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Allylpalladium(II)+chloride+dimer


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Catalog Number: (10272-892)

Supplier:  Bioss
Description:   SRCAP (Snf2-related CREBBP activator protein), also known as EAF1, SWR1, or DOMO1, is a 3,230 amino acid protein that belongs to a family of helicases and contains one HSA domain, one helicase C-terminal domain, one helicase ATP-binding domain and three A.T hook DNA-binding domains. Localized to the nucleus, SRCAP functions as a catalytic component of the SRCAP complex, a multi-protein structure that mediates the ATP-dependent exchange of histone dimers for nucleosomal histones, an event that regulates the transcription of select genes via chromatin remodeling. Additionally, the SRCAP complex acts as a coactivator for steroid receptor-mediated transcription, Notch-mediated transcription and CREB-mediated transcription. SRCAP is expressed as multiple alternatively spliced isoforms and is subject to DNA damage-dependent phosphorylation by ATM or ATR.

Supplier:  Bioss
Description:   The cJun proto-oncogene was first identified as the cellular homolog of the avian sarcoma virus vjun oncogene. JunB and JunD have been shown to be almost identical to cJun in their C terminal regions, which are involved in dimerization and DNA binding, whereas their N terminal domains, which are involved in transcriptional activation, diverge. JunB is a transcription factor involved in regulating gene activity following the primary growth factor response. It binds to the DNA sequence 5'-TGA[CG]TCA-3'.The protein encoded by this intronless gene is a member of the JUN family, and a functional component of the AP1 transcription factor complex. It has been proposed to protect cells from p53-dependent senescence and apoptosis. Alternate translation initiation site usage, including non-AUG codons, results in the production of different isoforms.
Supplier:  AVANTOR PERFORMANCE MATERIALS US
Description:   Pyrogen tested.
MSDS SDS
Catalog Number: (10282-328)

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: (10295-684)

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.

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.

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.

Supplier:  Bioss
Description:   14-3-3 proteins regulate many cellular processes relevant to cancer biology, notably apoptosis, mitogenic signaling and cell-cycle checkpoints. Seven isoforms comprise this family of signaling intermediates, denoted 14-3-3 b, g, e, z, h, q and s. 14-3-3 proteins form dimers that present two binding sites for ligand proteins, thereby bringing together two proteins that may not otherwise associate. These ligands largely share a 14-3-3 consensus binding motif and exhibit serine/threonine phosphorylation. 14-3-3 proteins function in broad regulation of these ligand proteins; by cytoplasmic sequestration, occupation of interaction domains and import/export sequences, prevention of degradation, activation/repression of enzymatic activity, and facilitation of protein modification. Loss of expression contributes to a vast array of pathogenic cellular activities.

Supplier:  Bioss
Description:   14-3-3 proteins regulate many cellular processes relevant to cancer biology, notably apoptosis, mitogenic signaling and cell-cycle checkpoints. Seven isoforms comprise this family of signaling intermediates, denoted 14-3-3 b, g, e, z, h, q and s. 14-3-3 proteins form dimers that present two binding sites for ligand proteins, thereby bringing together two proteins that may not otherwise associate. These ligands largely share a 14-3-3 consensus binding motif and exhibit serine/threonine phosphorylation. 14-3-3 proteins function in broad regulation of these ligand proteins; by cytoplasmic sequestration, occupation of interaction domains and import/export sequences, prevention of degradation, activation/repression of enzymatic activity, and facilitation of protein modification. Loss of expression contributes to a vast array of pathogenic cellular activities.

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 protein. ZBTB44 is a 570 amino acid member of the Krüppel C2H2-type zinc-finger protein family. Localized to the nucleus, ZBTB44 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 suggest that ZBTB44 functions as a transcription regulator. Four isoforms of ZBTB44 have been identified.

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 protein. ZBTB44 is a 570 amino acid member of the Krüppel C2H2-type zinc-finger protein family. Localized to the nucleus, ZBTB44 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 suggest that ZBTB44 functions as a transcription regulator. Four isoforms of ZBTB44 have been identified.
Supplier:  AVANTOR PERFORMANCE MATERIALS US
Description:   AR—The standard Macron Fine Chemicals™ grade of analytical reagents; suitable for laboratory and general use.
MSDS SDS
Catalog Number: (10282-314)

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]

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:  AVANTOR PERFORMANCE MATERIALS US
Description:   Desiccant, 20 mesh. Lot analysis on label.
Supplier:  AVANTOR PERFORMANCE MATERIALS US
Description:   Sodium chloride 99,0 - 100,5% 99.0-100.5% (dried basis), crystals USP, FCC
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