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Single-use+Pressure+Sensor
Numéro de catalogue:
(BOSSBS-11224R-A647)
Fournisseur:
Bioss
Description:
DNA damage or incomplete replication of DNA results in the inhibition of cell cycle progression at the G1 to S or the G2 to M phase transition by conserved regulatory mechanisms known as cell cycle checkpoints. Checkpoint proteins include Rad17, which is involved in regulating cell cycle progression at the G1 checkpoint as well as Chk1, Chk2, Rad1, Rad9 and Hus1, which are involved in regulating cell cycle arrest at the G2 checkpoint. In response to DNA damage, ATM and ATR kinases are important for cell cycle checkpoint response signalling. ATR-interacting protein (ATRIP), also designated ATM and Rad3-related-interacting protein, is required for checkpoint signaling after DNA damage. It is also important for ATR expression, which regulates DNA replication and damage checkpoint responses. ATRIP is a ubiquitously expressed protein that can form heterodimers with ATR. After dimerization they bind the RPA complex and are recruited to single stranded DNA. ATRIP is a nuclear protein that may also play a role in protein stabilization.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-9301R-CY7)
Fournisseur:
Bioss
Description:
SAS-6 (spindle assembly abnormal protein 6 homolog, HsSAS-6) is a 657 amino acid protein encoded by the human gene SAS6. SAS-6 is a component of the centrosome that contains one PISA (present in SAS-6) domain. LK4, SAS-6, CPAP and other centriole related proteins are required at different stages of procentriole formation and were associated with different centriolar structures. SAS-6 associates only transiently with nascent procentrioles, whereas CEP135 and CPAP form a core structure within the proximal lumen of both parental and nascent centrioles. SAS-6 is necessary for procentriole formation in human cell lines and is localized asymmetrically next to the centriole at the onset of procentriole formation. SAS-6 levels oscillate during the cell cycle; it is degraded in mitosis starting at anaphase, and it accumulates again at the end of the following G1 phase. The anaphase-promoting complex targets SAS-6 for degradation by the 26S Proteasome, and a KEN box in the C-terminus of SAS-6 is necessary for its degradation. Increased SAS-6 levels promoted the formation of multiple procentrioles forming next to a single centriole.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-7116R-A680)
Fournisseur:
Bioss
Description:
Ro autoantigens are of clinical significance because directed against them are found in most patients with primary Sjqgren syndrome, subacute cutaneous lupus erythematosus (SLE), neonatal lupus erythematosus, ANA-negative lupus erythematosus, and systemic lupus erythematosus-like disease secondary to homozygous C2 or C4 complement deficiency (1). Ro/SSA is a ribonucleoprotein that binds to auto in 35 to 50% of patients with SLE and in up to 97% of patients with Sjqgren syndrome (2). The Ro/SSA particle consists of a single immunoreactive protein noncovalently bound with one of four small RNA molecules (2). Most anti-Ro/SSA-positive sera detect not only the main protein, but also a smaller Ro/SSA protein (2). The genes which encode the smaller and larger proteins map to human chromosomes 11p15.5 and 1q31, respectively (3?). La/SSB is an autoimmune RNA-binding protein that plays a role in the transcription of RNA polymerase III was originally defined by its reactivity with auto from patients with Sjren syndrome and SLE (6).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-10493R-A488)
Fournisseur:
Bioss
Description:
Ubiquitin, a highly conserved protein that has a major role in targeting cellular proteins for degradation by the 26S proteosome, is synthesized as a precursor protein consisting of either polyubiquitin chains or a single ubiquitin fused to an unrelated protein. This gene encodes a fusion protein consisting of ubiquitin at the N terminus and ribosomal protein S27a at the C terminus. When expressed in yeast, the protein is post-translationally processed, generating free ubiquitin monomer and ribosomal protein S27a. Ribosomal protein S27a is a component of the 40S subunit of the ribosome and belongs to the S27AE family of ribosomal proteins. It contains C4-type zinc finger domains and is located in the cytoplasm. Pseudogenes derived from this gene are present in the genome. As with ribosomal protein S27a, ribosomal protein L40 is also synthesized as a fusion protein with ubiquitin; similarly, ribosomal protein S30 is synthesized as a fusion protein with the ubiquitin-like protein fubi. Multiple alternatively spliced transcript variants that encode the same proteins have been identified.[provided by RefSeq, Sep 2008].
