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6-(2-Methylpropoxy)pyridine-3-boronic+acid


37,995  results were found

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Supplier:  TCI America
Description:   CAS Number: 5336-08-3
MDL Number: MFCD00063241
Molecular Formula: C5H8O5
Molecular Weight: 148.11
Purity/Analysis Method: >97.0% (GC)
Form: Crystal
Color: White
Melting point (°C): 86
Specific rotation [a]20/D: 18 deg (C=1, H2O)
MSDS SDS
Supplier:  Bioss
Description:   The semaphorins are a family of proteins that are involved in signaling. All the family members have a secretion signal, a 500-amino acid sema domain, and 16 conserved cysteine residues(Kolodkin et al., 1993 [PubMed 8269517]). Sequence comparisons have grouped the secreted semaphorins into 3 general classes, all of which also have an immunoglobulin domain. The semaphorin III family, consisting of human semaphorin III (SEMA3A; MIM 603961), chicken collapsin, and mouse semaphorins A, D, and E, all have a basic domain at the C terminus. Chicken collapsin contributes to path finding by axons during development by inhibiting extension of growth cones (Luo et al., 1993 [PubMed 8402908]) through an interaction with a collapsin response mediator protein of relative molecular mass 62K (CRMP62) (Goshima et al., 1995 [PubMed7637782]), a putative homolog of an axonal guidance associated UNC33 gene product (MIM 601168). SEMA3F is a secreted member of the semaphorin III family.

Supplier:  Bioss
Description:   A gene on chromosome 20q13.1 encodes Eya2 (eyes absent). EYA2 is one of four members of the eyes absent family. A 271 amino acid domain at the carboxy-terminal is highly conserved amongst the members of the eyes absent family, while the PST (proline-serive-threonin)-rich amino-terminal is highly divergent. EYA2 is expressed relatively late in development in the cytoplasm of extensor tendons and ligaments of the phalangeal elements of the limb, cranial placodes, branchial arches, central nervous system, and the developing eye. Pax3 induces the expression of Eya2 in a cascade that is necessary and sufficient for myogenesis. EYA2, like EYA1, acts as a transcriptional activator in connective tissue patterning through its PST domain, which functions as a transactivation domain. EYA2 is translocated to the nucleus by Six proteins, which interact through their domain and homeodomain with EYA2. EYA2 carboxy-terminal interacts with the G Alpha z and G Alphai 2 proteins. This interaction prevents Six proteins from translocating EYA2 to the nucleus.

Supplier:  Bioss
Description:   Cytokeratins are proteins of keratin-containing intermediate filaments found in the intracytoplasmic cytoskeleton of epithelial tissue. The cytokeratins are encoded by a family encompassing 30 genes. Among them, 20 are epithelial genes and the remaining 10 are specific for trichocytes.
In the cytoplasm, the keratin filaments conform a complex network which extends from the surface of the nucleus to the cell membrane. Numerous accessory proteins are involved in the genesis and maintenance of such structure. This association between the plasma membrane and the nuclear surface provides important implications for the organization of the cytoplasm and cellular communication mechanisms. Apart from the relatively static functions provided in terms of supporting the nucleus and providing tensile strength to the cell, the cytokeratin networks undergo rapid phosphate exchanges mediated depolymerization, with important implications in the more dynamic cellular processes such as mitosis and post-mitotic period, cell movement and differentiation. Cytokeratins interact with desmosomes and hemidesmosomes, thus collaborating to cell-cell adhesion and basal cell-underlying connective tissue connection.

Supplier:  Bioss
Description:   Cytokeratins are proteins of keratin-containing intermediate filaments found in the intracytoplasmic cytoskeleton of epithelial tissue. The cytokeratins are encoded by a family encompassing 30 genes. Among them, 20 are epithelial genes and the remaining 10 are specific for trichocytes.
In the cytoplasm, the keratin filaments conform a complex network which extends from the surface of the nucleus to the cell membrane. Numerous accessory proteins are involved in the genesis and maintenance of such structure. This association between the plasma membrane and the nuclear surface provides important implications for the organization of the cytoplasm and cellular communication mechanisms. Apart from the relatively static functions provided in terms of supporting the nucleus and providing tensile strength to the cell, the cytokeratin networks undergo rapid phosphate exchanges mediated depolymerization, with important implications in the more dynamic cellular processes such as mitosis and post-mitotic period, cell movement and differentiation. Cytokeratins interact with desmosomes and hemidesmosomes, thus collaborating to cell-cell adhesion and basal cell-underlying connective tissue connection.

