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acids+and+salts+high+purity
Numéro de catalogue:
(BOSSBS-11722R-A647)
Fournisseur:
Bioss
Description:
Neural crest cell migration to the third and fourth pharyngeal pouches is a critical step in the structural formation of organs that are affected in DiGeorge syndrome. DGCR6 (DiGeorge syndrome critical region 6) is a nuclear protein that plays a role in neural crest cell migration and is located at the DiGeorge syndrome critical region (DGCR) on chromosome 22. Expressed ubiquitously with highest levels in heart, liver and skeletal muscle, DGCR6 shares high homology with the Drosophila gonadal (gdl) protein and with human Laminin ?1, both of which are involved in early tissue development. The gene encoding DGCR6, along with other DGCR genes, is deleted in DiGeorge syndrome; a developmental disorder characterized by improper facial, cardiac and palate formation. Upregulation of DGCR6 is implicated in lung and colon adenocarcinomas, as well as in Burkitt抯 lymphoma and lymphocytes transformed by EBV. Due to a duplication of the ancestral DGCR6 locus, there are two functional, highly homologous copies of the DGCR6 gene (designated DGCR6 and DGCR6L) on chromosome 22.
UOM:
1 * 100 µl
Fournisseur:
Biotium
Description:
The epitope of this MAb is located between aa343-357. 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.
Numéro de catalogue:
(BNUM0193-50)
Fournisseur:
Biotium
Description:
Recognizes a protein of 70 kDa, which is identified as CD86 (HLDA V; WS Code BP BP072. HLDA V; WS Code A A109. HLDA VI; WS Code BP 95. HLDA VI; WS Code B CD86.9). CD86 is a type I transmembrane glycoprotein and a member of the immunoglobulin superfamily of cell surface receptors. It is expressed at high levels on resting peripheral monocytes and dendritic cells and at very low density on resting B and T lymphocytes. CD86 expression is rapidly upregulated by B cell specific stimuli with peak expression at 18 to 42 hours after stimulation. CD86, along with CD80/B71, is an important accessory molecule in T cell co-stimulation via its interaction with CD28 and CD152/CTLA4. Since CD86 has rapid kinetics of induction, it is believed to be the major CD28 ligand expressed early in the immune response. It is also found on malignant Hodgkin and Reed Sternberg (HRS) cells in Hodgkin's disease.
UOM:
1 * 50 µl
Numéro de catalogue:
(BOSSBS-11210R-A555)
Fournisseur:
Bioss
Description:
Dyneins are multisubunit, high molecular weight ATPases that interact with microtubules to generate force by converting the chemical energy of ATP into the mechanical energy of movement. Cytoplasmic or axonemal Dynein heavy, intermediate, light and light-intermediate chains are all components of minus end-directed motors; the complex transports cellular cargos towards the central region of the cell. Axonemal dynein motors contain one to three non-identical heavy chains and cause a sliding of microtubules in the axonemes of cilia and flagella in a mechanism necessary for cilia to beat and propel the cell. DNAH9 (Dynein, axonemal, heavy chain 9), also known as DYH9, HL20, DNEL1, Dnahc9 or DNAH17L, is a member of the Dynein heavy chain family and comprises one of the heavy chain subunits of axonemal Dynein. DNAH9 consists of an N-terminal stem which is responsible for interacting with other Dynein components and binding cargo, and four P-loops that comprise the motor domain at its C-terminus.
UOM:
1 * 100 µl
Fournisseur:
Biotium
Description:
The epitope of this MAb is located between aa343-357 (ELAI kDaNAKLSELE). 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.
