Text Search >
3-[1,1\\\\\\\'-Biphenyl]-4-ylacrylic+acid
Print…
You Searched For:
145,862 results were found
3-[1,1\\\\\\\'-Biphenyl]-4-ylacrylic+acid
Catalog Number:
(76079-016)
Supplier:
Bioss
Description:
This gene encodes a member of the secretoglobin family of small secreted proteins. The encoded protein has been implicated in numerous functions including anti-inflammation, inhibition of phospholipase A2 and the sequestering of hydrophobic ligands. Defects in this gene are associated with a susceptibility to asthma. Binds phosphatidylcholine, phosphatidylinositol, polychlorinated biphenyls (PCB) and weakly progesterone.
Catalog Number:
(10307-682)
Supplier:
Bioss
Description:
This gene encodes a member of the secretoglobin family of small secreted proteins. The encoded protein has been implicated in numerous functions including anti-inflammation, inhibition of phospholipase A2 and the sequestering of hydrophobic ligands. Defects in this gene are associated with a susceptibility to asthma. Binds phosphatidylcholine, phosphatidylinositol, polychlorinated biphenyls (PCB) and weakly progesterone.
Catalog Number:
(10750-102)
Supplier:
Prosci
Description:
LGI2 Antibody: The leucine-rich, glioma inactivated gene 2 (LGI2) is a member of the LGI family in which LGI1 is the exemplar. The LGI family consists of four of highly related proteins containing leucine-rich repeats (LRRs) which are highly similar to other transmembrane signaling molecules and receptors. LGI1 has been identified as a candidate tumor suppressor gene for glioma and plays a role in autodominant lateral temporal epilepsy (ADTLE), an epileptic syndrome characterized by focal seizures with predominant auditory symptoms. Despite its high homology with LGI1 and similar pattern of expression, mutations in LGI2 have not been found to be associated with ADTLE.
Catalog Number:
(10749-778)
Supplier:
Prosci
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 can be found. These subtypes are classified based on the combination of the virus coat glycoproteins hemagglutinin (HA) and neuraminidase (NA) subtypes. H7N9 bird flu is the newest atypical influenza virus infection that has just been reported since early 2013. The emergence of this new strain occurred in China and has become the present focus for possible worldwide pandemic.
Catalog Number:
(89416-060)
Supplier:
Prosci
Description:
RP105 Antibody: 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:
(10748-604)
Supplier:
Prosci
Description:
RP105 Antibody: 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:
(77749-004)
Supplier:
AMBEED, INC
Description:
4-Phenylbenzylamine 98%
Catalog Number:
(10748-416)
Supplier:
Prosci
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 can be found. These subtypes are classified based on the combination of the virus coat glycoproteins hemagglutinin (HA) and neuraminidase (NA) subtypes. H7N9 bird flu is the newest atypical influenza virus infection that has just been reported since early 2013. The emergence of this new strain occurred in China and has become the present focus for possible worldwide pandemic.
Catalog Number:
(103322-756)
Supplier:
Novus Biologicals
Description:
The BPHL Antibody from Novus Biologicals is a mouse polyclonal antibody to BPHL. This antibody reacts with human. The BPHL Antibody has been validated for the following applications: Western Blot.
Catalog Number:
(89350-850)
Supplier:
Genetex
Description:
Tau proteins are microtubule-associated proteins that are abundant in neurons in the central nervous system and are less common elsewhere. They were discovered in 1975 in Marc Kirschner's laboratory at Princeton University. Tau proteins interact with tubulin to stabilize microtubules and promote tubulin assembly into microtubules. Tau has two ways of controlling microtubule stability: isoforms and phosphorylation. Six tau isoforms exist in brain tissue, and they are distinguished by their number of binding domains. Three isoforms have three binding domains and the other three have four binding domains. The binding domains are located in the carboxy-terminus of the protein and are positively-charged (allowing it to bind to the negatively-charged microtubule). The isoforms with four binding domains are better at stabilizing microtubules than those with three binding domains. The isoforms are a result of alternative splicing in exons 2,3, and 10 of the tau gene. Phosphorylation of tau is regulated by a host of kinases. For example, PKN, a serine/threonine kinase. When PKN is activated, it phosphorylates tau, resulting in disruption of microtubule organization. Hyperphosphorylation of the tau protein (tau inclusions), however, can result in the self-assembly of tangles of paired helical filaments and straight filaments, which are involved in the pathogenesis of Alzheimer's disease and other tauopathies. Tau protein is a highly soluble microtubule-associated protein (MAP). In humans, these proteins are mostly found in neurons compared to non-neuronal cells. One of tau's main functions is to modulate the stability of axonal microtubules. Tau is not present in dendrites and is active primarily in the distal portions of axons where it provides microtubule stabilization but also flexibility as needed. This contrasts with STOP proteins in the proximal portions of axons which essentially lock down the microtubules and MAP2 that stabilizes microtubules in dendrites. The tau gene locates on chromosome 17q21, containing 16 exons. The major tau protein in the human brain is encoded by 11 exons. Exon 2, 3 and 10 are alternative spliced, allowing six combinations (2-3-10-; 2+3-10-; 2+3+10-; 2-3-10+; 2+3-10+; 2+3+10+). Thus, in the human brain, the tau proteins constitute a family of six isoforms with the range from 352-441 amino acids. They differ in either no, one or two inserts of 29 amino acids at the N-terminal part (exon 2 and 3), and three or four repeat-regions at the C-terminal part exon 10 missing. So, the longest isoform in the CNS has four repeats (R1, R2, R3 and R4) and two inserts (441 amino acids total), while the shortest isoform has three repeats (R1, R3 and R4) and no insert (352 amino acids total). All of the six tau isoforms are present in an often hyperphosphorylated state in paired helical filaments from Alzheimer's Disease brain. In other neurodegenerative diseases, the deposition of aggregates enriched in certain tau isoforms has been reported. When misfolded this otherwise very soluble protein can form extremely insoluble aggregates that contribute to a number of neurodegenerative diseases.