UOM:
1 * 100 µl
Fournisseur:
LABCONCO
Description:
Accessory for Freeze Dryer, Heated shelf with sensor, 321×422 mm, 2,3 kg
Numéro de catalogue:
(BOSSBS-12361R-HRP)
Fournisseur:
Bioss
Description:
The leucine-rich (LRR) repeat is a 20-30 amino acid motif that forms a hydrophobic å/∫ horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. FLRT1 (fibronectin leucine rich transmembrane protein 1) is a 646 amino acid single-pass type I membrane protein that contains one fibronectin type-III domain and ten LRR repeats. Expressed in kidney and brain, FLRT1 is thought to play a role in cell adhesion and receptor signaling. FLRT1 shares similarity with FLRT2 and FLRT3 and is subject to post-translational N-glycosylation. The gene encoding FLRT1 maps to human chromosome 11, which houses over 1,400 genes and comprises nearly 4% of the human genome.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12333R-A647)
Fournisseur:
Bioss
Description:
ERMAP is a single-pass type one membrane protein that belongs to the immunoglobulin superfamily. Expressed in cord blood, fetal liver and adult bone marrow, ERMAP is thought to function as a cell adhesion molecule in erythroid cells and is responsible for expression of the Scianna/Radin (Sc/Rd) blood group antigen system. The Sc/Rd system is comprised of seven antigens that are present on the surface of red blood cells and have a variety of functions ranging from protein transport to cell adhesion. These seven blood antigens can differ in their expression within a population and may sometimes differ between mother and child. A fetus expressing different blood antigens than its mother may cause the mother to produce against the fetal blood. This condition is known as hemolytic disease of the newborn (HDN) and is characterized by jaundice, anemia and in some cases, infant death.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13628R-A488)
Fournisseur:
Bioss
Description:
The C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily consists of a variety of proteins that share a common protein fold and have diverse functions, including cell-cell signaling, cell adhesion, glycoprotein turnover and immune responses. CLEC-12A (C-type lectin domain family 12, member A), also known as CLL1, MICL, CLL-1 or DCAL-2, is a 275 amino acid single-pass type II membrane protein that contains one C-type lectin domain and belongs to the CTL/CTLD superfamily. Existing as multiple alternatively spliced isoforms that are expressed in neutrophils, eosinophils, monocytes and dendritic cells, CLEC-12A functions as a cell surface receptor that acts as a negative regulator of granulocyte and monocyte function and, via this activity, modulates signaling cascades. CLEC-12A is highly subject to post-translational glycosylation at its N-terminus and may also exist as a homodimer.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13628R-HRP)
Fournisseur:
Bioss
Description:
The C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily consists of a variety of proteins that share a common protein fold and have diverse functions, including cell-cell signaling, cell adhesion, glycoprotein turnover and immune responses. CLEC-12A (C-type lectin domain family 12, member A), also known as CLL1, MICL, CLL-1 or DCAL-2, is a 275 amino acid single-pass type II membrane protein that contains one C-type lectin domain and belongs to the CTL/CTLD superfamily. Existing as multiple alternatively spliced isoforms that are expressed in neutrophils, eosinophils, monocytes and dendritic cells, CLEC-12A functions as a cell surface receptor that acts as a negative regulator of granulocyte and monocyte function and, via this activity, modulates signaling cascades. CLEC-12A is highly subject to post-translational glycosylation at its N-terminus and may also exist as a homodimer.
UOM:
1 * 100 µl
Fournisseur:
Biotium
Description:
This MAb recognizes a 27 kDa protein, identified as the p27Kip1, a cell cycle regulatory mitotic inhibitor. It is highly specific and shows no cross-reaction with other related mitotic inhibitors. In Western blotting of cell lysates from 7 human breast cancer cell lines (ZR75-1, ZR75-30, MCF-7, MDAMB453, T47D, CAL51, 734B), the antibody labels a single band corresponding to p27Kip1. It functions as a negative regulator of G1 progression and has been proposed to function as a possible mediator of TGF- induced G1 arrest. p27Kip1 is a candidate tumor suppressor gene. Reportedly, low p27 expression has been associated with unfavorable prognosis in renal cell carcinoma, colon carcinoma, breast carcinomas, non-small-cell lung carcinoma, hepatocellular carcinoma, multiple myeloma, and lymph node metastases in papillary carcinoma of the thyroid, as well as a more aggressive phenotype in carcinoma of the cervix.
