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2-(Methoxymethyl)benzoic+acid
Catalog Number:
(75929-892)
Supplier:
Rockland Immunochemical
Description:
Toll-like receptors (TLRs) are evolutionarily conserved pattern-recognition molecules that recognize different microbial products during infection and serve as an important link between the innate and adaptive immune responses. The signaling of these TLRs is kept under tight control by the expression of endogenous inhibiting proteins such as RP105, a recently identified homolog of TLR4. This protein, in association with MD-1, interacts with and inhibits the TLR4/MD-2 signaling pathway. While MD-2 can directly bind to LPS, one of the activating molecules of TLR4, the function of MD-1 is less well-known. It has been suggested however, that the RP105/MD-1 complex influences antibody production mediated by both TLR4/MD-2 and TLR2 receptor complexes.
Catalog Number:
(75929-890)
Supplier:
Rockland Immunochemical
Description:
Toll-like receptors (TLRs) are evolutionarily conserved pattern-recognition molecules that recognize different microbial products during infection and serve as an important link between the innate and adaptive immune responses. The signaling of these TLRs is kept under tight control by the expression of endogenous inhibiting proteins such as RP105, a recently identified homolog of TLR4. This protein, in association with MD-1, interacts with and inhibits the TLR4/MD-2 signaling pathway. While MD-2 can directly bind to LPS, one of the activating molecules of TLR4, the function of MD-1 is less well-known. It has been suggested however, that the RP105/MD-1 complex influences antibody production mediated by both TLR4/MD-2 and TLR2 receptor complexes.
Supplier:
Upchurch Scientific
Description:
The Upchurch Scientific® Micro Static Mixing Tee by IDEX Health & Science utilizes a specifically engineered internal geometry to efficiently mix two fluid streams into one combined stream
Catalog Number:
(77437-584)
Supplier:
Bioss
Description:
AKT1 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling. Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport. AKT regulates also the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven. AKT regulates also cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF-kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1. AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis. Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis. Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P-5 activity. The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). AKT mediates the antiapoptotic effects of IGF-I. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. May be involved in the regulation of the placental development. Phosphorylates STK4/MST1 at 'Thr-120' and 'Thr-387' leading to inhibition of its: kinase activity, nuclear translocation, autophosphorylation and ability to phosphorylate FOXO3. Phosphorylates STK3/MST2 at 'Thr-117' and 'Thr-384' leading to inhibition of its: cleavage, kinase activity, autophosphorylation at Thr-180, binding to RASSF1 and nuclear translocation. Phosphorylates SRPK2 and enhances its kinase activity towards SRSF2 and ACIN1 and promotes its nuclear translocation. Phosphorylates RAF1 at 'Ser-259' and negatively regulates its activity. Phosphorylation of BAD stimulates its pro-apoptotic activity.
Catalog Number:
(77436-830)
Supplier:
Bioss
Description:
AKT1 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling. Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport. AKT regulates also the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven. AKT regulates also cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF-kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1. AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis. Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis. Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P-5 activity. The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). AKT mediates the antiapoptotic effects of IGF-I. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. May be involved in the regulation of the placental development. Phosphorylates STK4/MST1 at 'Thr-120' and 'Thr-387' leading to inhibition of its: kinase activity, nuclear translocation, autophosphorylation and ability to phosphorylate FOXO3. Phosphorylates STK3/MST2 at 'Thr-117' and 'Thr-384' leading to inhibition of its: cleavage, kinase activity, autophosphorylation at Thr-180, binding to RASSF1 and nuclear translocation. Phosphorylates SRPK2 and enhances its kinase activity towards SRSF2 and ACIN1 and promotes its nuclear translocation. Phosphorylates RAF1 at 'Ser-259' and negatively regulates its activity. Phosphorylation of BAD stimulates its pro-apoptotic activity.
Catalog Number:
(75931-670)
Supplier:
Rockland Immunochemical
Description:
Toll-like receptors (TLRs) are evolutionarily conserved pattern-recognition molecules resembling the toll proteins that mediate antimicrobial responses in Drosophila. These proteins recognize different microbial products during infection and serve as an important link between the innate and adaptive immune responses. The signaling of these TLRs is kept under tight control by the expression of endogenous inhibiting proteins. One such protein is RP105, a recently identified homolog to TLR4 that, with MD-1, interacts with and inhibits the TLR4/MD-2 signaling pathway. It has also been suggested that the RP105/MD-1 complex influences antibody production mediated by both TLR4/MD-2 and TLR2 receptor complexes.