Supplier:
PeproTech, Inc.
Description:
The dickkopf (DKK)-related protein family is comprised of four central members, DKK-1 - 4, along with the distantly-related DKK family member DKK-11 (Soggy), which is thought to be a descendent of an ancestral DKK-3 precursor due to its unique sequence homology to DKK-3 and no other DKK family member. DKK family members, with the exception of the divergent Soggy, share two conserved cysteine-rich domains and show very little sequence similarity outside of these domains. Playing an important regulatory role in vertebrate development through localized inhibition of Wnt-regulated processes, including anterior-posterior axial patterning, limb development, somitogenesis, and eye formation, DKKs have also been implicated post-developmentally in bone formation, bone disease, cancer, and neurodegenerative diseases. DKK proteins typically play an important regulatory role in the Wnt/β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/β-catenin signaling system. LRP5 and LRP6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/β-catenin signaling cascade. DKK-2 has been shown to both inhibit and enhance canonical Wnt signaling; enhancing Wnt signaling through direct high-affinity binding of DKK-2 to LRP6 during LRP6 overexpression, while inhibiting Wnt signaling and promoting LRP6 internalization through the formation of a ternary complex between DKK-2, LRP6, and Kremen-2. Recombinant Human DKK-2 expressed in
Catalog Number:
(89359-344)
Supplier:
Genetex
Description:
Tau proteins are microtubule-associated proteins that are abundant in neurons in the central nervous system and are less common elsewhere. They were discovered in 1975 in Marc Kirschner's laboratory at Princeton University. Tau proteins interact with tubulin to stabilize microtubules and promote tubulin assembly into microtubules. Tau has two ways of controlling microtubule stability: isoforms and phosphorylation. Six tau isoforms exist in brain tissue, and they are distinguished by their number of binding domains. Three isoforms have three binding domains and the other three have four binding domains. The binding domains are located in the carboxy-terminus of the protein and are positively-charged (allowing it to bind to the negatively-charged microtubule). The isoforms with four binding domains are better at stabilizing microtubules than those with three binding domains. The isoforms are a result of alternative splicing in exons 2,3, and 10 of the tau gene. Phosphorylation of tau is regulated by a host of kinases. For example, PKN, a serine/threonine kinase. When PKN is activated, it phosphorylates tau, resulting in disruption of microtubule organization. Hyperphosphorylation of the tau protein (tau inclusions), however, can result in the self-assembly of tangles of paired helical filaments and straight filaments, which are involved in the pathogenesis of Alzheimer's disease and other tauopathies. Tau protein is a highly soluble microtubule-associated protein (MAP). In humans, these proteins are mostly found in neurons compared to non-neuronal cells. One of tau's main functions is to modulate the stability of axonal microtubules. Tau is not present in dendrites and is active primarily in the distal portions of axons where it provides microtubule stabilization but also flexibility as needed. This contrasts with STOP proteins in the proximal portions of axons which essentially lock down the microtubules and MAP2 that stabilizes microtubules in dendrites. The tau gene locates on chromosome 17q21, containing 16 exons. The major tau protein in the human brain is encoded by 11 exons. Exon 2, 3 and 10 are alternative spliced, allowing six combinations (2-3-10-; 2+3-10-; 2+3+10-; 2-3-10+; 2+3-10+; 2+3+10+). Thus, in the human brain, the tau proteins constitute a family of six isoforms with the range from 352-441 amino acids. They differ in either no, one or two inserts of 29 amino acids at the N-terminal part (exon 2 and 3), and three or four repeat-regions at the C-terminal part exon 10 missing. So, the longest isoform in the CNS has four repeats (R1, R2, R3 and R4) and two inserts (441 amino acids total), while the shortest isoform has three repeats (R1, R3 and R4) and no insert (352 amino acids total). All of the six tau isoforms are present in an often hyperphosphorylated state in paired helical filaments from Alzheimer's Disease brain. In other neurodegenerative diseases, the deposition of aggregates enriched in certain tau isoforms has been reported. When misfolded this otherwise very soluble protein can form extremely insoluble aggregates that contribute to a number of neurodegenerative diseases.
