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mycoplasma+detection
Numéro de catalogue:
(BOSSBS-13247R-CY5)
Fournisseur:
Bioss
Description:
Heterotrimeric G proteins function to relay information from cell surface receptors to intracellular effectors. 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., adenyl 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. Most interest in G proteins has been focused on their Alpha 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 G Alpha s, G Alpha i, G Alpha q and G Alpha 12/13. The two members of the fourth class of G Alpha subunit proteins, G Alpha 12 and G Alpha 13, are insensitive to ADP-ribosylation by pertussis toxin, share 67% identity with each other and less than 45% identity with other G Alpha subunits and are widely expressed in a broad range of tissues.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12297R-A647)
Fournisseur:
Bioss
Description:
Pbx 1, 2, 3 and 4 are members of the TALE (three amino acid loop extension) family of homeodomain-containing proteins. Human pre-B cell acute leukemias are frequently associated with a t(1;19)(q23;p13.3) chromosomal rearrangement, which creates a chimeric gene encoding a fusion between the E2A and Pbx 1 gene products. Pbx 2 and Pbx 3 share 92% and 94% respective identities with Pbx 1 over a 266 amino acid region flanking their homeobox domains, while all three proteins are quite divergent at their amino- and carboxy-termini. Two forms of Pbx 1 and Pbx 3 each differ primarily in their carboxy-termini and result from alternative mRNA splicing. Unlike other homeotic selector genes which are expressed transiently during development and differentiation, Pbx gene transcripts are ubiquitously expressed in both fetal and adult tissues and cell lines. Additionally, Pbx 2 and Pbx 3 transcripts are detected in lymphoid cells, which do not express Pbx 1. Pbx 4 expression is confined to the testis, especially to spermatocytes in the pachytene stage of the first meiotic prophase.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12298R-CY7)
Fournisseur:
Bioss
Description:
Pbx 1, 2, 3 and 4 are members of the TALE (three amino acid loop extension) family of homeodomain-containing proteins. Human pre-B cell acute leukemias are frequently associated with a t(1;19)(q23;p13.3) chromosomal rearrangement, which creates a chimeric gene encoding a fusion between the E2A and Pbx 1 gene products. Pbx 2 and Pbx 3 share 92% and 94% respective identities with Pbx 1 over a 266 amino acid region flanking their homeobox domains, while all three proteins are quite divergent at their amino- and carboxy-termini. Two forms of Pbx 1 and Pbx 3 each differ primarily in their carboxy-termini and result from alternative mRNA splicing. Unlike other homeotic selector genes which are expressed transiently during development and differentiation, Pbx gene transcripts are ubiquitously expressed in both fetal and adult tissues and cell lines. Additionally, Pbx 2 and Pbx 3 transcripts are detected in lymphoid cells, which do not express Pbx 1. Pbx 4 expression is confined to the testis, especially to spermatocytes in the pachytene stage of the first meiotic prophase.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12298R-FITC)
Fournisseur:
Bioss
Description:
Pbx 1, 2, 3 and 4 are members of the TALE (three amino acid loop extension) family of homeodomain-containing proteins. Human pre-B cell acute leukemias are frequently associated with a t(1;19)(q23;p13.3) chromosomal rearrangement, which creates a chimeric gene encoding a fusion between the E2A and Pbx 1 gene products. Pbx 2 and Pbx 3 share 92% and 94% respective identities with Pbx 1 over a 266 amino acid region flanking their homeobox domains, while all three proteins are quite divergent at their amino- and carboxy-termini. Two forms of Pbx 1 and Pbx 3 each differ primarily in their carboxy-termini and result from alternative mRNA splicing. Unlike other homeotic selector genes which are expressed transiently during development and differentiation, Pbx gene transcripts are ubiquitously expressed in both fetal and adult tissues and cell lines. Additionally, Pbx 2 and Pbx 3 transcripts are detected in lymphoid cells, which do not express Pbx 1. Pbx 4 expression is confined to the testis, especially to spermatocytes in the pachytene stage of the first meiotic prophase.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12295R-FITC)
Fournisseur:
Bioss
Description:
Pbx 1, 2, 3 and 4 are members of the TALE (three amino acid loop extension) family of homeodomain-containing proteins. Human pre-B cell acute leukemias are frequently associated with a t(1;19)(q23;p13.3) chromosomal rearrangement, which creates a chimeric gene encoding a fusion between the E2A and Pbx 1 gene products. Pbx 2 and Pbx 3 share 92% and 94% respective identities with Pbx 1 over a 266 amino acid region flanking their homeobox domains, while all three proteins are quite divergent at their amino- and carboxy-termini. Two forms of Pbx 1 and Pbx 3 each differ primarily in their carboxy-termini and result from alternative mRNA splicing. Unlike other homeotic selector genes which are expressed transiently during development and differentiation, Pbx gene transcripts are ubiquitously expressed in both fetal and adult tissues and cell lines. Additionally, Pbx 2 and Pbx 3 transcripts are detected in lymphoid cells, which do not express Pbx 1. Pbx 4 expression is confined to the testis, especially to spermatocytes in the pachytene stage of the first meiotic prophase.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12295R-A555)