Catalog Number:
(10750-570)
Supplier:
Prosci
Description:
Avian Influenza Nonstructural Protein 2 Antibody: Influenza A virus is a major public health threat, killing more than 30, 000 people per year in the USA. Novel influenza virus strains caused by genetic drift and viral recombination emerge periodically to which humans have little or no immunity, resulting in devastating pandemics. Influenza A can exist in a variety of animals; however, it is in birds that all subtypes, including the so-called "avian flu" or H5N1, can be found. These subtypes are classified based on the combination of the virus coat glycoproteins hemagglutinin (HA) and neuraminidase (NA) subtypes. One of the less studied proteins encoded by the influenza virus is the nonstructural protein (NS) 2. NS2 binds to the influenza matrix protein M1 that is bound to the ribonucleoprotein (RNP) complex and mediates the contact between the M1/RNP complex and the cellular exportin CRM, but does not interact with nucleosomes.
Catalog Number:
(10750-918)
Supplier:
Prosci
Description:
APC4 Antibody: Cell cycle regulated protein ubiquitination and degradation within subcellular domains is thought to be essential for the normal progression of mitosis. APC4 is a highly conserved component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. APC/C is responsible for degrading anaphase inhibitors, mitotic cyclins, and spindle-associated proteins ensuring that events of mitosis take place in proper sequence. The individual APC/C components mRNA and protein levels are expressed at approximately the same levels in most tissues and cell lines, suggesting that they perform their functions as part of a complex. While little is known of APC4, it is thought that APC4 associates with other APC/C components APC1, APC5, and CDC23 interdependently, such that loss of any one subunit reduces binding between the remaining three.
Catalog Number:
(10750-844)
Supplier:
Prosci
Description:
DCLK1 Antibody: DCLK1 is one of three doublecortin-like kinases similar to the Ca2+/calmodulin-dependent protein kinase (CaMK) family. DCLK1 mRNA, like that of the homologous DCLK2 and DCLK3, is highly expressed in adult brain, but only DCLK1 and DCLK2 transcripts are present in human fetal brain and the developing mouse embryo, suggesting that DCLK1 and DCLK2 may play roles in cortical development. The DCLK proteins are homologous to Doublecortin (DCX), a gene that is mutated in X-linked human lissencephaly. In mouse models where the DCX gene has been disrupted, DCLK1 expression increases slightly and appears to compensate for the loss of DCX, as mice mutant for both DCX and DCLK1 show a severe phenotype including perinatal lethality, disorganized neocortical layering, and profound hippocampal cytoarchitectural disorganization. Unlike DCLK1, DCLK2 expression does not change in DCX-null mice.
Catalog Number:
(10750-222)
Supplier:
Prosci
Description:
Nanos1 Antibody: Nanos1 is one of three known mammalian homologs to the Drosophila gene nanos. Nanos1 is an RNA-binding protein containing a zinc-finger motif and is expressed in the developing nervous system and continues in the adult brain. Interestingly, unlike mice deficient in either nanos2 or nanos3, mice lacking the nanos1 gene develop normally with no sign of abnormalities. Recently it has been found that expression of nanos1 mRNA is down-regulated by E-cadherin in a human breast cancer cell line and the amino-terminal domain on Nanos1 interacts with the E-cadherin-binding protein p120ctn. Furthermore, overexpression of Nanos1 in human colorectal DLD1 cancer cells functionally abolished cell-cell adhesion, allowing the cancer cells to develop strong migratory and invasive properties. These results suggest that targeting Nanos1 might prove an effective strategy in the treatment of E-cadherin-negative tumors.
Catalog Number:
(10750-590)
Supplier:
Prosci
Description:
MAK10 Antibody: The MAK10 gene encodes a 733-amino acid protein with several regions of similarity to T cell receptor alpha-subunit V (variable) regions in yeast. The mammalian homologue of yeast MAK10, also known as EGAP, is one subunit of a novel N-terminal acetyltransferase (NAT) that is highly conserved among vertebrate species. It is expressed in a variety of tissues in the developing rat embryo but restricted in expression in the adult, remaining detectable only in tissues undergoing continual cell renewal or in cells responding to pathological injury. The MAK10-NAT complex is an essential regulatory enzyme controlling the function of a subset of proteins required for embryonic growth control and vessel development. This complex functionally co-assembles in mammalian cells to regulate cell proliferation and is essential for embryonic development, at least in part through the regulation of target of rapamycin (TOR) signaling events. At least two isoforms of MAK10 are known to exist.
