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Allylpalladium(II)+chloride+dimer
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Allylpalladium(II)+chloride+dimer
Catalog Number:
(76101-954)
Supplier:
Bioss
Description:
The kinesin motor proteins include at least two forms of conventional kinesin encoded by different genes and designated as ubiquitous kinesin, which is expressed in all cells and tissues, or neuronal kinesin, which is expressed exclusively in neural cells. Kinesin is a microtubule associated protein comprised of three different structural domains. A considerable globular N-terminal domain regulates the hydrolysis of ATP and also microtubule binding while central coiled-coil domains promote heavy chain dimerization. Lastly, small globular C-terminal domains interact with kinesin light chains, membranous organelles and vesicles. Expression of ubiquitous kinesin heavy chain, also designated UKHC, is found subcellularly in areas of heavy vesicular trafficking such as the microtubule pathways of neural cells and also the Golgi of non-neural cell types.
Catalog Number:
(76101-956)
Supplier:
Bioss
Description:
The kinesin motor proteins include at least two forms of conventional kinesin encoded by different genes and designated as ubiquitous kinesin, which is expressed in all cells and tissues, or neuronal kinesin, which is expressed exclusively in neural cells. Kinesin is a microtubule associated protein comprised of three different structural domains. A considerable globular N-terminal domain regulates the hydrolysis of ATP and also microtubule binding while central coiled-coil domains promote heavy chain dimerization. Lastly, small globular C-terminal domains interact with kinesin light chains, membranous organelles and vesicles. Expression of ubiquitous kinesin heavy chain, also designated UKHC, is found subcellularly in areas of heavy vesicular trafficking such as the microtubule pathways of neural cells and also the Golgi of non-neural cell types.
Catalog Number:
(10400-404)
Supplier:
Bioss
Description:
Alpha 1 Fetoprotein is a major plasma protein produced by the yolk sac and the liver during fetal life. Alpha fetoprotein expression in adults is often associated with hepatoma or teratoma. However, hereditary persistance of alpha-fetoprotein may also be found in individuals with no obvious pathology. The protein is thought to be the fetal counterpart of serum albumin, and the alpha fetoprotein and albumin genes are present in tandem in the same transcriptional orientation on chromosome 4. Alpha fetoprotein is found in monomeric as well as dimeric and trimeric forms, and binds copper, nickel, fatty acids and bilirubin. The level of alpha fetoprotein in amniotic fluid is used to measure renal loss of protein to screen for spina bifida and anencephaly. Expression has been documented in human adrenal, liver, ovary, testis, and pancreas. ESTs have been isolated from normal human brain, liver/spleen, embryo and uterus tissue libraries.
Supplier:
AVANTOR PERFORMANCE MATERIALS US
Description:
2,3,5-Triphenyltetrazolium chloride (TTC) 90-100%
Supplier:
AVANTOR PERFORMANCE MATERIALS US
Description:
Pellets. Desiccant, 4 to 8 mesh.
Catalog Number:
(JT0980-1)
Catalog Number:
(JT1582-1)
Supplier:
Biotium
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. They are located in the nucleus, though some estrogen receptors associate with the cell surface membrane and can be rapidly activated by exposure of cells to estrogen. ER-alpha and ER-beta are 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:
(10670-978)
Supplier:
Bioss
Description:
Alpha 1 Fetoprotein is a major plasma protein produced by the yolk sac and the liver during fetal life. Alpha fetoprotein expression in adults is often associated with hepatoma or teratoma. However, hereditary persistance of alpha-fetoprotein may also be found in individuals with no obvious pathology. The protein is thought to be the fetal counterpart of serum albumin, and the alpha fetoprotein and albumin genes are present in tandem in the same transcriptional orientation on chromosome 4. Alpha fetoprotein is found in monomeric as well as dimeric and trimeric forms, and binds copper, nickel, fatty acids and bilirubin. The level of alpha fetoprotein in amniotic fluid is used to measure renal loss of protein to screen for spina bifida and anencephaly. Expression has been documented in human adrenal, liver, ovary, testis, and pancreas. ESTs have been isolated from normal human brain, liver/spleen, embryo and uterus tissue libraries.
Catalog Number:
(10447-532)
Supplier:
Bioss
Description:
Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein. Isoform 5, isoform 6, isoform 7 and isoform 8 lack the catalytic site and may interfere with the pro-apoptotic activity of the complex.
Catalog Number:
(10451-840)
Supplier:
Bioss
Description:
Cell surface receptor for Reelin (RELN) and apolipoprotein E (apoE)-containing ligands. LRP8 participates in transmitting the extracellular Reelin signal to intracellular signaling processes, by binding to DAB1 on its cytoplasmic tail. Reelin acts via both the VLDL receptor (VLDLR) and LRP8 to regulate DAB1 tyrosine phosphorylation and microtubule function in neurons. LRP8 has higher affinity for Reelin than VLDLR. LRP8 is thus a key component of the Reelin pathway which governs neuronal layering of the forebrain during embryonic brain development. Binds the endoplasmic reticulum resident receptor-associated protein (RAP). Binds dimers of beta 2-glycoprotein I and may be involved in the suppression of platelet aggregation in the vasculature. Highly expressed in the initial segment of the epididymis, where it affects the functional expression of clusterin and phospholipid hydroperoxide glutathione peroxidase (PHGPx), two proteins required for sperm maturation. May also function as an endocytic receptor.
Catalog Number:
(10749-878)
Supplier:
Prosci
Description:
MAPKAP1 Antibody: MAPKAP1 was initially identified as the human homolog of S. pombe SIN1. Recent evidence has shown that it identical to Mip1, a protein that interacts with MEKK2, a member of the mitogen-activated protein kinase (MAPK) intracellular signaling network. MAPKAP1 is thought to prevent MEKK2 activation and dimerization by forming a complex with the inactive and non-phosphorylated MEKK2, thereby blocking the JNK1/2, ERK1/2, p38 and ERK5 MAPKs. MAPKAP1 has also been shown to play a role in the TOR signaling process, a pathway that is involved in controlling cell growth and proliferation in response to environmental cues such as nutrients, growth factors and hormones. Experiments showed that MAPKAP1 helped to maintain the TOR/rictor assembly but not the TOR/RAPTOR complex, which allowed specific phosphorylation of Akt, a kinase that is believed to couple the growth factor-PI3K signaling pathway to the nutrient-regulated TOR signaling pathway. Multiple alternatively spliced isoforms of MAPKAP1 have been identified.
Catalog Number:
(76100-952)
Supplier:
Bioss
Description:
Transmembrane serine/threonine kinase forming with the TGF-beta type I serine/threonine kinase receptor, TGFBR1, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFRB1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways.
Catalog Number:
(10283-880)
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.
Catalog Number:
(10288-154)
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.
Catalog Number:
(10274-784)
Supplier:
Bioss
Description:
The protein encoded by this gene is a member of the platelet-derived growth factor family. The four members of this family are mitogenic factors for cells of mesenchymal origin and are characterized by a motif of eight cysteines. This gene product can exist either as a homodimer (PDGF-BB) or as a heterodimer with the platelet-derived growth factor alpha polypeptide (PDGF-AB), where the dimers are connected by disulfide bonds. Mutations in this gene are associated with meningioma. Reciprocal translocations between chromosomes 22 and 7, at sites where this gene and that for COL1A1 are located, are associated with a particular type of skin tumor called dermatofibrosarcoma protuberans resulting from unregulated expression of growth factor. Two alternatively spliced transcript variants encoding different isoforms have been identified for this gene. [provided by RefSeq, Oct 2008].
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