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(S)-6,6-Dimethylmorpholine-3-carboxylic+acid+hydrochloride
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(S)-6,6-Dimethylmorpholine-3-carboxylic+acid+hydrochloride
Catalog Number:
(10241-510)
Supplier:
Bioss
Description:
Spectrins are a family of filamentous cytoskeletal proteins that function as essential scaffold proteins that stabilize the plasma membrane and organize intracellular organelles. Spectrins are composed of alpha and beta dimers that associate to form tetramers linked in a head-to-head arrangement. This gene encodes an alpha spectrin that is specifically expressed in nonerythrocytic cells. The encoded protein has been implicated in other cellular functions including DNA repair and cell cycle regulation. Mutations in this gene are the cause of early infantile epileptic encephalopathy-5. Alternate splicing results in multiple transcript variants.[provided by RefSeq, Sep 2010].
Catalog Number:
(10287-528)
Supplier:
Bioss
Description:
The steroid receptor superfamily acts through direct association with DNA sequences known as hormone response elements (HREs) and binds DNA as either homo- or heterodimers. The promiscuous mediator of heterodimerization, RXR, is the receptor for 9-cis retinoic acid, and dimerizes with VDR, TR, PPAR, and several novel receptors including LXR (also referred to as RLD-1) and FXR. FXR and LXR fall into a category of proteins termed “orphan receptors†because of their lack of a defined function, and in the case of LXR, the lack of a defined ligand. FXR has been shown to bind a class of lipid molecules called farnesoids. LXR/RXR heterodimers have highest affinity for DR-4 DNA elements while FXR/RXR heterodimers bind IR-1 elements. Both LXR/RXR and FXR/RXR heterodimers retain their responsiveness to 9-cis retinoic acid.
Catalog Number:
(10287-536)
Supplier:
Bioss
Description:
The steroid receptor superfamily acts through direct association with DNA sequences known as hormone response elements (HREs) and binds DNA as either homo- or heterodimers. The promiscuous mediator of heterodimerization, RXR, is the receptor for 9-cis retinoic acid, and dimerizes with VDR, TR, PPAR, and several novel receptors including LXR (also referred to as RLD-1) and FXR. FXR and LXR fall into a category of proteins termed “orphan receptors†because of their lack of a defined function, and in the case of LXR, the lack of a defined ligand. FXR has been shown to bind a class of lipid molecules called farnesoids. LXR/RXR heterodimers have highest affinity for DR-4 DNA elements while FXR/RXR heterodimers bind IR-1 elements. Both LXR/RXR and FXR/RXR heterodimers retain their responsiveness to 9-cis retinoic acid.
Catalog Number:
(10481-084)
Supplier:
Bioss
Description:
Collapsin response mediator proteins (CRMPs) are cytosolic phosphoproteins involved in neuronal differentiation and axonal guidance. CRMP2 was previously shown to mediate the repulsive effect of Sema3A on axons and to participate in axonal specification. The CRMPs appear to play a complex role in axon growth as well as microtubule dynamics and axon induction. CRMPs localize to the lamellipodia and filopodia of axonal growth cones, suggesting a role in axon guidance. Moreover, CRMP2 is upregulated after axotomy, and appears to increase the formation of axon-type processes from hippocampal neurons. CRMP2 has been reported to bind tubulin dimers directly and modulate microtubule assembly. CRMPs have also been implicated in the pathogenesis of a paraneoplastic neurologic syndrome. Interaction studies have implicated phospholipase D2 (PLD2), the cytosolic tyrosine kinase Fes, and intersectin in CRMP function. Hyperphosphorylation of CRMP2 is an early event in the progression of Alzheimer's disease.
Catalog Number:
(10447-534)
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:
(10481-086)
Supplier:
Bioss
Description:
Collapsin response mediator proteins (CRMPs) are cytosolic phosphoproteins involved in neuronal differentiation and axonal guidance. CRMP2 was previously shown to mediate the repulsive effect of Sema3A on axons and to participate in axonal specification. The CRMPs appear to play a complex role in axon growth as well as microtubule dynamics and axon induction. CRMPs localize to the lamellipodia and filopodia of axonal growth cones, suggesting a role in axon guidance. Moreover, CRMP2 is upregulated after axotomy, and appears to increase the formation of axon-type processes from hippocampal neurons. CRMP2 has been reported to bind tubulin dimers directly and modulate microtubule assembly. CRMPs have also been implicated in the pathogenesis of a paraneoplastic neurologic syndrome. Interaction studies have implicated phospholipase D2 (PLD2), the cytosolic tyrosine kinase Fes, and intersectin in CRMP function. Hyperphosphorylation of CRMP2 is an early event in the progression of Alzheimer's disease.
Catalog Number:
(10800-224)
Supplier:
Rockland Immunochemical
Description:
The ATM/ATR-substrate CHK2-interacting zinc finger protein (ATMIN), also known as ASCIZ, forms DNA damage-induced nuclear foci that contain the DNA repair protein Rad51 (1). ATMIN is also thought to be involved in embryonic development, as an absence of ATMIN causes late-embryonic lethality in mice with a range of organ development defects (2). It also activates the transcription DYNLL1, a light chain of the dynein motor complex and sequence-specific regulator of protein dimerization of numerous targets. DYNLL1 can bind to and inhibit the transcription activation domain of ATMIN, forming a simple dynamic feedback loop for DYNLL1 expression (3).
Catalog Number:
(10451-844)
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.
Supplier:
PeproTech, Inc.
