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mycoplasma+detection
Numéro de catalogue:
(BOSSBS-9474R-A555)
Fournisseur:
Bioss
Description:
Members of the NFAT (nuclear factor of activated T cells) family of transcription factors are related to NFkB/Rel proteins and form cooperative complexes with the AP-1 proteins, Fos and Jun, on DNA to regulate cytokine expression in T cells. NFAT proteins are widely expressed and alternatively modified to generate splice variants, and they are localized to both the cytosol (NFATc) and to the nucleus (NFATn). NFAT1, NFAT2, and NFAT4 are predominantly expressed in immune cells, and NFAT2 and NFAT3 are expressed at high levels in cardiac tissues. In addition to activating cytokine gene transcription, NFAT2 is also implicated in cardiac valve development, and NFAT3 is involved in cardiac hypertrophy. NFAT5 is detected in both immune and nonimmune cells and, like other NFAT proteins, contains a highly conserved Rel-like binding domain that mediates NFAT proteins associating with specific consensus sequences on DNA. NFAT proteins are activated by increases in intracellular calcium, which leads to the calmodulin-dependent phosphatase, calcineurin, dephosphorylating NFAT proteins. This activating event induces a conformational change in the protein structure that exposes the nuclear localization signal and facilitates the translocation of NFAT proteins from the cytosol into the nucleus.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13248R-A680)
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
Fournisseur:
Tonbo Biosciences
Description:
The PK136 antibody is specific for mouse NK1.1, a type II transmembrane lectin-like receptor and member of the killer cell lectin-like receptor (KLR) family. NK1.1 is prominently expressed on natural killer (NK) cells, and is correlated with NK cytotoxic effects toward virus-infected cells and tumor cells. NK1.1 is expressed on subsets of NKT cells in certain mouse strains (C57BL/6, FVB/N, and NZB), yet absent from others (AKR, BALB/c, CBA/J, C3H, DBA/1, DBA/2, NOD, SJL, and 129). Putative subsets of NK cells and their expression of NK1.1 antigen are of continuing interest, including NK1.1+/CD117+ (c-Kit) cells reported to be immunosuppressive for CD8+ T cells in a mechanism involving PD-1 and PD-L1 (Ehlers et al. 2012. Endocrinology. 10: 1247). The PK136 antibody may be used for detection of NK1.1 expression on mouse strains including CE, B6, NZB, C58, Ma/My, ST, SJL, and FVB. The antibody is reported to react with an epitope common to NKR-P1B and NKR-P1C alloantigenic forms of NK1.1 (Carlyle et al. 2006. J. Immunol. 176: 7511-7524).
Fournisseur:
Biotium
Description:
This MAb is specific to Complement 4d (C4d) and it reacts with the secreted as well as cell-bound C4d.C4d is a degradation product of the activated complement factor C4b. Complement 4b is typically activated by binding of Abs to specific target molecules. Following activation and degradation of the C4 molecule, thio-ester groups are exposed, which allow transient, covalent binding of the degradation product Complement 4d to endothelial cell surfaces and extracellular matrix components of vascular basement membranes near the sites of C4 activation. The presence of C4d in peritubular capillaries is a key indicator for acute humoral (i.e. antibody-mediated) rejection of kidney, heart, pancreas and lung allografts. As an established marker of antibody-mediated acute renal allograft rejection and its proclivity for endothelium, this component can be detected in peritubular capillaries in chronic renal allograft rejection as well as hyperacute rejection, acute vascular rejection, acute cellular rejection, and borderline rejection. It has been shown to be a significant predictor of transplant kidney graft survival. Anti-C4d, combined with anti-C3d, can be utilized as a tool for diagnosis of allograft rejection that may warrant a prompt and aggressive anti-rejection treatment.
Fournisseur:
Biotium
Description:
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.