Catalog Number:
(10748-772)
Supplier:
Prosci
Description:
Rkhd4 Antibody: Rkhd4, also known as MEX3A is a member of a novel family of four homologous human MEX3 proteins each containing two heterogeneous nuclear ribonucleoprotein K homology (KH) domains and one carboxy-terminal RING finger module. MEX3 proteins, including Rkhd4, are phosphoproteins that bind RNA through their KH domains and shuttle between the nucleus and the cytoplasm via the CRM1 export pathway. These proteins are a novel family of evolutionarily conserved RNA-binding proteins, differentially recruited to P bodies and potentially involved in post-transcriptional regulatory mechanisms. While Rkhd2 has been suggested to be associated with susceptibility to essential hypertension type 8, the function of Rkhd4 remains unknown. Rkhd3 and Rkhd4, but not Rkhd2, co-localize with both the hDcp1a decapping factor and Argonaute (Ago) proteins in processing bodies (P bodies), recently characterized as centers of mRNA turnover.
Catalog Number:
(10750-846)
Supplier:
Prosci
Description:
DCLK2 Antibody: DCLK2 is one of three doublecortin-like kinases similar to the Ca2+/calmodulin-dependent protein kinase (CaMK) family. DCLK2 mRNA, like that of the homologous DCLK1 and DCLK3, is highly expressed in adult brain, but only DCLK1 and DCLK2 transcripts are present in human fetal brain and the developing mouse embryo, suggesting that DCLK1 and DCLK2 may play roles in cortical development. The DCLK proteins are homologous to Doublecortin (DCX), a protein that is mutated in X-linked human lissencephaly. In mouse models where the DCX gene has been disrupted, DCLK1 expression increases slightly and appears to compensate for the loss of DCX, as mice mutant for both DCX and DCLK1 show a severe phenotype including perinatal lethality, disorganized neocortical layering, and profound hippocampal cytoarchitectural disorganization. Unlike DCLK1, DCLK2 expression does not change in DCX-null mice.
Catalog Number:
(10801-670)
Supplier:
Rockland Immunochemical
Description:
Influenza A virus is a major public health threat, killing more than 30, 000 people per year in the USA. Novel influenza virus strains caused by genetic drift and viral recombination emerge periodically to which humans have little or no immunity, resulting in devastating pandemics. Influenza A can exist in a variety of animals; however, it is in birds that all subtypes, including the so-called "avian flu" or H5N1, can be found. These subtypes are classified based on the combination of the virus coat glycoproteins hemagglutinin (HA) and neuraminidase (NA) subtypes. One of the less studied proteins encoded by the influenza virus is the nonstructural protein (NS) 2. NS2 binds to the influenza matrix protein M1 that is bound to the ribonucleoprotein (RNP) complex and mediates the contact between the M1/RNP complex and the cellular exportin CRM, but does not interact with nucleosomes.
Catalog Number:
(75933-200)
Supplier:
Rockland Immunochemical
Description:
Tetratricopeptide repeat protein 5 (TTC5) is a member of a diverse group of functionally distinct proteins that are characterized by containing one or more tetratricopeptide repeats. Each motif consists of two anti-parallel a-helices such that tandem arrays of TPR motifs generate a right-handed helical structure with an amphipathic channel that may serve to accommodate the complementary region of a target protein. While the exact function of TTC5 remains unclear, it is thought that the TPR motifs serve to mediate protein-protein interactions such as those seen with protein chaperones HSP70 and HSP90 and some proteins involved in cell stress response signaling pathways such as protein phosphatase 5, suggesting that TTC5 may also function via protein-protein interactions mediated by its TPR motifs.
Catalog Number:
(10800-986)
Supplier:
Rockland Immunochemical
Description:
DCLK3 is one of three doublecortin-like kinases similar to the Ca2+/calmodulin-dependent protein kinase (CaMK) family. DCLK3 mRNA, like that of the homologous DCLK1 and DCLK3, is highly expressed in adult brain, but only DCLK3 transcripts are present in liver and kidney, suggesting that DCLK3 may play other roles than in cortical development. The DCLK proteins are homologous to Doublecortin (DCX), a protein that is mutated in X-linked human lissencephaly. In mouse models where the DCX gene has been disrupted, DCLK1 expression increases slightly and appears to compensate for the loss of DCX, as mice mutant for both DCX and DCLK1 show a severe phenotype including perinatal lethality, disorganized neocortical layering, and profound hippocampal cytoarchitectural disorganization.
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is still displayed and you need assistance, please call us at 1-800-932-5000.
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