Numéro de catalogue:
(BOSSBS-11468R)
Fournisseur:
Bioss
Description:
Nogo is an oligodendrocyte-specific member of the Reticulon family and is a component of CNS white matter that inhibits axon outgrowth, induces collapse of growth cones of chick dorsal root ganglion cells, and inhibits the spreading of 3T3 fibroblasts. Nogo is expressed by oligodendrocytes but not by Schwann cells and associates primarily with the endoplasmic reticulum. Nogo exists in three different splice forms, Nogo-A, -B and -C. NgBR (Nogo-B receptor), also known as nuclear undecaprenyl pyrophosphate synthase 1 homolog, is a 293 amino acid single-pass type I membrane protein that acts as a specific receptor for the amino-terminus of Nogo-B. Through this interaction, NgBR is involved in the regulation of vascular remodeling and angiogenesis. NgBR also enhances Niemann-Pick type C2 protein (NPC2) stabilization. Knockdown of NgBR mRNA leads to decreased NPC2 levels, which results in the hallmarks of NPC2 mutation: increased intracellular cholesterol accumulation and a loss of sterol sensing.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11468R-A488)
Fournisseur:
Bioss
Description:
Nogo is an oligodendrocyte-specific member of the Reticulon family and is a component of CNS white matter that inhibits axon outgrowth, induces collapse of growth cones of chick dorsal root ganglion cells, and inhibits the spreading of 3T3 fibroblasts. Nogo is expressed by oligodendrocytes but not by Schwann cells and associates primarily with the endoplasmic reticulum. Nogo exists in three different splice forms, Nogo-A, -B and -C. NgBR (Nogo-B receptor), also known as nuclear undecaprenyl pyrophosphate synthase 1 homolog, is a 293 amino acid single-pass type I membrane protein that acts as a specific receptor for the amino-terminus of Nogo-B. Through this interaction, NgBR is involved in the regulation of vascular remodeling and angiogenesis. NgBR also enhances Niemann-Pick type C2 protein (NPC2) stabilization. Knockdown of NgBR mRNA leads to decreased NPC2 levels, which results in the hallmarks of NPC2 mutation: increased intracellular cholesterol accumulation and a loss of sterol sensing.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11468R-CY3)
Fournisseur:
Bioss
Description:
Nogo is an oligodendrocyte-specific member of the Reticulon family and is a component of CNS white matter that inhibits axon outgrowth, induces collapse of growth cones of chick dorsal root ganglion cells, and inhibits the spreading of 3T3 fibroblasts. Nogo is expressed by oligodendrocytes but not by Schwann cells and associates primarily with the endoplasmic reticulum. Nogo exists in three different splice forms, Nogo-A, -B and -C. NgBR (Nogo-B receptor), also known as nuclear undecaprenyl pyrophosphate synthase 1 homolog, is a 293 amino acid single-pass type I membrane protein that acts as a specific receptor for the amino-terminus of Nogo-B. Through this interaction, NgBR is involved in the regulation of vascular remodeling and angiogenesis. NgBR also enhances Niemann-Pick type C2 protein (NPC2) stabilization. Knockdown of NgBR mRNA leads to decreased NPC2 levels, which results in the hallmarks of NPC2 mutation: increased intracellular cholesterol accumulation and a loss of sterol sensing.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-6049R-A488)
Fournisseur:
Bioss
Description:
FGFRL1 is a member of the fibroblast growth factor receptor (FGFR) family, where amino acid sequence is highly conserved between members and throughout evolution. FGFR family members differ from one another in their ligand affinities and tissue distribution. A full-length representative protein would consist of an extracellular region, composed of three immunoglobulin-like domains, a single hydrophobic membrane-spanning segment and a cytoplasmic tyrosine kinase domain. The extracellular portion of the protein interacts with fibroblast growth factors, setting in motion a cascade of downstream signals, ultimately influencing mitogenesis and differentiation. A marked difference between FGFRL1 and the other family members is its lack of a cytoplasmic tyrosine kinase domain. The result is a transmembrane receptor that could interact with other family members and potentially inhibit signaling. Multiple alternatively spliced transcript variants encoding the same isoform have been found.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13028R-CY7)
Fournisseur:
Bioss
Description:
Dipeptidyl peptidases (DPPs) mediate regulatory activity of their substrates and have been linked to a variety of diseases including type 2 diabetes, obesity and cancer. DPPs have post-proline dipeptidyl aminopeptidase activity, cleaving Xaa-Pro dipeptides from the N-termini of proteins. DPPs can bind specific voltage-gated potassium channels and alter their expression and biophysical properties and may also influence T cells. DPP proteins include DPRP1, DPRP2, DPP3, DPP7, DPP10, DPPX and CD26. DPP10 (dipeptidyl-peptidase 10), also known as DPRP3 (dipeptidyl peptidase IV-related protein 3), DPL2 or DPPY, is a non-functional dipeptidyl peptidase which can bind to the potassium channels KV4.1 and KV4.2. It is a single-pass type II membrane protein expressed in spinal cord, adrenal glands, pancreas and brain tissues and may act as a modulator for cell surface expression and activity of KV4.1 and KV4.2.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13162R-CY7)
Fournisseur:
Bioss
Description:
Ficolin B is the designation in mouse and rat of a protein also known as L-ficolin, ficolin-2, collagen/fibrinogen domain-containing protein 2, serum lectin p35, EBP-37 or hucolin. Ficolin B is a 313 amino acid member of the ficolin lectin family. It is a secreted innate immunity pattern recognition molecule expressed in liver and plasma that forms a disulfide-linked homopolymer. This extensive N-terminal disulfide bridge formation can lead to a functional dodecamer polypeptide. Ficolin B binds to DNA ligands expressed by late apoptotic and necrotic cells to increase attachment and engulfment. Variation in ficolin B concentrations amongst individuals is associated with polymorphisms in the promoter and structural portion of the FCN2 gene. In patients with Behé´t's disease (BD), there exists a significant difference in allele frequency for FCN2 gene single nucleotide polymorphisms (SNPs) within the -557 and -64 promoter sites within HLA-B51 positive and HLA-B51 negative subgroups.
UOM:
1 * 100 µl
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