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Single-use+Pressure+Sensor
Numéro de catalogue:
(PRSI26-003)
Fournisseur:
ProSci Inc.
Description:
LRRC24 contains 1 Ig-like C2-type (immunoglobulin-like) domain and 7 LRR (leucine-rich) repeats. It is a single-pass membrane protein. The function of the LRRC24 protein remains unknown.
UOM:
1 * 50 µG
Numéro de catalogue:
(PRSI25-870)
Fournisseur:
ProSci Inc.
Description:
RNF148 is a single-pass membrane protein. It contains 1 PA (protease associated) domain and 1 RING-type zinc finger. The exact function of RNF148 remains unknown.
UOM:
1 * 50 µG
Numéro de catalogue:
(PRSI25-992)
Fournisseur:
ProSci Inc.
Description:
VSIG8 contains 2 Ig-like V-type (immunoglobulin-like) domains. VSIG8 is single-pass type I membrane protein. The function of the VSIG8 protein remains unknown.
UOM:
1 * 50 µG
Numéro de catalogue:
(634-0388)
Fournisseur:
Thermo Fisher Scientific
Description:
Accessoire pour spectrophotomètre UV/Vis, Portoir de rechange pour cuves, GENESYS™ 20, Genesys®
UOM:
1 * 1 ST
Fournisseur:
Portwest
Description:
Anti-static, laced lab shoe manufactured from high quality, water resistant microfibre plus a single-density lightweight PU sole, resistant to oil.
Fournisseur:
Corning
Description:
These polypropylene reagent vessels are appropriate for automated and manual applications
Numéro de catalogue:
(PRSI26-469)
Fournisseur:
ProSci Inc.
Description:
KIRREL2 is a single-pass type I membrane protein. KIRREL2 protein is a beta-cell-expressed Ig domain protein and may be involved in pancreas development or beta cell function.
UOM:
1 * 50 µG
Numéro de catalogue:
(BOSSBS-1906R-A488)
Fournisseur:
Bioss
Description:
The synaptotagmins are integral membrane proteins of synaptic vesicles thought to serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Calcium binding to synaptotagmin participates in triggering neurotransmitter release at the synapse. The first C2 domain mediates Ca(2+)-dependent phospholipid binding. The second C2 domain mediates interaction with Stonin 2. Synaptotagmin may have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1906R-A350)
Fournisseur:
Bioss
Description:
The synaptotagmins are integral membrane proteins of synaptic vesicles thought to serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Calcium binding to synaptotagmin participates in triggering neurotransmitter release at the synapse. The first C2 domain mediates Ca(2+)-dependent phospholipid binding. The second C2 domain mediates interaction with Stonin 2. Synaptotagmin may have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3027R-CY3)
Fournisseur:
Bioss
Description:
Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1906R-A647)
Fournisseur:
Bioss
Description:
The synaptotagmins are integral membrane proteins of synaptic vesicles thought to serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Calcium binding to synaptotagmin participates in triggering neurotransmitter release at the synapse. The first C2 domain mediates Ca(2+)-dependent phospholipid binding. The second C2 domain mediates interaction with Stonin 2. Synaptotagmin may have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2.
UOM:
1 * 100 µl
Numéro de catalogue:
(PRSI30-064)
Fournisseur:
ProSci Inc.
Description:
PTPRR is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP possesses an extracellular region, a single transmembrane region, and a single intracellular catalytic domains, and thus represents a receptor-type PTP.The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP possesses an extracellular region, a single transmembrane region, and a single intracellular catalytic domains, and thus represents a receptor-type PTP. The similar gene predominately expressed in mouse brain was found to associate with, and thus regulate the activity and cellular localization of MAP kinases. The rat counterpart of this gene was reported to be regulated by the nerve growth factor, which suggested the function of this gene in neuronal growth and differentiation. Telomerase is a ribonucleoprotein polymerase that maintains telomere ends by addition of the telomere repeat TTAGGG. The enzyme consists of a protein component with reverse transcriptase activity, and an RNA component, encoded by this gene, that serves as a template for the telomere repeat. Telomerase expression plays a role in cellular senescence, as it is normally repressed in postnatal somatic cells resulting in progressive shortening of telomeres. Deregulation of telomerase expression in somatic cells may be involved in oncogenesis. Studies in mouse suggest that telomerase also participates in chromosomal repair, since de novo synthesis of telomere repeats may occur at double-stranded breaks. Mutations in this gene cause autosomal dominant dyskeratosis congenita, and may also be associated with some cases of aplastic anemia.
