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Bioss
Numéro de catalogue:
(BOSSBS-1696R-CY5)
Fournisseur:
Bioss
Description:
Receptor for the cytotoxic ligand TNFSF10/TRAIL. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Promotes the activation of NF-kappa-B. Essential for ER stress-induced apoptosis (By similarity).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-0016R-CY5)
Fournisseur:
Bioss
Description:
Neuronal Marker Tyrosine hydroxylase is involved in the conversion of tyrosine to dopamine. As the rate-limiting enzyme in the synthesis of catecholamines, tyrosine hydroxylase has a key role in the physiology of adrenergic neurons. Tyrosine hydroxylase is regularly used as a marker for dopaminergic neurons, which is particularly relevant for research into Parkinson's disease.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5620R-FITC)
Fournisseur:
Bioss
Description:
Stat 5a protein is a transcription factor activated by hormone and cytokines. Two highly related, but distinct Stat 5 genes (Stat 5a and Stat 5b) were identified in mouse. The amino acid sequences of Stat 5a and Stat 5b show 96% sequence similarity, and both proteins are co expressed in most tissues of both virgin and lactating mice. However, differential accumulation of Stat 5a and Stat 5b mRNA has been reported for both muscle and mammary tissue. Stat 5a is critically involved in a variety of physiological functions, including reproduction, lactation, immune function and somatic growth.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1696R-CY3)
Fournisseur:
Bioss
Description:
Receptor for the cytotoxic ligand TNFSF10/TRAIL. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Promotes the activation of NF-kappa-B. Essential for ER stress-induced apoptosis (By similarity).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13035R-A680)
Fournisseur:
Bioss
Description:
Mitogen-activated protein (MAP) kinases are a large class of proteins involved in signal transduction pathways that are activated by a range of stimuli and mediate a number of physiological and pathological changes in the cell. Dual specificity phosphatases (DSPs) are a subclass of the protein tyrosine phosphatase (PTP) gene superfamily, which are selective for dephosphorylating critical phosphothreonine and phosphotyrosine residues within MAP kinases. DSP gene expression is induced by a host of growth factors and/or cellular stresses, thereby negatively regulating MAP kinase superfamily members including MAPK/ERK, SAPK/JNK and p38. MKP-5 preferentially binds to p38, but also to SAPK/JNK. It is ubiquitously expressed and localizes to both the cytoplasm and the nucleus. MKP-5 has been implicated in cell proliferation and apoptosis, tumor invasion and immune responses.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-2700R-FITC)
Fournisseur:
Bioss
Description:
Cytokeratin 10 is a heterotetramer of two type I and two type II keratins. Cytokeratin 10 is generally associated with keratin 1. It is seen in all suprabasal cell layers including stratum corneum. A number of alleles are known that mainly differ in the Gly-rich region (positions 490-560). Defects in cytokeratin 10 are a cause of epidermolytic hyperkeratosis (EHK), also known as bullous congenital ichthyosiform erythroderma (BCIE) or bullous erythroderma ichthyosiformis congenita of Brocq. EHK is an hereditary skin disorder characterized by blistering and a marked thickening of the stratum corneum. At birth, affected individuals usually present with redness, blisters and superficial erosions due to cytolysis. Within a few weeks, the erythroderma and blister formation diminish and hyperkeratoses develop. Transmission is autosomal dominant, but most cases are sporadic. Defects in cytokeratin 10 are also a cause of annular epidermolytic ichthyosis (AEI), also known as cyclic ichthyosis with epidermolytic hyperkeratosis. AEI resembles clinical and histologic features of both epidermolytic hyperkeratosis and ichthyosis bullosa of Siemens.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-0123R-A647)
Fournisseur:
Bioss
Description:
This is a receptor for the tachykinin neuropeptide substance K (neurokinin A). It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of affinity of this receptor to tachykinins is: substance K >neuromedin-K >substance P.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1827R-FITC)
Fournisseur:
Bioss
Description:
Interleukin 11 is a pleiotropic cytokine produced by mesenchymal-derived adherent cells. IL11 shares many functions of IL6 and LIF, including potentiation of megakaryocyte activity, enhancement of human myeloma cell proliferation, and enhancement of hepatic acute phase protein production.Interleukin 11 directly stimulates the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells, and induces megakaryocyte maturation resulting in increased platelet production. Clinically it is used to prevent severe thrombocytopenia and the reduction of the need for platelet transfusion following myelosuppressive chemotherapy.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-10380R-A680)
Fournisseur:
Bioss
Description:
The protein encoded by this gene belongs to the SMAD, a family of proteins similar to the gene products of the Drosophila gene 'mothers against decapentaplegic' (Mad) and the C. elegans gene Sma. SMAD proteins are signal transducers and transcriptional modulators that mediate multiple Signalling pathways. This protein mediates the signals of the bone morphogenetic proteins (BMPs), which are involved in a range of biological activities including cell growth, apoptosis, morphogenesis, development and immune responses. In response to BMP ligands, this protein can be phosphorylated and activated by the BMP receptor kinase. The phosphorylated form of this protein forms a complex with SMAD4, which is important for its function in the transcription regulation. This protein is a target for SMAD-specific E3 ubiquitin ligases, such as SMURF1 and SMURF2, and undergoes ubiquitination and proteasome-mediated degradation. Alternatively spliced transcript variants encoding the same protein have been observed.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-10037R-A350)
Fournisseur:
Bioss
Description:
This gene encodes a subunit of the transcription factor complex nuclear factor-kappa-B (NFkB). The NFkB complex is expressed in numerous cell types and functions as a central activator of genes involved in inflammation and immune function. The protein encoded by this gene can function as both a transcriptional activator or repressor depending on its dimerization partner. The p100 full-length protein is co-translationally processed into a p52 active form. Chromosomal rearrangements and translocations of this locus have been observed in B cell lymphomas, some of which may result in the formation of fusion proteins. There is a pseudogene for this gene on chromosome 18. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2013]
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-10381R-A488)
Fournisseur:
Bioss
Description:
The protein encoded by this gene belongs to the SMAD, a family of proteins similar to the gene products of the Drosophila gene 'mothers against decapentaplegic' (Mad) and the C. elegans gene Sma. SMAD proteins are signal transducers and transcriptional modulators that mediate multiple signaling pathways. This protein mediates the signals of the bone morphogenetic proteins (BMPs), which are involved in a range of biological activities including cell growth, apoptosis, morphogenesis, development and immune responses. In response to BMP ligands, this protein can be phosphorylated and activated by the BMP receptor kinase. The phosphorylated form of this protein forms a complex with SMAD4, which is important for its function in the transcription regulation. This protein is a target for SMAD-specific E3 ubiquitin ligases, such as SMURF1 and SMURF2, and undergoes ubiquitination and proteasome-mediated degradation. Alternatively spliced transcript variants encoding the same protein have been observed. [provided by RefSeq].
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3543R-A750)
Fournisseur:
Bioss
Description:
NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p15, NFKB1/p5, REL and NFKB2/p52 and the heterodimeric p65-p5 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p5 and p65-c-Rel complexes are transcriptional activators. The NF-kappa-B p65-p65 complex appears to be involved in invasin-mediated activation of IL-8 expression. The inhibitory effect of I-kappa-B upon NF-kappa-B the cytoplasm is exerted primarily through the interaction with p65. p65 shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappa-B complex. Associates with chromatin at the NF-kappa-B promoter region via association with DDX1.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3757R-A350)
Fournisseur:
Bioss
Description:
DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3699R-CY5)
Fournisseur:
Bioss
Description:
GPR15 is a probable chemokine receptor,its expression has been reported in CD4(+) T lymphocytes, alveolar macrophages, and the basal surface of the small intestinal epithelium. ESTs have been isolated from normal brain and kidney cancer libraries.This gene encodes a G protein-coupled receptor that acts as a chemokine receptor for human immunodeficiency virus type 1 and 2. The encoded protein localizes to the cell membrane. [provided by RefSeq, Nov 2012].
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3756R-A750)
Fournisseur:
Bioss
Description:
PPP1A is a serine/threonine protein phosphatase catalytic subunit that is essential for regulating cellular stress responses in eukaryotes. It binds to magnesium or manganese ions and exists as a monomer. It is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. PPP1A is involved in the regulation long term synaptic plasticity and may play an important role in dephosphorylating substrates such as Ca2+/calmodulin dependent protein kinase II.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11654R-A680)
Fournisseur:
Bioss
Description:
Bleomycin hydrolase (BMH) is a cytoplasmic cysteine peptidase that is highly conserved through evolution; however, the only known activity of the enzyme is metabolic inactivation of the glycopeptide bleomycin (BLM), an essential component of combination chemotherapy regimens for cancer. The protein contains the signature active site residues of the cysteine protease papain superfamily.
UOM:
1 * 100 µl
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