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Single-use+Temperature+Sensor
Numéro de catalogue:
(BOSSBS-6204R-CY3)
Fournisseur:
Bioss
Description:
NAP125, also known as NCKAP1 (NCK-associated protein 1), p125Nap1 or membrane-associated protein HEM-2, is a 1,128 amino acid single pass membrane protein that exists as two alternatively spliced isoforms and belongs to the HEM-1/HEM-2 family. While widely expressed, NAP125 is found at highest levels in heart, brain and skeletal muscle where it regulates Rac-dependent actin remodeling as part of a lamellipodial complex with WAVE2, Abi-1 and CYFIP1. NAP125 localizes to the cytoplasmic side of lamellipodium membrane and is encoded by a gene that maps to human chromosome 2q32.1 and mouse chromosome 2 C3. NAP125 expression is markedly reduced in Alzheimer disease (AD)-affected brains, suggesting a possible role in the disease.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13038R-A350)
Fournisseur:
Bioss
Description:
Dynamin I is a GTPase enzyme required for the retrieval of synaptic vesicles after exocytosis and functions in endocytosis by stimulating assembly of invaginating synaptic vesicles (1). Dynamin I is phosphorylated in nerve terminals exclusively in the cytosolic compartment and in vitro by protein kinase C (PKC) (2–5). The phosphorylation site in PKC-phosphorylated Dynamin I is a single site at Serine 795, which is located near a binding site for the SH3 domain of p85, the regulatory subunit of phosphatidylinositol 3-kinase (2–5). Dephosphorylation is required for synaptic vesicle retrieval, suggesting that phosphorylation affects the subcellular localization of Dynamin I (5). Mouse, rat and human Dynamin I are phosphorylated on serine residues, including Ser 778, by Cdk5, regulating PACSIN1 recruitment and enabling synaptic vesicle endocytosis.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-7546R-CY3)
Fournisseur:
Bioss
Description:
This gene encodes Lutheran blood group glycoprotein, a member of the immunoglobulin superfamily and a receptor for the extracellular matrix protein, laminin. The protein contains five extracellular immunoglobulin domains, a single transmembrane domain, and a short C-terminal cytoplasmic tail. This protein may play a role in epithelial cell cancer and in vaso-occlusion of red blood cells in sickle cell disease. Polymorphisms in this gene define some of the antigens in the Lutheran system and also the Auberger system. Inactivating variants of this gene result in the recessive Lutheran null phenotype, Lu(a-b-), of the Lutheran blood group. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, May 2012].
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12927R-A680)
Fournisseur:
Bioss
Description:
Cytochrome P450 proteins are heme-thiolate monooxygenases that mediate NADPH-dependent electron transport and function to oxidize a variety of structurally unrelated compounds, including steroids, fatty acids and xenobiotics. Specifically, Cytochrome P450s are responsible for metabolizing arachidonic acid to hydroxyeicosatetraenoic acid (a regulator of blood pressure) and epoxyeicosatrienoic acid (a molecule involved in Signalling events). CYP20A1 (cytochrome P450, family 20, subfamily A, polypeptide 1), also known as CYP-M, is a 462 amino acid single-pass membrane protein that belongs to the cytochrome P450 family. CYP20A1 is thought to carry its own oxygen as it lacks a conserved I-helix motif and one amino acid of its conserved heme binding site.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-10465R)
Fournisseur:
Bioss
Description:
Alpha-1-adrenergic receptors (alpha-1-ARs) are members of the G protein-coupled receptor superfamily. They activate mitogenic responses and regulate growth and proliferation of many cells. There are 3 alpha-1-AR subtypes: alpha-1A, -1B and -1D, all of which signal through the Gq/11 family of G-proteins and different subtypes show different patterns of activation. This gene encodes alpha-1B-adrenergic receptor, which induces neoplastic transformation when transfected into NIH 3T3 fibroblasts and other cell lines. Thus, this normal cellular gene is identified as a protooncogene. This gene comprises 2 exons and a single large intron of at least 20 kb that interrupts the coding region. [provided by RefSeq, Jul 2008].
UOM:
1 * 100 µl
Fournisseur:
Biotium
Description:
Recognizes a protein of 104 kDa-110 kDa, characterized as major vault protein (MVP). Vaults are large ribonucleoprotein particles (RNPs) present in all eukaryotic cells. They have a complex morphology, including several small molecules of RNA, but a single protein species. The MVP accounts for >70% of their mass. Their shape is reminiscent of the nucleopore central plug. Treatment of cells with estradiol increases the amount of MVP in nuclear extract. The hormone-dependent interaction of vaults with ER is prevented in vitro by sodium molybdate. Antibodies to estrogen, progesterone and glucocorticoid receptors are able to co-immunoprecipitate the MVP. MVP is overexpressed in many neoplastic tissues and cell lines. Expression of MVP predicts a poor response to chemotherapy.