Catalog Number:
(10307-684)
Supplier:
Bioss
Description:
This gene encodes a member of the secretoglobin family of small secreted proteins. The encoded protein has been implicated in numerous functions including anti-inflammation, inhibition of phospholipase A2 and the sequestering of hydrophobic ligands. Defects in this gene are associated with a susceptibility to asthma. Binds phosphatidylcholine, phosphatidylinositol, polychlorinated biphenyls (PCB) and weakly progesterone.
Catalog Number:
(89350-852)
Supplier:
Genetex
Description:
Tau proteins are microtubule-associated proteins that are abundant in neurons in the central nervous system and are less common elsewhere. They were discovered in 1975 in Marc Kirschner's laboratory at Princeton University. Tau proteins interact with tubulin to stabilize microtubules and promote tubulin assembly into microtubules. Tau has two ways of controlling microtubule stability: isoforms and phosphorylation. Six tau isoforms exist in brain tissue, and they are distinguished by their number of binding domains. Three isoforms have three binding domains and the other three have four binding domains. The binding domains are located in the carboxy-terminus of the protein and are positively-charged (allowing it to bind to the negatively-charged microtubule). The isoforms with four binding domains are better at stabilizing microtubules than those with three binding domains. The isoforms are a result of alternative splicing in exons 2,3, and 10 of the tau gene. Phosphorylation of tau is regulated by a host of kinases. For example, PKN, a serine/threonine kinase. When PKN is activated, it phosphorylates tau, resulting in disruption of microtubule organization. Hyperphosphorylation of the tau protein (tau inclusions), however, can result in the self-assembly of tangles of paired helical filaments and straight filaments, which are involved in the pathogenesis of Alzheimer's disease and other tauopathies. Tau protein is a highly soluble microtubule-associated protein (MAP). In humans, these proteins are mostly found in neurons compared to non-neuronal cells. One of tau's main functions is to modulate the stability of axonal microtubules. Tau is not present in dendrites and is active primarily in the distal portions of axons where it provides microtubule stabilization but also flexibility as needed. This contrasts with STOP proteins in the proximal portions of axons which essentially lock down the microtubules and MAP2 that stabilizes microtubules in dendrites. The tau gene locates on chromosome 17q21, containing 16 exons. The major tau protein in the human brain is encoded by 11 exons. Exon 2, 3 and 10 are alternative spliced, allowing six combinations (2-3-10-; 2+3-10-; 2+3+10-; 2-3-10+; 2+3-10+; 2+3+10+). Thus, in the human brain, the tau proteins constitute a family of six isoforms with the range from 352-441 amino acids. They differ in either no, one or two inserts of 29 amino acids at the N-terminal part (exon 2 and 3), and three or four repeat-regions at the C-terminal part exon 10 missing. So, the longest isoform in the CNS has four repeats (R1, R2, R3 and R4) and two inserts (441 amino acids total), while the shortest isoform has three repeats (R1, R3 and R4) and no insert (352 amino acids total). All of the six tau isoforms are present in an often hyperphosphorylated state in paired helical filaments from Alzheimer's Disease brain. In other neurodegenerative diseases, the deposition of aggregates enriched in certain tau isoforms has been reported. When misfolded this otherwise very soluble protein can form extremely insoluble aggregates that contribute to a number of neurodegenerative diseases.
Supplier:
Matrix Scientific
Description:
MF=C38H32N2 MW=516.69 CAS=65181-78-4 MDL=MFCD00144965 5G
Inquire for Price
Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the
 is still displayed and you need assistance, please call us at 1-800-932-5000.
Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the
is still displayed and you need assistance, please call us at 1-800-932-5000.
This product is marked as restricted and can only be purchased by approved Shipping Accounts. If you need further assistance, email VWR Regulatory Department at Regulatory_Affairs@vwr.com
-Additional Documentation May be needed to purchase this item. A VWR representative will contact you if needed.
This product has been blocked by your organization. Please contact your purchasing department for more information.
The original product is no longer available. The replacement shown is available.
This product is no longer available. Alternatives may be available by searching with the VWR Catalog Number listed above. If you need further assistance, please call VWR Customer Service at 1-800-932-5000.
|
|||||||||
List View