Numéro de catalogue:
(BOSSBS-13492R-FITC)
Fournisseur:
Bioss
Description:
The Golgi apparatus is a highly complex organelle comprised of a stack of cisternal membranes on the secretory pathway from the ER to the cell surface. The structure is maintained by an exoskeleton or Golgi matrix constructed from a family of coiled-coil protein, the golgins and other peripheral membrane components such as GRASP55 and GRASP65 (1). GRASP55 (Golgi reassembly stacking protien or p59) is a component of the Golgi stacking machinery. GRASP55 is highly homologous to GRASP65 and contains two PDZ domains. GRASP55 is myristoylated and palmitoylated. Unlike GRASP65, GRASP55 does not have detectable binding with the vesicle docking protein GM130 and is located on the medial-Golgi rather than cis-Golgi. Both GRASP55 and GRASP65 function in the stacking of Golgi Cisternae (2,3). The novel coiled-coil protein golgin 45 interacts with GRASP55 and the GTP form of Rab 2, suggesting that GRASP55 and golgin 45 form a Rab 2 effector complex on medial-Golgi essential for normal protein transport and Golgi structure (4). ERK2 directly phosphorylates GRASP55, which is phosphorylated in mitotic cells, suggesting that mitogen-activated protein kinase kinase (MKK)/ERK pathway phosphorylates the Golgi during mitosis (5).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13492R-A555)
Fournisseur:
Bioss
Description:
The Golgi apparatus is a highly complex organelle comprised of a stack of cisternal membranes on the secretory pathway from the ER to the cell surface. The structure is maintained by an exoskeleton or Golgi matrix constructed from a family of coiled-coil protein, the golgins and other peripheral membrane components such as GRASP55 and GRASP65 (1). GRASP55 (Golgi reassembly stacking protien or p59) is a component of the Golgi stacking machinery. GRASP55 is highly homologous to GRASP65 and contains two PDZ domains. GRASP55 is myristoylated and palmitoylated. Unlike GRASP65, GRASP55 does not have detectable binding with the vesicle docking protein GM130 and is located on the medial-Golgi rather than cis-Golgi. Both GRASP55 and GRASP65 function in the stacking of Golgi Cisternae (2,3). The novel coiled-coil protein golgin 45 interacts with GRASP55 and the GTP form of Rab 2, suggesting that GRASP55 and golgin 45 form a Rab 2 effector complex on medial-Golgi essential for normal protein transport and Golgi structure (4). ERK2 directly phosphorylates GRASP55, which is phosphorylated in mitotic cells, suggesting that mitogen-activated protein kinase kinase (MKK)/ERK pathway phosphorylates the Golgi during mitosis (5).
UOM:
1 * 100 µl
Numéro de catalogue:
(BNUM0204-50)
Fournisseur:
Biotium
Description:
This MAb is specific to Complement 4d (C4d) and it reacts with the secreted as well as cell-bound C4d.C4d is a degradation product of the activated complement factor C4b. Complement 4b is typically activated by binding of Abs to specific target molecules. Following activation and degradation of the C4 molecule, thio-ester groups are exposed, which allow transient, covalent binding of the degradation product Complement 4d to endothelial cell surfaces and extracellular matrix components of vascular basement membranes near the sites of C4 activation. The presence of C4d in peritubular capillaries is a key indicator for acute humoral (i.e. antibody-mediated) rejection of kidney, heart, pancreas and lung allografts. As an established marker of antibody-mediated acute renal allograft rejection and its proclivity for endothelium, this component can be detected in peritubular capillaries in chronic renal allograft rejection as well as hyperacute rejection, acute vascular rejection, acute cellular rejection, and borderline rejection. It has been shown to be a significant predictor of transplant kidney graft survival. Anti-C4d, combined with anti-C3d, can be utilized as a tool for diagnosis of allograft rejection that may warrant a prompt and aggressive anti-rejection treatment.