Supplier:  Bioss
Description:   Cytokeratins are proteins of keratin-containing intermediate filaments found in the intracytoplasmic cytoskeleton of epithelial tissue. The cytokeratins are encoded by a family encompassing 30 genes. Among them, 20 are epithelial genes and the remaining 10 are specific for trichocytes.
In the cytoplasm, the keratin filaments conform a complex network which extends from the surface of the nucleus to the cell membrane. Numerous accessory proteins are involved in the genesis and maintenance of such structure. This association between the plasma membrane and the nuclear surface provides important implications for the organization of the cytoplasm and cellular communication mechanisms. Apart from the relatively static functions provided in terms of supporting the nucleus and providing tensile strength to the cell, the cytokeratin networks undergo rapid phosphate exchanges mediated depolymerization, with important implications in the more dynamic cellular processes such as mitosis and post-mitotic period, cell movement and differentiation. Cytokeratins interact with desmosomes and hemidesmosomes, thus collaborating to cell-cell adhesion and basal cell-underlying connective tissue connection.

Supplier:  Bioss
Description:   The cadherins represent a family of Ca2+-dependent adhesion molecules that function to mediate cell to cell binding that is critical for the maintenance of structure and morphogenesis. Cadherins each contain a large extracellular domain at the N-terminus, which is characterized by a series of five homologous repeats, the most distal of which is thought to be responsible for binding specificity. The relatively short C-terminal intracellular domain interacts with a variety of cytoplasmic proteins, including ∫-catenin, to regulate cadherin function. The cadherin superfamily includes cadherins, protocadherins, desmogleins and desmocollins. FAT3 (FAT tumor suppressor homolog 3, also known as CDHF15 or CDHR10, is a 4,589 amino acid single-pass type I membrane protein expressed in ES cells, primitive neuroectoderm, fetal brain, infant brain, adult neural tissues and prostate. Containing thirty-three cadherin domains, four EGF-like domains and one laminin G-like domain, FAT3 may participate in the interactions between neurites derived from specific subsets of neurons during development.

Supplier:  Bioss
Description:   SerpinB2 is a serine proteinase inhibitor of the ovalbumin like B clade of serpins. It was first discovered in the placenta, and given the name PAI-2 because of the ability to inhibit urokinase plasminogen activator (u-PA) at low micromolar efficiency. SerpinB2 also inhibits tissue plasminogen activator (t-PA), but with micromolar efficiency, and PAI-1 is much more efficient that SerpinB2 on both forms of plasminogen activator. The structure of PAI-2 is not terribly similar to PAI-1, however, which is an E clade serpin. SerpinB2 is made by many cell types, and is found intracellularly as an unglycosylated kDa protein, and secreted as a 60 kDa protein. SerpinB2 is found in saliva, secreted by gingival fibroblasts, and in the skin. SerpinB2 levels are elevated in serum during pregnancy, and in leukemia, breast cancer and ovarian cancer, although it was lowered in some cancers.A shorter SerpinB2 isoform of 382 amino acids, has been reported, with a predicted mass of 43.1 kDa and a pI of 5.69. The shorter form has a deletion just after the start of the mature protein, but it is unclear what the relative production and distribution is for the shorter sequence.
Catalog Number: (10251-570)