Numéro de catalogue:
(BOSSBS-7692R-CY5.5)
Fournisseur:
Bioss
Description:
Relaxin is a peptide hormone produced by the corpora lutea of ovaries during pregnancy in many mammalian species, including man. The secretion of the hormone into the blood stream just before parturition results in a marked softening and lengthening of the pubic symphysis and a softening of the cervix, which facilitates the birth process. By inhibiting uterine contractions, relaxin may influence the timing of parturition. Like insulin, relaxin consists of two peptide chains, A and B, covalently linked by disulfide bonds. By further analogy to insulin, the two peptides are synthesized as a single-chain precursor polypeptide with the B chain at the NH2-terminus.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-7692R)
Fournisseur:
Bioss
Description:
Relaxin is a peptide hormone produced by the corpora lutea of ovaries during pregnancy in many mammalian species, including man. The secretion of the hormone into the blood stream just before parturition results in a marked softening and lengthening of the pubic symphysis and a softening of the cervix, which facilitates the birth process. By inhibiting uterine contractions, relaxin may influence the timing of parturition. Like insulin, relaxin consists of two peptide chains, A and B, covalently linked by disulfide bonds. By further analogy to insulin, the two peptides are synthesized as a single-chain precursor polypeptide with the B chain at the NH2-terminus.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11262R-CY5)
Fournisseur:
Bioss
Description:
MP21 is a member of the EMP24/GP25L/p24 cargo family of proteins that regulates vesicular trafficking in the early secretory pathway. TMP21 is a ubiquitously expressed single-pass type I membrane protein localizing to the Golgi cisternae and the plasma membrane. It contains one GOLD (Golgi dynamics) domain and participates in protein transport and quality control between the endoplasmic reticulum (ER) and the Golgi complex. In addition, TMP21 is a component of the heteromeric secretase complex (or Presenilin complex) and functions to regulate the ?secretase activity. Two isoforms, namely TMP21-I and TMP21-II, exist for this protein.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11239R-CY5)
Fournisseur:
Bioss
Description:
CREB3L3 is a 461 amino acid single-pass type II membrane protein that localizes to the endoplasmic reticulum (ER) and, in response to ER stress, is cleaved and translocated to the nucleus. Expressed exclusively in liver, CREB3L3 functions as a transcription factor that, during ER stress, is thought to activate genes that are involved in both the unfolded protein response and the acute phase response (APR). Additionally, CREB3L3 is underexpressed in hepatocellular carcinoma, suggesting a possible role as a tumor suppressor. CREB3L3 functions as a dimer and contains one leucine zipper domain, a KDEL-like sequence and a bZIP domain, through which it conveys its DNA binding ability. Three isoforms of CREB3L3 exist due to alternative splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-15458R-CY7)
Fournisseur:
Bioss
Description:
Hephaestin is a single-pass type I membrane protein that belongs to the multicopper oxidase family of proteins. Hephaestin, a copper-dependant ferroxidase protein, is crucial for iron exiting intestinal enterocytes into the circulation. It mediates the movement of iron across the basolateral membrane in conjunction with ferroportin 1. This is an important link between iron and copper metabolism in mammalian systems, as copper deficiency leads to reduced hephaestin and reduced iron absorption resulting in anemia. Hephaestin can bind six copper ions per monomer and is regulated by the homeobox transcription factor CDX2. Increased levels of iron leads to an increase in CDX2 expression and thus Hephaestin. Hephaestin is primarily detected in the intestine, but is also expressed in colon, breast, bone trabecural cells and fibroblasts.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13093R-A750)
Fournisseur:
Bioss
Description:
This gene is a member of the Tyr protein kinase family and the epidermal growth factor receptor subfamily. It encodes a single-pass type I membrane protein with multiple cysteine rich domains, a transmembrane domain, a tyrosine kinase domain, a phosphotidylinositol-3 kinase binding site and a PDZ domain binding motif. The protein binds to and is activated by neuregulins and other factors and induces a variety of cellular responses including mitogenesis and differentiation. Multiple proteolytic events allow for the release of a cytoplasmic fragment and an extracellular fragment. Mutations in this gene have been associated with cancer. Alternatively spliced variants which encode different protein isoforms have been described; however, not all variants have been fully characterized.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-0855R-CY7)
Fournisseur:
Bioss
Description:
Insulin is a pancreatic hormone that regulates glucose and is involved in the synthesis of protein and fat. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver. Heterodimer of a B chain and an A chain linked by two disulfide bonds.Belongs to the insulin family. The insulin-link growth factors, IGF-I and IGF-II (also desinated somatomedin C and multiplication stimulating activator, respectvely), share approximatly 76% sequence identity and are 50% related to pro-insulin.IGF-I and IGF-II are nonglycosylated, single chain proteins of 70 and 76 amino acids in length, respectivelly. IGF-I functions as an autocrine regulator of growth in vaious, whereas the function of IGF-II is less well defined.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5990R-A488)
Fournisseur:
Bioss
Description:
This gene encodes a member of the ALEX family of proteins which may play a role in tumor suppression. The encoded protein contains a potential N-terminal transmembrane domain and a single Armadillo (arm) repeat. Other proteins containing the arm repeat are involved in development, maintenance of tissue integrity, and tumorigenesis. This gene is closely localized with other family members on the X chromosome. Three transcript variants encoding the same protein have been identified for this gene. [provided by RefSeq, Jul 2008].
UOM:
1 * 100 µl
Fournisseur:
Biotium
Description:
Recognizes a protein of 185 kDa, which is identified as c-erbB-2/HER-2/neu. Its epitope is localized in the extracellular domain. C-erbB-2/HER-2 is a member of the EGFR family. This MAb is specific and shows minimal cross-reaction with other members of the EGFR-family. Receptors of this family are located on the plasma membrane and consist of an extracellular ligand-binding domain that is connected to a large intracellular domain by a single transmembrane sequence. c-erbB-2/HER-2 protein is over-expressed in a variety of carcinomas especially those of breast and ovary.
Fournisseur:
Biotium
Description:
Recognizes a protein of 185 kDa, which is identified as c-erbB-2/HER-2/neu. Its epitope is localized in the extracellular domain. C-erbB-2/HER-2 is a member of the EGFR family. This MAb is specific and shows minimal cross-reaction with other members of the EGFR-family. Receptors of this family are located on the plasma membrane and consist of an extracellular ligand-binding domain that is connected to a large intracellular domain by a single transmembrane sequence. c-erbB-2/HER-2 protein is over-expressed in a variety of carcinomas especially those of breast and ovary.
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