UOM:
1 * 50 µl
Numéro de catalogue:
(BOSSBS-12093R-CY7)
Fournisseur:
Bioss
Description:
Cyclic nucleotide-gated (CNG) cation channels are heteromeric complexes made up of principal alpha and modulatory beta subunits (1,2). The alpha subunits consist of CNG1-3 and form functional cation channels by themselves (1,2). The beta subunits consist of CNG4-6 and, unlike the alpha subunits, do not form functional channels, but rather modify the properties of channels (1,2). CNG channels are essential components of olfactory and visual transduction (1,2). In olfactory neurons, CNG2, CNG4.3 and CNG5 form Ca2+ permeable channels, which open and depolarize the cell in response to cAMP (1-3). In rod photoreceptors, CNG1 and CNG4.1 combine to form Ca ion permeable channels, which give rise to a current in response to cGMP (1-3). CNG3 and CNG6 are expressed in cone receptors and may combine to form a native cGMP-activated channel (2,3). CNG channels have been implicated in other areas (4-6). CNG1 is also expressed in medium-sized and small-sized arteries, suggesting a role for CNG in the regulation of arterial blood pressure and of blood supply to different regions (4). CNG1, CNG4.1 and CNG4.2 have been detected in the rat pineal gland (5). CNG2, CNG4.3 and CNG5 are present in GT1 cell lines and may play a role in the secretion of gonadotropin-releasing hormone (6).
UOM:
1 * 100 µl
Fournisseur:
PATHOGEN DETECTION SYSTEMS
Description:
The TECTA™ B16 and TECTA™ B4 are complete, self-contained automated microbiology testing systems for water quality capable of producing laboratory grade results with unprecedented 'time-to-result' performance. Tests can be inititated at any time, with automatic reporting of results that are sent directly via email notification to any device immediately upon detection.
Fournisseur:
Biotium
Description:
PAb122 binds to the C-terminus (aa370-378) of both wild type and mutated p53. When microinjected into nuclei, PAb122 blocked re-entry into the S-phase of the cell cycle. Mutation and/or allelic loss of p53 is one of the causes of a variety of mesenchymal and epithelial tumors. If it occurs in the germ line, such tumors run in families. p53 Binds to a DNA consensus sequence, the p53 response element, and it regulates normal cell growth cycle events by activating transcription of genes, involved either in progression through the cycle, or causing arrest in G1 when the genome is damaged. In most transformed and tumor cells the concentration of p53 is increased 51000 fold over the minute concentrations (1000 molecules cell) in normal cells, principally due to the increased half-life (4 h) compared to that of the wild-type (20 min). p53 Localizes in the nucleus, but is detectable at the plasma membrane during mitosis and when certain mutations modulate cytoplasmic/nuclear distribution. p53 Is the most commonly mutated gene in spontaneously occurring human cancers. Mutations arise with an average frequency of 70% but incidence varies from zero in carcinoid lung tumors to 97% in primary melanomas. High concentrations of p53 protein are transiently expressed in human epidermis and superficial dermal fibroblasts following mild ultraviolet irradiation.
Numéro de catalogue:
(BOSSBS-1913R-A555)
Fournisseur:
Bioss
Description:
Matrix Metalloproteinase 8 (MMP8) is also known as neutrophil collagenase and collagenase 2. MMP8 degrades fibrillar collagens types I, II, III, aggrecan, serpins and alpha 2 macroglobulin. All collagenases cleave fibrillar collagens at one specific site resulting in generation of N terminal three quarter and C terminal one quarter fragments, which then denature to gelatin at body temperature. The substrate specificity of collagenases is variable: MMP1 degrades type III collagen more efficiently than type I or type II collagen, whereas MMP8 is more potent in degrading type I collagen than type III or type II collagen. MMP13, in turn degrades type II collagen 6 fold more efficiently than type I and type II collagens and displays almost 50 fold stronger gelatinolytic activity than MMP1 and MMP8. MMP8 is very similar to MMP1, sharing 57 % amino acid identity. Most cell types do not produce MMP8. Until recently, it was thought that MMP8 was produced exclusively by neutrophils, but it has also been detected in other cell types including arthritic chondrocytes and gingival fibroblasts. The human MMP8 gene has the chromosomal location of 11q22.2-22.3. MMP8 is heavily glycosylated, and the zymogen has a mass of 85 Kd. The zymogen is quickly activated to the 64 Kd form, and this breaks down to a cascade of active forms.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1913R-HRP)
