to GABA-containing secretory vesicles. The two isoforms appear to have distinct intraneuronal distribution in the brain. GAD65 has been identified as an autoantigen in insulindependent diabetes mellitus (IDDM) and stiff-man syndrome (SMS), IDDM is an autoimmune disease that results from T cell mediated destruction of pancreatic insulin-secreting beta cells. Islet-reactive T cells and primarily to GAD65 (also named beta cell autoantigen) can be detected in peripheral blood of 80% of recent-onset IDD patients and in pre-diabetic high-risk subjects before onset of clinical symptoms. This suggests that GAD may be an important marker in the early stages of the disease.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3055R-CY5)
Fournisseur:
Bioss
Description:
Non-receptor tyrosine kinase indispensable for B lymphocyte development, differentiation and signaling. Binding of antigen to the B-cell antigen receptor (BCR) triggers signaling that ultimately leads to B-cell activation. After BCR engagement and activation at the plasma membrane, phosphorylates PLCG2 at several sites, igniting the downstream signaling pathway through calcium mobilization, followed by activation of the protein kinase C (PKC) family members. PLCG2 phosphorylation is performed in close cooperation with the adapter protein B-cell linker protein BLNK. BTK acts as a platform to bring together a diverse array of signaling proteins and is implicated in cytokine receptor signaling pathways. Plays an important role in the function of immune cells of innate as well as adaptive immunity, as a component of the Toll-like receptors (TLR) pathway. The TLR pathway acts as a primary surveillance system for the detection of pathogens and are crucial to the activation of host defense. Especially, is a critical molecule in regulating TLR9 activation in splenic B-cells. Within the TLR pathway, induces tyrosine phosphorylation of TIRAP which leads to TIRAP degradation. BTK plays also a critical role in transcription regulation. Induces the activity of NF-kappa-B, which is involved in regulating the expression of hundreds of genes. BTK is involved on the signaling pathway linking TLR8 and TLR9 to NF-kappa-B. Transiently phosphorylates transcription factor GTF2I on tyrosine residues in response to BCR. GTF2I then translocates to the nucleus to bind regulatory enhancer elements to modulate gene expression. ARID3A and NFAT are other transcriptional target of BTK. BTK is required for the formation of functional ARID3A DNA-binding complexes. There is however no evidence that BTK itself binds directly to DNA. BTK has a dual role in the regulation of apoptosis.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3069R-FITC)
Fournisseur:
Bioss
Description:
Non-receptor tyrosine kinase indispensable for B lymphocyte development, differentiation and signaling. Binding of antigen to the B-cell antigen receptor (BCR) triggers signaling that ultimately leads to B-cell activation. After BCR engagement and activation at the plasma membrane, phosphorylates PLCG2 at several sites, igniting the downstream signaling pathway through calcium mobilization, followed by activation of the protein kinase C (PKC) family members. PLCG2 phosphorylation is performed in close cooperation with the adapter protein B-cell linker protein BLNK. BTK acts as a platform to bring together a diverse array of signaling proteins and is implicated in cytokine receptor signaling pathways. Plays an important role in the function of immune cells of innate as well as adaptive immunity, as a component of the Toll-like receptors (TLR) pathway. The TLR pathway acts as a primary surveillance system for the detection of pathogens and are crucial to the activation of host defense. Especially, is a critical molecule in regulating TLR9 activation in splenic B-cells. Within the TLR pathway, induces tyrosine phosphorylation of TIRAP which leads to TIRAP degradation. BTK plays also a critical role in transcription regulation. Induces the activity of NF-kappa-B, which is involved in regulating the expression of hundreds of genes. BTK is involved on the signaling pathway linking TLR8 and TLR9 to NF-kappa-B. Transiently phosphorylates transcription factor GTF2I on tyrosine residues in response to BCR. GTF2I then translocates to the nucleus to bind regulatory enhancer elements to modulate gene expression. ARID3A and NFAT are other transcriptional target of BTK. BTK is required for the formation of functional ARID3A DNA-binding complexes. There is however no evidence that BTK itself binds directly to DNA. BTK has a dual role in the regulation of apoptosis.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13248R-CY3)
Fournisseur:
Bioss
Description:
Heterotrimeric G proteins function to relay information from cell surface receptors to intracellular effectors (1). Each of a very broad range of receptors specifically detects an extracellular stimulus (a photon, pheromone, odorant, hormone or neurotransmitter) while the effectors (i.e., adenylyl cyclase), which act to generate one or more intracellular messengers, are less numerous. In mammals, G protein alpha, Beta and Gamma polypeptides are encoded by at least 16, 4 and 7 genes, respectively (2-5). Most interest in G proteins has been focused on their a subunits, since these proteins bind and hydrolyze GTP and most obviously regulate the activity of the best studied effectors. Four distinct classes of G alpha subunits have been identified; these include Gs, Gi, Gq and Ga 12/13 (3,4). The Gi class comprises all the known a subunits that are susceptible to pertussis toxin modifications, including Ga i-1, Ga i-2, Ga i-3, Ga o, Ga t1, Ga t2, Ga z and Ga gust (4). Of these, the three Ga i subtypes function to open atrial potassium channels (6). Ga 16 is a member of the Gq subfamily and is expressed specifically in hematopoietic cells (7).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-2190R-CY3)
Fournisseur:
Bioss
Description:
Cytokeratins, a group comprising at least 29 different proteins, are characteristic of epithelial and trichocytic cells. Cytokeratins 1, 4, 5, 6, and 8 are members of the type II neutral to basic subfamily. Antibody to cytokeratins are specific markers of epithelial cell differentiation and have been widely used as tools in tumor identification and classification. Anti Pan Cytokeratin (mixture) is a broadly reactive reagent, which recognizes epitopes present in most human epithelial tissues. It facilitates typing of normal, metaplastic and neoplastic cells. Synergy between the various components results in staining amplification. This enables identification of cells, which would otherwise be stained only marginally. The mixture may aid in the discrimination of carcinomas and nonepithelial tumors such as sarcomas, lymphomas and neural tumors. It is also useful in detecting micrometastases in lymph nodes, bone marrow and other tissues and for determining the origin of poorly differentiated tumors. There are two types of cytokeratins the acidic type I cytokeratins and the basic or neutral type II cytokeratins. Cytokeratins are usually found in pairs comprising a type I cytokeratin and a type II cytokeratin. Usually the type II cytokeratins are 8kD larger than their type I counterparts.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13248R)
Fournisseur:
Bioss
Description:
Heterotrimeric G proteins function to relay information from cell surface receptors to intracellular effectors (1). Each of a very broad range of receptors specifically detects an extracellular stimulus (a photon, pheromone, odorant, hormone or neurotransmitter) while the effectors (i.e., adenylyl cyclase), which act to generate one or more intracellular messengers, are less numerous. In mammals, G protein alpha, Beta and Gamma polypeptides are encoded by at least 16, 4 and 7 genes, respectively (2-5). Most interest in G proteins has been focused on their a subunits, since these proteins bind and hydrolyze GTP and most obviously regulate the activity of the best studied effectors. Four distinct classes of G alpha subunits have been identified; these include Gs, Gi, Gq and Ga 12/13 (3,4). The Gi class comprises all the known a subunits that are susceptible to pertussis toxin modifications, including Ga i-1, Ga i-2, Ga i-3, Ga o, Ga t1, Ga t2, Ga z and Ga gust (4). Of these, the three Ga i subtypes function to open atrial potassium channels (6). Ga 16 is a member of the Gq subfamily and is expressed specifically in hematopoietic cells (7).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11020R-HRP)
Fournisseur:
Bioss
Description:
Actin filament associated protein (AFAP-110) interacts directly with actin filaments through its C-terminal actin-binding domain. AFAP-110 contains additional protein-binding domains as well, and serves as an adaptor protein. By linking signaling molecules to actin filaments, AFAP-110 provides a platform for the preparation of larger signaling complexes, activates Src kinases in response to cellular signals and also directly affects Actin organization as an Actin filament cross-linking protein. AFAP-1L2 (Actin filament-associated protein 1-like 2), also known as XB130, is a 818 amino acid cytoplasmic protein that contains two Pleckstrin homology (PH) domains, which are normally found in proteins involved in intracellular signaling. Like its relative AFAP110, AFAP-1L2 interacts with Src kinase and may play a role in Src-regulated transcription activation. AFAP-1L2 is expressed in thyroid and spleen and can also be detected at lower levels in lung, brain, pancreas and kidney. There are four isoforms of AFAP-1L2 that are produced as a result of alternative splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BSENS-078-50)
Fournisseur:
Biosensis
Description:
Alpha synuclein is an abundant 140 amino acid neuronal protein, expressed primarily at presynaptic terminals in the central nervous system. Alpha synuclein has been associated with several neurodegenerative diseases. A point mutation in the gene coding for the alpha-synuclein protein was the first discovery linking this protein to a rare familial form of Parkinson's disease (PD). Subsequently, other mutations in the alpha-synuclein gene have been identified in familial PD. The aggregated proteinaceous inclusions called Lewy bodies found in PD and cortical Lewy body dementia (LBD) were discovered to be predominantly alpha-synuclein. Aberrant aggregation of alpha-synuclein has been detected in an increasing number of neurodegenerative diseases, collectively known as synucleopathies. Alpha-synuclein exists physiologically in both soluble and membrane-bound states, in unstructured and alpha-helical conformations, respectively. The physiological function of alpha-synuclein appears to require its translocation between these subcellular compartments and interconversion between the 2 conformations. Abnormal processing of alpha-synuclein is predicted to lead to pathological changes in its binding properties and function.
UOM:
1 * 50 µG
Numéro de catalogue:
(BOSSBS-7116R-A488)
Fournisseur:
Bioss
Description:
Ro autoantigens are of clinical significance because directed against them are found in most patients with primary Sjqgren syndrome, subacute cutaneous lupus erythematosus (SLE), neonatal lupus erythematosus, ANA-negative lupus erythematosus, and systemic lupus erythematosus-like disease secondary to homozygous C2 or C4 complement deficiency (1). Ro/SSA is a ribonucleoprotein that binds to auto in 35 to 50% of patients with SLE and in up to 97% of patients with Sjqgren syndrome (2). The Ro/SSA particle consists of a single immunoreactive protein noncovalently bound with one of four small RNA molecules (2). Most anti-Ro/SSA-positive sera detect not only the main protein, but also a smaller Ro/SSA protein (2). The genes which encode the smaller and larger proteins map to human chromosomes 11p15.5 and 1q31, respectively (3?). La/SSB is an autoimmune RNA-binding protein that plays a role in the transcription of RNA polymerase III was originally defined by its reactivity with auto from patients with Sjé°ƒren syndrome and SLE (6).
UOM:
1 * 100 µl
Fournisseur:
Biotium
Description:
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.
Fournisseur:
Biotium
Description:
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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