Allylpalladium(II)+chloride+dimer
Catalog Number:
(10291-104)
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:
(10282-342)
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:
(10282-344)
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:
(10291-102)
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:
(10294-898)
Supplier:
Bioss
Description:
GARNL1 is expressed during embryogenesis with E12. During development, GARNL1 expression decreases, persisting at high levels only in neurons of the adult brain. GARNL1 localizes to the cytoplasm where it may play a role regulating GTP hydrolysis of proteins such as Ran and Rap. GARNL1 is imported to the nucleus via dimerization with E12. GARNL1 interacts with the HLH region of E12 and may function to negatively regulate the transcription of E12-dependent downstream target genes. This suggests that at least a portion of the function of GARNL1 is dependent upon its association with E12. GARNL1 may also associate with other HLH proteins and influence a variety of HLH signaling cascades. In adult brain, GARNL1 activity does not involve E12 and therefore it may serve a different function in developed neural tissue.
Catalog Number:
(10291-096)
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:
(10280-282)
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:
(10303-070)
Supplier:
Bioss
Description:
Zinc-finger proteins contain DNA-binding domains and have a wide variety of functions, most of which encompass some form of transcriptional activation or repression. The majority of zinc-finger proteins contain a Krüppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. Zinc finger and BTB domain-containing protein 43 (ZBTB43), also known as ZNF297B or ZBTB22B, is a 467 amino acid member of the Krüppel C2H2-type zinc-finger protein family. Localized to the nucleus, ZBTB43 contains a BTB domain, also known as a POZ domain, which inhibits DNA binding and mediates homotypic and heterotypic dimerization. Characteristics of the BTB domain and the interaction of ZBTB43 with BDP1 suggest that ZBTB43 functions as a transcription regulator.
Catalog Number:
(10303-084)
Supplier:
Bioss
Description:
Zinc-finger proteins contain DNA-binding domains and have a wide variety of functions, most of which encompass some form of transcriptional activation or repression. The majority of zinc-finger proteins contain a Krüppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. Zinc finger and BTB domain-containing protein 43 (ZBTB43), also known as ZNF297B or ZBTB22B, is a 467 amino acid member of the Krüppel C2H2-type zinc-finger protein family. Localized to the nucleus, ZBTB43 contains a BTB domain, also known as a POZ domain, which inhibits DNA binding and mediates homotypic and heterotypic dimerization. Characteristics of the BTB domain and the interaction of ZBTB43 with BDP1 suggest that ZBTB43 functions as a transcription regulator.
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.
CF® dyes are Biotium's next-generation fluorescent dyes. CF®568 is a red fluorescent dye (Ex/Em 562/583 nm) with superior brightness and photostability. It also is compatible with super-resolution imaging by STORM and TIRF.
Catalog Number:
(76110-080)
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. TRIM50 (tripartite motif containing 50), also known as TRIM50A or E3 ubiquitin-protein ligase TRIM50, is a 487 amino acid cytoplasmic protein that functions as an E3 ubiquitin-protein ligase. Containing one RING-type zinc finger, a B30.2/SPRY domain and a single B box-type zinc finger, TRIM50 belongs to the TRIM/RBCC family and undergoes post-translational auto-ubiquitination. TRIM50 exists as two alternatively spliced isoforms, designated TRIM50 alpha and TRIM50 beta, and has the ability to form dimers and trimers. The gene encoding TRIM50 maps to human chromosome 7, which houses over 1,000 genes, comprises nearly 5% of the human genome and has been linked to Osteogenesis imperfecta, Pendred syndrome, Lissencephaly, Citrullinemia and Shwachman-Diamond syndrome.
Catalog Number:
(102552-836)
Supplier:
BioVendor
Description:
Trefoil factor 3 (TFF3, also known as intestinal trefoil factor) belongs together with TFF1 and TFF2 to a small group of mucin-associated peptides. TFF3 contains seven cysteine residues, six of which form disulfide bonds to create a characteristic three-leafed structure. Due to its compact structure, TFF3 is extremely resistant toward acids, proteolytical cleavage or heat degradation. Monomeric form of TFF3 consists of 60 amino acids and has 6.7 kDa, while the dimer (13.1 kDa) consists of 118 amino acids. TFF3 is expressed mainly in gastrointestinal tract, in the mucous cells of the small and large intestine, where it maintains the integrity of mucous layer and in cooperation with mucins protects the gastrointestinal epithelial cells against various injurious agents. However, TFF3 was also detected in salivary glands, posterior pituitary gland and in the inner ear. Secretion of TFF3 is triggered by the presence of certain inflammation mediators and neurotransmitters.
Catalog Number:
(75928-826)
Supplier:
Rockland Immunochemical
Description:
Anti-Human IgG F(ab')2 Antibody generated in goat recognizes the dimeric Fab portion of the human IgG molecule. Human IgG F(ab')2 is a proteolytic fragment of immunoglobulin G (IgG) obtained by limited digestion with the enzyme pepsin under controlled conditions of temperature, time and pH. F(ab')2 molecules lack the Fc portion of IgG and therefore receptors that bind human IgG F(c) will not bind human IgG F(ab')2 molecules. Secondary Antibodies are available in a variety of formats and conjugate types. When choosing a secondary antibody product, consideration must be given to species and immunoglobulin specificity, conjugate type, fragment and chain specificity, level of cross-reactivity, and host-species source and fragment composition. Anti-Human IgG F(ab')2 fragment antibody is ideal for investigators in Immunology, Cancer, and Microbiology research.
Catalog Number:
(75932-928)
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 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:
(75932-930)
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 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:
(76193-842)
Supplier:
Prosci
Description:
Estrogen receptor (ER) is an important regulator of growth and differentiation in the mammary gland. It is found in two forms, alpha and beta. Both forms are widely expressed, however, alpha is the predominant form in endometrium and breast cancer cells, and beta is more highly expressed in brain, kidney, heart, lung and bone. Activated Estrogen receptor dimerizes and forms both homo- and heterodimers. ER contains five domains: A-F. The A and B domain are able to weakly activate ER in the absence of ligand. The C domain binds DNA and the E domain contains the ligand binding site. Presence of ER in breast tumors indicates an increased likelihood of response to anti-estrogen (e.g. tamoxifen) therapy. This antibody is specific to estrogen receptor alpha and shows minimal cross-reaction with other members of the family.
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