Fournisseur:
Bioss
Description:
Pbx 1, 2, 3 and 4 are members of the TALE (three amino acid loop extension) family of homeodomain-containing proteins. Human pre-B cell acute leukemias are frequently associated with a t(1;19)(q23;p13.3) chromosomal rearrangement, which creates a chimeric gene encoding a fusion between the E2A and Pbx 1 gene products. Pbx 2 and Pbx 3 share 92% and 94% respective identities with Pbx 1 over a 266 amino acid region flanking their homeobox domains, while all three proteins are quite divergent at their amino- and carboxy-termini. Two forms of Pbx 1 and Pbx 3 each differ primarily in their carboxy-termini and result from alternative mRNA splicing. Unlike other homeotic selector genes which are expressed transiently during development and differentiation, Pbx gene transcripts are ubiquitously expressed in both fetal and adult tissues and cell lines. Additionally, Pbx 2 and Pbx 3 transcripts are detected in lymphoid cells, which do not express Pbx 1. Pbx 4 expression is confined to the testis, especially to spermatocytes in the pachytene stage of the first meiotic prophase.
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-11020R)
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-075-50)
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:
(BNUM0712-50)
Fournisseur:
Biotium
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.
UOM:
1 * 50 µl
Fournisseur:
Tonbo Biosciences
Description:
The HIB19 antibody reacts with human CD19, a 95 kDa glycoprotein which acts as a co-receptor, along with CD21, CD81 and CD225, in support of the functional B cell receptor (BCR). This complex provides antigen-specific recognition and subsequent activation of B cells to proliferate and differentiate into antibody-secreting cells (plasma cells) or memory B cells, which are crucial for secondary antigen encounter. CD19 is a lineage-differentiation marker, as its expression is detectable at the earliest B cell stages, through development, and is finally lost upon transition to mature plasma cells.
Fournisseur:
Biotium
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.
Numéro de catalogue:
(BNUM0713-50)
Fournisseur:
Biotium
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.
UOM:
1 * 50 µl
Numéro de catalogue:
(BOSSBS-13247R-HRP)
Fournisseur:
Bioss
Description:
Heterotrimeric G proteins function to relay information from cell surface receptors to intracellular effectors. 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., adenyl 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. Most interest in G proteins has been focused on their Alpha 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 G Alpha s, G Alpha i, G Alpha q and G Alpha 12/13. The two members of the fourth class of G Alpha subunit proteins, G Alpha 12 and G Alpha 13, are insensitive to ADP-ribosylation by pertussis toxin, share 67% identity with each other and less than 45% identity with other G Alpha subunits and are widely expressed in a broad range of tissues.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13248R-FITC)
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-11059R-HRP)
Fournisseur:
Bioss
Description:
Netrin proteins are a family of laminin-related secreted proteins that provide guidance signals for axonal growth and cell migration during development. Netrin signaling is dependent on the concentration of calcium outside the cell and the level of PKA activity. In axonal cells, a reduction in PKA activity converts the responsiveness of the axons to the netrin proteins as the cells are repelled, rather than attracted, by the netrin gradient. Neogenin serves as the primary guidance receptor for netrin-3. Netrin-2 and the corresponding mouse homolog netrin-3 are expressed primarily in the lower two-thirds of the spinal cord, and, like netrin-1, they can either attract or repel commissural axons at a distance. Netrin-3 proteins are associated with the axon fibers projecting from motor neurons and from neurons within sympathetic and sensory ganglia, suggesting that netrin-3 may be involved in pathfinding and fasciculation of axon projection. Neogenin serves as the primary guidance receptor for netrin-3. During peripheral nerve development, high netrin-3 expression has been detected in mesenchymal cells, sensory ganglia and muscles. In humans, the gene encoding for the netrin-3 protein is localized to chromosome 16p13.3.
UOM:
1 * 100 µl
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