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Allylpalladium(II)+chloride+dimer
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Allylpalladium(II)+chloride+dimer
Supplier:
Biotium
Description:
CD309, also known as VEGFR2, KDR3, and Flk-1 (mouse), is a type I transmembrane glycoprotein. It is a member of the CSF-1/PDGF receptor family of type III tyrosine kinase receptors. Human VEGFR2 is mainly expressed by endothelial cells, embryonic tissues, and megakaryocytes. It plays an important role in the regulation of angiogenesis, vasculogenesis, and vascular permeability. The ligands of VEGFR2 include VEGF-A, VEGF-C, VEGF-D, and VEGF splice isoforms. Ligation of VEGFR2 with its ligands results in the receptor dimerization and auto-phosphorylation, stimulating endothelial cell proliferation and migration.
CF® dyes are Biotium's next-generation fluorescent dyes. CF®640R is a far-red fluorescent dye (Ex/Em 642/662 nm) with excellent brightness, and the best photostabiity among spectrally-similar dyes.
Catalog Number:
(10410-612)
Supplier:
Bioss
Description:
The androgen receptor gene is more than 90 kb long and codes for a protein that has 3 major functional domains: the N-terminal domain, DNA-binding domain, and androgen-binding domain. The protein functions as a steroid-hormone activated transcription factor. Upon binding the hormone ligand, the receptor dissociates from accessory proteins, translocates into the nucleus, dimerizes, and then stimulates transcription of androgen responsive genes. This gene contains 2 polymorphic trinucleotide repeat segments that encode polyglutamine and polyglycine tracts in the N-terminal transactivation domain of its protein. Expansion of the polyglutamine tract causes spinal bulbar muscular atrophy (Kennedy disease). Mutations in this gene are also associated with complete androgen insensitivity (CAIS). Two alternatively spliced variants encoding distinct isoforms have been described. [provided by RefSeq, Jul 2008]
Catalog Number:
(76083-548)
Supplier:
Bioss
Description:
Fibroblast growth factors (FGFs) produce mitogenic and angiogenic effects in target cells by signaling through the cellular surface tyrosine kinase receptors. There are four members of the FGF receptor family: FGFR-1 (flg), FGFR-2 (bek, KGFR), FGFR-3 and FGFR-4. Each receptor contains an extracellular ligand binding domain, a transmembrane region and a cytoplasmic kinase domain (1). Following ligand binding and dimerization, the receptors are phosphorylated at specific tyrosine residues (2). Seven tyrosine residues in the cytoplasmic tail of FGFR-1 can be phosphorylated: Tyr463, Tyr583, Tyr585, Tyr653, Tyr654, Tyr730 and Tyr766. Tyrosine 653 and 654 are important for catalytic activity of the activated FGFR and are essential for signaling (3). The other phosphorylated tyrosine residues may provide docking sites for downstream signaling components such as Crk and PLCgamma.
Catalog Number:
(10749-760)
Supplier:
Prosci
Description:
TLR6 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 TLRs act through adaptor molecules such as MyD88 and TIRAP to activate various kinases and transcription factors so the organism can respond to potential infection. TLR6 was first identified as a close homolog of TLR1, sharing 69% sequence identify. Like TLR1, TLR6 can form heterodimers with TLR2, and these TLR6:TLR2 dimers coordinate macrophage activation by Gram-positive bacteria and the yeast cell wall particle zymosan. Activation of these complexes not only initiates pro-inflammatory cascades, but also can lead to apoptotic responses.
Catalog Number:
(89415-946)
Supplier:
Prosci
Description:
TLR6 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 TLRs act through adaptor molecules such as MyD88 and TIRAP to activate various kinases and transcription factors so the organism can respond to potential infection. TLR6 was first identified as a close homolog of TLR1, sharing 69% sequence identify. Like TLR1, TLR6 can form heterodimers with TLR2, and these TLR6:TLR2 dimers coordinate macrophage activation by Gram-positive bacteria and the yeast cell wall particle zymosan. Activation of these complexes not only initiates pro-inflammatory cascades, but also can lead to apoptotic responses.