Numéro de catalogue:
(BOSSBS-3619R-FITC)
Fournisseur:
Bioss
Description:
Talin, a multifunctional constituent of cell-substratum attachment sites, is a high molecular weight protein (225-270 kDa) found in variety of tissues and cell types. It is localized at a subset of adherens junctions, specialized cell-cell and cell-matrix associations that are characterized by the presence of filamentous actin at the cytoplasmic face of the junctional complex. In cultured cells, talin is absent from cell-cell junctions and found predominantly at adhesion plaques and in fibrillar streaks underlying cell surface fibronectin. Talin interacts with at least two other proteins that are localized at adhesion plaques, vinculin and integrin. Talin and vinculin have been shown to interact with each other and both have been proposed to be involved in generating the transmembrane connection, between the extracellular matrix and the cytoskeleton, that occurs at adhesion plaques. At physiological ionic strength, talin is an elongate, flexible, monomeric protein with the ability to self-associate into dimers at higher protein concentrations.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3619R-A647)
Fournisseur:
Bioss
Description:
Talin, a multifunctional constituent of cell-substratum attachment sites, is a high molecular weight protein (225-270 kDa) found in variety of tissues and cell types. It is localized at a subset of adherens junctions, specialized cell-cell and cell-matrix associations that are characterized by the presence of filamentous actin at the cytoplasmic face of the junctional complex. In cultured cells, talin is absent from cell-cell junctions and found predominantly at adhesion plaques and in fibrillar streaks underlying cell surface fibronectin. Talin interacts with at least two other proteins that are localized at adhesion plaques, vinculin and integrin. Talin and vinculin have been shown to interact with each other and both have been proposed to be involved in generating the transmembrane connection, between the extracellular matrix and the cytoskeleton, that occurs at adhesion plaques. At physiological ionic strength, talin is an elongate, flexible, monomeric protein with the ability to self-associate into dimers at higher protein concentrations.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-6991R-CY7)
Fournisseur:
Bioss
Description:
In mammalian cells, transcription is regulated in part by high molecular weight coactivating complexes that mediate signaling between transcriptional activators and initiation factors. These complexes include the thyroid hormone receptor-associated protein (TRAP) complex, which interacts with thyroid receptors (TR), vitamin D receptors and other steroid receptors to facilitate hormone induced transcriptional activation. The TRAP complex consists of numerous proteins ranging in size including TRAP95, TRAP100, TRAP150, TRAP220 and TRAP230, that are characterized by the presence of a nuclear receptor recognition motif which mediates the ligand-dependent binding of TRAP proteins to the nuclear receptors. TRAP220 and TRAP100 are widely expressed and most abundantly detected in skeletal muscle, heart and placenta. TRAP95, TRAP150 and TRAP230 facilitate TR induced transcription by associating with an additional transcriptional coactivating complex SMCC (SRB and MED protein cofactor complex), which consists of various subunits that share homology with several components of the yeast transcriptional mediator complexes.
UOM:
1 * 100 µl
Numéro de catalogue:
(664-0175)
Fournisseur:
VWR Collection
Description:
Cet instrument avec porte-électrodes articulé et boîtier de protection IP 43 offre une haute résolution et fiabilité pour des mesures précises. Sortie USB pour connexion à un ordinateur. Conforme aux BPL.
UOM:
1 * 1 SET
Numéro de catalogue:
(BOSSBS-0362R-CY3)
Fournisseur:
Bioss
Description:
Protein A is a 40-60 kDa surface protein originally found in the cell wall of the bacteria Staphylococcus aureus (SPA). SPA binds proteins from many of mammalian species, most notably IgGs, and helps inhibit phagocytic engulfment and acts as an immunological disguise via this type of interaction, thus the bacteria will disrupts opsonization and phagocytosis. SPA is known to bind with Fc region of immunoglobulins preferentially through interaction with the VH3 variable region of the heavy chain. SPA has been shown to bind with high affinity to human IgG1 and IgG2 as well as mouse IgG2a and IgG2b, whereas bind with moderate affinity to human IgM, IgA and IgE as well as mouse IgG3 and IgG1. SPA is often produced in E. coli and is practically coupled to other molecules such as enzymes, biotin, radioactive iodine for use in immunology and other biological research. SPA is also immobilized onto solid supports such as agarose beads for total IgG purifying or interest protein or protein complex identifying in immunoprecipitation studies.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11427R-CY3)
Fournisseur:
Bioss
Description:
In mammalian cells, transcription is regulated in part by high molecular weight coactivating complexes that mediate signals between transcriptional activators and RNA polymerase (1). These complexes include the SMCC (SRB and MED protein cofactor complex), which consists of various subunits that share homology with several components of the yeast transcriptional mediator complexes, and including the human proteins Srb7, Med6 (also designated DRIP33) and Med7 (also designated DRIP34) (2,3). SMCC associates with the RNAPII (RNA polymerase II) holoenzyme through Srb7 and, in turn, enhances gene-specific activation or repression induced by DNA-binding transcription factors (4). Med6 and Med7, as well as other components of SMCC, associate with coactivator proteins from the TRAP (thyroid hormone receptor-activating protein) complex and DRIP (for vitamin D receptor interacting protein) complex to facilitate steroid receptor dependent transcriptional activation (4,5). Additionally, SMCC associates with PC4 (positive cofactor 4) to repress basal transcription independent of RNAPII activity (6).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11907R-FITC)