Supplier:  Bioss
Description:   The Myc family, including c-Myc-, N-Myc- and L-Myc, are nuclear proteins with relatively short half lives that contribute an important role in cellular processes such as proliferation, differentiation, apoptosis and transformation. The c-Myc protein activates transcription as part of a heteromeric complex with a number of interacting partners, including Max and Mxi 1; however the transforming properties of the Myc proto-oncogene are believed to be associated with Myc-mediated transcriptional repression. A POZ domain Zn finger protein, designated Miz-1 for Myc-interacting Zn finger protein-1, is a specific target of Myc-induced gene repression. Miz-1 interacts with Myc, but not Max or other Myc partners, and binding of Myc to Miz-1 requires the helix-loop-helix domain of Myc and a short amphipathic helix located in the carboxy-terminus of Miz-1. Miz-1 associates with DNA elements on the adenovirus major late and cyclin D1 promoters and activates transcription of both promoters. Expression of Miz-1 induces potent growth arrest function, and this latency is reversed by the addition of Myc.
Supplier:  ACROBIOSYSTEMS INC MS
Description:   Human IL-3 R alpha/CD123 Protein, Fc Tag (MALS & SPR verified), Source: expressed from human 293 cells (HEK293). It contains AA Thr 19 - Arg 305, Predicted N-terminus: Thr 19, protein carries a human IgG1 Fc tag at the C-terminus, Synonyms: IL3R, IL3RA, IL-3Ra, IL-3R-alpha, IL3RAY, Size: 1mg
Supplier:  Spectrum Chemicals
Description:   Sorbitan Trioleate is used in lubricants and rust preventive oils for its corrosion inhibition property. Ungraded products supplied by Spectrum are indicative of a grade suitable for general industrial use or research purposes and typically are not suitable for human consumption or therapeutic use.
Small Business Enterprise
Supplier:  BeanTown Chemical
Description:   CAS: 2004-07-1; EC No: 217-905-3; MDL No: MFCD00005735 Crystalline/Solid; Molecular Formula: C10H12ClN5O4; MW: 301.69 Melting Point: 165-167° (decomposes)
MSDS SDS

Supplier:  Prosci
Description:   C-X-C chemokine receptor type 4 is also known as fusin or CD184 (cluster of differentiation 184), CXCR4, CD184, D2S201E, FB22, HM89, HSY3RR, LAP3, LCR1, LESTR, NPY3R, NPYR, NPYRL, NPYY3R or WHIM. CXCR-4 is an alpha-chemokine receptor specific for stromal-derived-factor-1 (SDF-1 also called CXCL12), a molecule endowed with potent chemotactic activity for lymphocytes. This receptor is one of several chemokine receptors that HIV isolates can use to infect CD4+ T cells. HIV isolates that use CXCR4 are traditionally known as T-cell tropic isolates. Typically, these viruses are found late in infection. It is unclear as to whether the emergence of CXCR4 using HIV is a consequence or a cause of immunodeficiency.CXCR4 is upregulated during the implantation window in natural and hormone replacement therapy cycles in the endometrium, producing, in presence of a human blastocyst, a surface polarization of the CXCR4 receptors suggesting that this receptor is implicated in the adhesion phase of human implantation. SDF-1 and CXCR4 were believed to be a relatively "monogamous" ligand-receptor pair (other chemokines tend to use several different chemokine receptors in a fairly "promiscuous" manner). Recent evidence demonstrates ubiquitin is also a natural ligand of CXCR4. Chronic exposure to THC increased T lymphocyte CXCR4 expression on both CD4+ and CD8+ T lymphocytes. Drugs that block the CXCR4 receptor appear to be capable of "mobilizing" hematopoietic stem cells into the bloodstream as peripheral blood stem cells.

Supplier:  Prosci
Description:   Hemagglutinin Monoclonal 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 can be found. These subtypes are classified based on the combination of the virus coat glycoproteins hemagglutinin (HA) and neuraminidase (NA) subtypes. During 1997, an H5N1 avian influenza virus was determined to be the cause of death in 6 of 18 infected patients in Hong Kong. The more recent virulent strain of H5N1 is now seen in Africa and Europe, as well as in southeast Asia. There is some evidence of human to human spread of this virus, but it is thought that the transmission efficiency was fairly low. HA interacts with cell surface proteins containing oligosaccharides with terminal sialyl residues. Virus isolated from a human infected with the H5N1 strain in 1997 could bind to oligosaccharides from human as well as avian sources, indicating its species-jumping ability. While efforts were made to use relatively conserved regions of the viral sequence as the antigen, the influenza virus genome has drifted somewhat from what was first reported. However, this antibody was able to recognize peptides derrived from viruses from Indonesian human patients infected in 2007.
Supplier:  Matrix Scientific
Description:   MF=C13H18O9 MW=318.28 CAS=13035-61-5 MDL=MFCD00005358 100G

Supplier:  TCI America
Description:   CAS Number: 146-80-5
MDL Number: MFCD00005726
Molecular Formula: C10H12N4O6
Molecular Weight: 284.23
Purity/Analysis Method: >98.0% (HPLC,T)
Form: Crystal
Color: White
Specific rotation [a]20/D: -59 deg (C=1, 0.1mol/L NaOH sol.)
MSDS SDS
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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 call is still displayed and you need assistance, please call us at 1-800-932-5000.
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