Catalog Number:
(10668-284)
Supplier:
Bioss
Description:
The tripartite motif (TRIM) family of proteins are characterized by a conserved TRIM domain that includes a coiled-coil region, a B-box type zinc finger, one RING finger and three zinc-binding domains. TRIM7 (tripartite motif-containing 7), also known as RNF90 or GNIP, is a 511 amino acid protein that belongs to the TRIM family and contains one RING-type zinc finger, one B box-type zinc finger and one SPRY domain. Expressed in placenta and skeletal muscle and present at lower levels in brain, heart and pancreas, TRIM7 localizes to both the cytoplasm and the nucleus where it exists as dimers and is thought to participate in the initiation of glycogen synthesis. Multiple isoforms of TRIM7 exist due to alternative splicing events.
Catalog Number:
(10668-282)
Supplier:
Bioss
Description:
The tripartite motif (TRIM) family of proteins are characterized by a conserved TRIM domain that includes a coiled-coil region, a B-box type zinc finger, one RING finger and three zinc-binding domains. TRIM7 (tripartite motif-containing 7), also known as RNF90 or GNIP, is a 511 amino acid protein that belongs to the TRIM family and contains one RING-type zinc finger, one B box-type zinc finger and one SPRY domain. Expressed in placenta and skeletal muscle and present at lower levels in brain, heart and pancreas, TRIM7 localizes to both the cytoplasm and the nucleus where it exists as dimers and is thought to participate in the initiation of glycogen synthesis. Multiple isoforms of TRIM7 exist due to alternative splicing events.
Catalog Number:
(10412-428)
Supplier:
Bioss
Description:
E2F's are DNA binding proteins, which associate with negative regulators, such as the retinoblastoma p107 protein, resulting in an altered rate of gene transcription. The E2F proteins contain several evolutionally conserved domains found in most members of the family. These domains include a DNA binding domain, a dimerization domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids, and a tumor suppressor protein association domain which is embedded within the transactivation domain. This protein and another 2 members, E2F2 and E2F3, have an additional cyclin binding domain. E2F1 is proposed to be involved in several cellular processes that range from tumor suppressor, cell progression and oncogenesis. E2F1 overexpression can also drive cells into apoptosis.
Catalog Number:
(10413-400)
Supplier:
Bioss
Description:
Fibroblast growth factors (FGFs) produce mitogenic and angiogenic effects in target cells by signaling through the cellular surface tyrosine kinase receptors. There are four members of the FGF receptor family: FGFR-1 (flg), FGFR-2 (bek, KGFR), FGFR-3 and FGFR-4. Each receptor contains an extracellular ligand binding domain, a transmembrane region and a cytoplasmic kinase domain (1). Following ligand binding and dimerization, the receptors are phosphorylated at specific tyrosine residues (2). Seven tyrosine residues in the cytoplasmic tail of FGFR-1 can be phosphorylated: Tyr463, Tyr583, Tyr585, Tyr653, Tyr654, Tyr730 and Tyr766. Tyrosine 653 and 654 are important for catalytic activity of the activated FGFR and are essential for signaling (3). The other phosphorylated tyrosine residues may provide docking sites for downstream signaling components such as Crk and PLCgamma.
Catalog Number:
(10412-422)
Supplier:
Bioss
Description:
E2F's are DNA binding proteins, which associate with negative regulators, such as the retinoblastoma p107 protein, resulting in an altered rate of gene transcription. The E2F proteins contain several evolutionally conserved domains found in most members of the family. These domains include a DNA binding domain, a dimerization domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids, and a tumor suppressor protein association domain which is embedded within the transactivation domain. This protein and another 2 members, E2F2 and E2F3, have an additional cyclin binding domain. E2F1 is proposed to be involved in several cellular processes that range from tumor suppressor, cell progression and oncogenesis. E2F1 overexpression can also drive cells into apoptosis.