Description:
GDNF is a disulfide-linked, homodimeric neurotrophic factor structurally related to Artemin, Neurturin and Persephin. These proteins belong to the cysteine-knot superfamily of growth factors that assume stable dimeric protein structures. GDNF signals through a multicomponent receptor system, composed of a RET and one of the four GFRα (α1-α4) receptors. GDNF specifically promotes dopamine uptake and survival, and morphological differentiation of midbrain neurons. Using a Parkinson’s disease mouse model, GDNF has been shown to improve conditions such as bradykinesia, rigidity, and postural instability. The functional murine GDNF ligand is a disulfide-linked homodimer consisting of two 15.1 kDa polypeptide chains called monomers. Each monomer contains seven conserved cysteine residues, including Cys-101, which is used for inter-chain disulfide bridging, and others that are involved in the intramolecular ring formation known as the cysteine knot configuration. The calculated molecular weight of Recombinant Murine GDNF is 30.2 kDa.
Supplier:
PeproTech, Inc.
Description:
Persephin is a disulfide-linked, homodimeric, neurotrophic factor structurally related to GDNF, artemin, and neurturin. These proteins belong to the cysteine knot family of growth factors that assume stable dimeric structures. Persephin signals through a multicomponent receptor system, composed of RET and one of four GFR α (α1-α4) receptors. The GFRα4 was first identified in chicken, and was later shown to be the preferential binding subunit for persephin. Persephin promotes the survival of ventral midbrain dopaminergic neurons and motor neurons after sciatic nerve oxotomy, and, like GDNF, promotes ureteric bud branching. However, in contrast to GDNF and neurturin, persephin does not support the survival of peripheral neurons. Recombinant Human Persephin is a disulfide-linked homodimer, composed of two 10.4 kDa polypeptide chains (194 total amino acid residues). Each chain contains seven conserved cysteine residues, one of which (Cys 64) is used for inter-chain disulfide bridging, and the others are involved in the intramolecular ring formation known as the cysteine knot configuration.
Catalog Number:
(77436-992)
Supplier:
Bioss
Description:
The protein encoded by this gene is a member of the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intra-cellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This protein is a member of the ALD subfamily, which is involved in peroxisomal import of fatty acids and/or fatty acyl-CoAs in the organelle. All known peroxisomal ABC transporters are half transporters which require a partner half transporter molecule to form a functional homodimeric or heterodimeric transporter. The function of this peroxisomal membrane protein is unknown; however this protein is speculated to function as a dimerization partner of ABCD1 and/or other peroxisomal ABC transporters. Mutations in this gene have been observed in patients with adrenoleukodystrophy, a severe demyelinating disease. This gene has been identified as a candidate for a modifier gene, accounting for the extreme variation among adrenoleukodystrophy phenotypes. This gene is also a candidate for a complement group of Zellweger syndrome, a genetically heterogeneous disorder of peroxisomal biogenesis. [provided by RefSeq, Jul 2008]
Catalog Number:
(76234-894)
Supplier:
Rockland Immunochemical
Description:
Rockland produces a wide range of human GST antibodies in our laboratories. Select appropriate GST antibodies for your research by isotype, epitope, applications and species reactivity. There are 22 members of the human GST family of proteins. GST is responsible for the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. The amino acid sequence GST is highly conserved in most organisms including mammals. GSTs proteins are typically homodimeric, with both heterologous GST dimers have been observed. GST monomers have an average molecular weight of approximately 25-28 kDa in size. Note a different form of non-human GST (Glutathione-S-Transferase) is used as a protein expression tag commonly in molecular biology applications. All anti-GST antibodies my not react with recombinant GST-fusion proteins.
Supplier:
PeproTech, Inc.
Description:
PDGFs are disulfide-linked dimers consisting of two 12.0-13.5 kDa polypeptide chains, designated PDGF-A and PDGF-B chains. The three naturally occurring PDGFs, PDGF-AA, PDGF-BB and PDGF-AB, are potent mitogens for a variety of cell types, including smooth muscle cells, connective tissue cells, bone and cartilage cells, and some blood cells. The PDGFs are stored in platelet α-granules, and are released upon platelet activation. The PDGFs are involved in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubule epithelial cell development. Two distinct signaling receptors used by PDGFs have been identified and named PDGFR-α and PDGFR-β. PDGFR-α is high-affinity receptor for each of the three PDGF forms. On the other hand, PDGFR-β interacts with only PDGF-BB and PDGF-AB. Recombinant Human PDGF-AA is a 28.5 kDa disulfide-linked homodimer of two α chains (250 total amino acids).
Catalog Number:
(89358-928)
Supplier:
Genetex
Description:
Superoxide dismutase (SOD) is responsible for the elimination of cytotoxic active oxygen by catalyzing the dismutation of the superoxide radical to oxygen and hydrogen peroxide. There are three SOD isoenzymes in mammalian cells. They are: extracellular SOD (EC SOD), copper and zinc-containing SOD (Cu/Zn SOD) and manganese-containing SOD (Mn SOD). The Cu/Zn form contains Cu and Zn ions and exists as a 32 kDa dimer in the cytosol. Mn SOD is an 80 kDa tetramer that contains Mn ion and resides in the mitochondrial matrix. Mn SOD is a tumor necrosis factor (TNF)-inducible enzyme that protects cells from TNF-mediated apoptosis via superoxide anion detoxification and the subsequent regulation of apoptosis through cytochrome c release and the modulation of the redox state of the mitochondria. Mn SOD has also been shown to be a tumor suppressor in human breast cancer. Overexpression of this enzyme protects neurons from NMDA- and nitric oxide-induced neurotoxicity.
Catalog Number:
(10668-276)
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:
(76116-650)
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.
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