Fournisseur:
Bioss
Description:
Matrix Metalloproteinase 8 (MMP8) is also known as neutrophil collagenase and collagenase 2. MMP8 degrades fibrillar collagens types I, II, III, aggrecan, serpins and alpha 2 macroglobulin. All collagenases cleave fibrillar collagens at one specific site resulting in generation of N terminal three quarter and C terminal one quarter fragments, which then denature to gelatin at body temperature. The substrate specificity of collagenases is variable: MMP1 degrades type III collagen more efficiently than type I or type II collagen, whereas MMP8 is more potent in degrading type I collagen than type III or type II collagen. MMP13, in turn degrades type II collagen 6 fold more efficiently than type I and type II collagens and displays almost 50 fold stronger gelatinolytic activity than MMP1 and MMP8. MMP8 is very similar to MMP1, sharing 57 % amino acid identity. Most cell types do not produce MMP8. Until recently, it was thought that MMP8 was produced exclusively by neutrophils, but it has also been detected in other cell types including arthritic chondrocytes and gingival fibroblasts. The human MMP8 gene has the chromosomal location of 11q22.2-22.3. MMP8 is heavily glycosylated, and the zymogen has a mass of 85 Kd. The zymogen is quickly activated to the 64 Kd form, and this breaks down to a cascade of active forms.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-4202R)
Fournisseur:
Bioss
Description:
Activates Rho-GTPases by promoting the exchange of GDP for GTP. May be involved in epithelial barrier permeability, cell motility and polarization, dendritic spine morphology, antigen presentation, leukemic cell differentiation, cell cycle regulation, innate immune response, and cancer. Binds Rac-GTPases, but does not seem to promote nucleotide exchange activity toward Rac-GTPases, which was uniquely reported in PubMed:9857026. May stimulate instead the cortical activity of Rac. Inactive toward CDC42, TC10, or Ras-GTPases. Forms an intracellular sensing system along with NOD1 for the detection of microbial effectors during cell invasion by pathogens. Required for RHOA and RIP2 dependent NF-kappaB signaling pathways activation upon S.flexneri cell invasion. Involved not only in sensing peptidoglycan (PGN)-derived muropeptides through NOD1 that is independent of its GEF activity, but also in the activation of NF-kappaB by Shigella effector proteins (IpgB2 and OspB) which requires its GEF activity and the activation of RhoA. Involved in innate immune signaling transduction pathway promoting cytokine IL6/interleukin-6 and TNF-alpha secretion in macrophage upon stimulation by bacterial peptidoglycans; acts as a signaling intermediate between NOD2 receptor and RIPK2 kinase. Contributes to the tyrosine phosphorylation of RIPK2 through Src tyrosine kinase leading to NF-kappaB activation by NOD2.
UOM:
1 * 100 µl
Numéro de catalogue:
(181-0332)
Fournisseur:
VACUUBRAND
Description:
The CVC 3000 detect compact vacuum controller complete with integral vacuum valve and sensor is ready to use either as a bench top or stand mounted unit. The CVC 3000 detect is a compact two-point vacuum regulator, with integrated ceramic vacuum sensor and ventilation valve. The "detect" function provides the ability to recognise and find the boiling pressure and thus greatly facilitates the work of solvent evaporation. With integrated non-return valve and chemistry vacuum valve, it forms a highly compact and easy-to-install unit for vacuum regulation. Used in conjunction with existing vacuum pumps or networks, process efficiency is significantly increased through the "detect" electronic vacuum control, the solvent recovery is increased and the environment better protected. The programmable CVC 3000 detect is available for both bench top and stand mounting operation.
UOM:
1 * 1 ST
Fournisseur:
Dräger
Description:
Pour la mesure des « concentrations ponctuelles » du toluène. Les utilisations comprennent la détermination et la mesure des pics de concentration, la mesure de l'exposition personnelle dans la zone d'inhalation, la détection des fuites, par exemple dans les pipelines ou les installations gazières, et l'analyse de l'air dans les orifices d'évacuation, les tiges et les espaces confinés.
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