Fournisseur:
Bioss
Description:
ATP-binding cassette (ABC) transporters are an evolutionarily conserved family of widely-expressed proteins that use ATP hydrolysis to catalyze the transport of various molecules across extracellular and intracellular membranes. As the largest family of transmembrane proteins, ABC genes comprise several subfamilies (ABC1, ABCA, ABCE, ABCF, MDR/TAP, MRP, ALD, OABP, GCN20 and White (also known as ABCG)). In bacteria, ABC transporters are used to import compunds that cannot be obtained by diffusion. Eukaryotic ABC transporters are largely responsible for trafficking hydrophobic compounds either within the cell as part of a metabolic process or outside the cell for transport to other organs, or for secretion from the body. ABCB9 (also designated Transporter associated with antigen processing (TAP)-like or TAPL) forms a homodimer, which is localized in lysosomes. It functions as an ATP-dependent peptide transporter that shows a broad peptide specificity ranging from 6-mer up to 59-mer peptides. ABCB9 transports these peptides with low affinity but high efficiency.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11907R-HRP)
Fournisseur:
Bioss
Description:
ATP-binding cassette (ABC) transporters are an evolutionarily conserved family of widely-expressed proteins that use ATP hydrolysis to catalyze the transport of various molecules across extracellular and intracellular membranes. As the largest family of transmembrane proteins, ABC genes comprise several subfamilies (ABC1, ABCA, ABCE, ABCF, MDR/TAP, MRP, ALD, OABP, GCN20 and White (also known as ABCG)). In bacteria, ABC transporters are used to import compunds that cannot be obtained by diffusion. Eukaryotic ABC transporters are largely responsible for trafficking hydrophobic compounds either within the cell as part of a metabolic process or outside the cell for transport to other organs, or for secretion from the body. ABCB9 (also designated Transporter associated with antigen processing (TAP)-like or TAPL) forms a homodimer, which is localized in lysosomes. It functions as an ATP-dependent peptide transporter that shows a broad peptide specificity ranging from 6-mer up to 59-mer peptides. ABCB9 transports these peptides with low affinity but high efficiency.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11907R-A647)
Fournisseur:
Bioss
Description:
ATP-binding cassette (ABC) transporters are an evolutionarily conserved family of widely-expressed proteins that use ATP hydrolysis to catalyze the transport of various molecules across extracellular and intracellular membranes. As the largest family of transmembrane proteins, ABC genes comprise several subfamilies (ABC1, ABCA, ABCE, ABCF, MDR/TAP, MRP, ALD, OABP, GCN20 and White (also known as ABCG)). In bacteria, ABC transporters are used to import compunds that cannot be obtained by diffusion. Eukaryotic ABC transporters are largely responsible for trafficking hydrophobic compounds either within the cell as part of a metabolic process or outside the cell for transport to other organs, or for secretion from the body. ABCB9 (also designated Transporter associated with antigen processing (TAP)-like or TAPL) forms a homodimer, which is localized in lysosomes. It functions as an ATP-dependent peptide transporter that shows a broad peptide specificity ranging from 6-mer up to 59-mer peptides. ABCB9 transports these peptides with low affinity but high efficiency.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3147R-CY5)
Fournisseur:
Bioss
Description:
CD135 is a tyrosine kinase receptor expressed on normal cells including CD34+ hematopoietic stem cells, myelomonocytic progenitors, primitive B cell progenitors, and thymocytes. CD135 is also expressed on malignant hematopoietic cells including AML, ALL and CML BC. CD135, also known as FMS-like tyrosine kinase 3, FLT3, STK1, and Flk2, is a growth factor receptor that binds the FLT3 ligand to promote the growth and differentiation of primitive hematopoietic cells. The intracytoplasmic domain of CD135 is modified by phosphorylation and has been shown to interact with Grb2, SOCS1, VAV1, and Shc. In humans, expression of Flt3 is restricted to subsets of CD34 positive as well as CD34 negative normal bone marrow cells. In these cells, the level of expression of Flt3 is rather low. Most of the CD34 bright Flt3+ cells co-express CD117 at high levels. They may represent early cycling, but not quiescent stem cells. Flt3+ cells in the CD34lo and CD34- populations do not co-express CD117 molecule and may represent B lymphoid precursors.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11427R-A350)
Fournisseur:
Bioss
Description:
In mammalian cells, transcription is regulated in part by high molecular weight coactivating complexes that mediate signals between transcriptional activators and RNA polymerase (1). These complexes include the SMCC (SRB and MED protein cofactor complex), which consists of various subunits that share homology with several components of the yeast transcriptional mediator complexes, and including the human proteins Srb7, Med6 (also designated DRIP33) and Med7 (also designated DRIP34) (2,3). SMCC associates with the RNAPII (RNA polymerase II) holoenzyme through Srb7 and, in turn, enhances gene-specific activation or repression induced by DNA-binding transcription factors (4). Med6 and Med7, as well as other components of SMCC, associate with coactivator proteins from the TRAP (thyroid hormone receptor-activating protein) complex and DRIP (for vitamin D receptor interacting protein) complex to facilitate steroid receptor dependent transcriptional activation (4,5). Additionally, SMCC associates with PC4 (positive cofactor 4) to repress basal transcription independent of RNAPII activity (6).
UOM:
1 * 100 µl
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