Catalog Number:
(10390-814)
Supplier:
Bioss
Description:
PKA (or cAPK) is a cyclic AMP dependent protein kinase. When activated by the second messenger cAMP, PKA mediates diverse cellular mechanisms, including proliferation, ion transport, regulation of metabolism, plus gene transcription. PKA is comprised of two dimers of two subunits, R (regulatory) and C (catalytic). Two families of R subunit (RI and RII) and three C subunit isoforms (C alpha, C beta, and C gamma) have been identified each possessing distinct cAMP binding properties and resulting in different phosphorylation states. C subunit is activated through autophosphorylation and direct phosphorylation at Thr197 by PDK-1. Tissue specific expression of C gamma, indicates pressure on C gamma during evolution, acting to modulate it in a functionally specific way. Certain amino acid substitutions make C gamma a distinct member of the cAMP dependent subfamily of protein kinases, and suggest that C gamma may be distinct in its protein substrate specificity or its interaction with the different regulatory subunits.
Catalog Number:
(10061-790)
Supplier:
Prosci
Description:
Alpha-tubulin Antibody: Alpha-tubulin belongs to the tubulin superfamily, which is composed of six distinct families. Along with beta-tubulins, alpha-tubulins are the major components of microtubules. These microtubules are involved in a wide variety of cellular activities ranging from mitosis and transport events to cell movement and the maintenance of cell shape. Alpha- and beta-tubulin dimers are assembled to 13 protofilaments that form a microtubule of 22-nm diameter. Tyrosine ligase adds a C-terminal tyrosine to monomeric alpha-tubulin. Assembled microtubules can again be detyrosinated by a cytoskeleton-associated carboxypeptidase. Another post-translational modification of detyrosinated alpha-tubulin is C-terminal polyglutamylation, which is characteristic of microtubules in neuronal cells and the mitotic spindle. Like GAPDH and beta-Actin, this antibody makes an excellent loading control in immunoblots.
Supplier:
Thermo Scientific Chemicals
Description:
Fieser: 8,327 9,49 10,39 11,54 12,59 13,38 15,37 16,37
Catalog Number:
(10463-358)
Supplier:
Bioss
Description:
B-ATF is a nuclear basic leucine zipper protein that belongs to the AP-1/ATF superfamily of transcription factors. The leucine zipper of B-ATF mediates dimerization with members of the Jun family of proteins. The B-ATF protein does not homodimerize efficiently, but rather forms a heterodimer preferentially with c-Jun. The B-ATF/c-Jun protein complex can interact with DNA containing a consensus binding site for AP-1, suggesting that B-ATF functions as a tissue-specific modulator of the AP-1 transcription complex in human cells. B-ATF also associates with IFP35, a leucine zipper protein that translocates to the nucleus following IFN treatment. The gene encoding B-ATF, also designated SFA-2, is strongly expressed in mature T and B lymphocytes, and is up-regulated after transformation by human T-cell leukemia virus type I.
Catalog Number:
(10458-618)
Supplier:
Bioss
Description:
Estrogen receptors (ER) are members of the steroid/thyroid hormone receptor superfamily of ligand-activated transcription factors. Estrogen receptors, including ER alpha and ER beta, contain DNA binding and ligand binding domains and are critically involved in regulating the normal function of reproductive tissues. ER alpha and ER beta A have been shown to be differentially activated by various ligands. Receptor-ligand interactions trigger a cascade of events, including dissociation from heat shock proteins, receptor dimerization, phosphorylation and the association of the hormone activated receptor with specific regulatory elements in target genes. Evidence suggests that ER alpha and ER beta may be regulated by distinct mechanisms even though they share many functional characteristics.
Catalog Number:
(75976-480)
Supplier:
Biotium
Description:
This MAb recognizes TGF beta 1, 2 and 3. Three TGF betas have been identified in mammals. TGF beta 1, TGF beta 2 and TGF beta 3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecules. Biologically active TGF beta requires dimerization of the monomers (usually homodimers) and release of the latent peptide portion. Overall, the mature region of the TGF beta 3 protein has approximately 80% identity to the mature region of both TGF beta 1 and TGF beta 2. However, the NH2 terminals or precursor regions of their molecules share only 27% sequence identity. TGF betas inhibit the growth of epithelial cells and stimulate the growth of mesenchymal cells.
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is still displayed and you need assistance, please call us at 1-800-932-5000.
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