UOM:
1 * 50 µG
Numéro de catalogue:
(PRSI26-917)
Fournisseur:
ProSci Inc.
Description:
HABP2 is an extracellular serine protease that binds hyaluronic acid and is involved in cell adhesion. It is synthesized as a single chain, but then undergoes an autoproteolytic event to form the functional heterodimer. Further autoproteolysis leads to smaller, inactive peptides. This protease is known to cleave urinary plasminogen activator, coagulation factor VII, and the alpha and beta chains of fibrinogen, but not prothrombin, plasminogen, or the gamma chain of fibrinogen. The protein encoded by this gene is an extracellular serine protease that binds hyaluronic acid and is involved in cell adhesion. The encoded protein is synthesized as a single chain, but then undergoes an autoproteolytic event to form the functional heterodimer. Further autoproteolysis leads to smaller, inactive peptides. This protease is known to cleave urinary plasminogen activator, coagulation factor VII, and the alpha and beta chains of fibrinogen, but not prothrombin, plasminogen, or the gamma chain of fibrinogen. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.
UOM:
1 * 50 µG
Numéro de catalogue:
(PRSI92-418)
Fournisseur:
ProSci Inc.
Description:
Cadherin-16(CDH16) is a single-pass type I membrane protein which contains six cadherin domains. Mature cadherin proteins consist of a large N-terminal extracellular domain, a single membrane-spanning domain, and a small highly conserved C-terminal cytoplasmic domain. Cadherins are calcium-dependent cell adhesion proteins and may contribute to the sorting of heterogeneous cell types. They preferentially interact with themselves in a homophilic manner in connecting cells. Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. CDH16 is exclusively expressed in kidney, where the protein functions as the principal mediator of homotypic cellular recognition. It plays a role in the morphogenic direction of tissue development. CDH16 is composed of an extracellular domain containing 6 cadherin domains, a transmembrane region and a truncated cytoplasmic domain. However, it lacks the prosequence and tripeptide HAV adhesion recognition sequence typical of most classical cadherins.
UOM:
1 * 50 µG
Numéro de catalogue:
(BOSSBS-4114R-HRP)
Fournisseur:
Bioss
Description:
Serine/threonine kinase that plays an essential role in regulating inflammatory responses to viral infection, through the activation of the type I IFN, NF-kappa-B and STAT signaling. Also involved in TNFA and inflammatory cytokines, like Interleukin-1, signaling. Following activation of viral RNA sensors, such as RIG-I-like receptors, associates with DDX3X and phosphorylates interferon regulatory factors (IRFs), IRF3 and IRF7, as well as DDX3X. This activity allows subsequent homodimerization and nuclear translocation of the IRF3 leading to transcriptional activation of pro-inflammatory and antiviral genes including IFNB. In order to establish such an antiviral state, IKBKE forms several different complexes whose composition depends on the type of cell and cellular stimuli. Thus, several scaffolding molecules including IPS1/MAVS, TANK, AZI2/NAP1 or TBKBP1/SINTBAD can be recruited to the IKBKE-containing-complexes. Activated by polyubiquitination in response to TNFA and interleukin-1, regulates the NF-kappa-B signaling pathway through, at least, the phosphorylation of CYLD. Phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. In addition, is also required for the induction of a subset of ISGs which displays antiviral activity, may be through the phosphorylation of STAT1 at 'Ser-708'. Phosphorylation of STAT1 at 'Ser-708' seems also to promote the assembly and DNA binding of ISGF3 (STAT1:STAT2:IRF9) complexes compared to GAF (STAT1:STAT1) complexes, in this way regulating the balance between type I and type II IFN responses. Protects cells against DNA damage-induced cell death. Also plays an important role in energy balance regulation by sustaining a state of chronic, low-grade inflammation in obesity, wich leads to a negative impact on insulin sensitivity. Phosphorylates AKT1.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12972R)
Fournisseur:
Bioss
Description:
Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively. Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3. AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160. Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm. In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription. Acts as a key regulator of cell growth and proliferation by phosphorylating TSC2, RPTOR and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2.
UOM:
1 * 100 µl
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