"Bioss"

Supplier: Bioss

GOT1L1, Glutamate oxaloacetate transaminase 1-like protein 1, is a 421 amino acid member of the class-I pyridoxal-phosphate-dependent aminotransferase family. Similar to glutamate-oxaloacetate transaminase (GOT1), GOT1L1 is found primarily as a homodimer in the cytoplasmic space but also has mitochondrial and chloroplastic isozymes. GOT1L1 transaminates 2-oxoglutarate with L-aspartate to yield oxaloacetate and L-glutamate. This reaction requires a pyridoxal phosphate cofactor to occur. The GOT1L1 peptidase is predominately expressed in the liver and serum levels of this protein can be used as an indicator of liver disease. Also, elevated glutamate concentrations in the brain interstitial fluids can lead to pathological brain conditions. The glutamate-scavenging properties of these aminotranferase type enzymes likely prevent glutamate excitotoxicity and the long-lasting neurological deficits seen after stroke.

Supplier: Bioss

IL-1R9 is a member of the interleukin-1/Toll-like receptor family expressed in fetal brain. It is a single pass transmembrane protein with a highly conserved cytoplasmic region that is slightly longer than that of other family members. IL-1R9 is highly homologous to IL-1R8 and the IL-1 accessory protein receptor chains. The genes encoding IL-1R9 and IL-1R8 are both found on the X-chromosome in the region associated with X-linked non-syndromic mental retardation. Unlike other family members, IL-1R9 and IL-1R8 do not activate NF-kB.

Supplier: Bioss

Component of the vault ribonucleoprotein particle which is at least composed of MVP, PARP4 and one or more vault RNAs (vRNAs). Binds to MVP. Associates with TEP1. Widely expressed; the highest levels are in the kidney; also detected in heart, placenta, lung, liver, skeletal muscle, spleen, leukocytes and pancreas.

Supplier: Bioss

Spindly/CCDC99

Supplier: Bioss

C19orf46 is a 404 amino acid single-pass type IV membrane protein that belongs to the nesprin family. C19orf46 partcipates in the establishment of secretory epithelial morphology by inducing kinesin-dependent apical migration of the centrosome and Golgi apparatus as well as basal localization of the nucleus. C19orf46 interacts with UKHC and KCL1, and exists as two alternatively spliced isoforms. C19orf46 contains a KASH domain, which consists of a transmembrane motif, mediates nuclear enevelop targeting and binds to the SUN domain of SUN1 and SUN2. C19orf46 is encoded by a gene located on human chromosome 19, which consists of approximately 63 million bases and makes up over 2% of human genomic DNA.

Supplier: Bioss

Catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. Catalyzes the reduction of mevaldate to mevalonic acid and of glyceraldehyde to glycerol. Has broad substrate specificity. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid. Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs, including the anthracyclines doxorubicin (DOX) and daunorubicin (DAUN).

Supplier: Bioss

PJA2, also known as E3 ubiquitin-protein ligase praja-2, RNF131 (ring finger protein 131) or Neurodap1, is a 708 amino acid protein that contains one ring-type zinc finger and exists as two alternatively spliced isoforms. Significantly conserved in chimpanzee, dog, cow, mouse, rat, chicken and zebrafish, PJA2 shares 52% identity with PJA1, which is involved in protein ubiquitination in brain and may play a role in X-linked mental retardation. Encoded by a gene that maps to human chromosome 5q21.3, PJA2 localises to both endoplasmic reticulum and Golgi apparatus membranes. Participating in E2-dependent, E3 ubiquitin-protein ligase activity, PJA2 binds to a variety of E2s and interacts with ubiquitin-conjugating enzymes, such as UBE2D2, in vitro.

Supplier: Bioss

Constitutive NADPH oxidase which generates superoxide intracellularly upon formation of a complex with CYBA/p22phox. Regulates signaling cascades probably through phosphatases inhibition. May function as an oxygen sensor regulating the KCNK3/TASK-1 potassium channel and HIF1A activity. May regulate insulin signaling cascade. May play a role in apoptosis, bone resorption and lipolysaccharide-mediated activation of NFKB.

Supplier: Bioss

PSD 93 is believed to participate in the clustering of certain proteins, including N-methyl-D-aspartate (NMDA) receptors and shaker-type potassium channels at the synaptic membrane. There are two principal modes of interaction between PSD 93 and other proteins. NMDA receptors and shaker-type potassium channels both share C-terminal sequence homology consisting of a threonine/serine-X-valine-COOH (T/SXV) motif. Other neuronal proteins that share this motif (beta 1 adrenergic receptor, some serotonin receptors, some sodium channel subunits, and additional potassium channel subunits) may interact with PSD 93 by binding to its PDZ domains. Neuronal nitric oxide synthase (nNOS), which lacks the T/SXV motif but which has its own PDZ domain, has been shown to associate with PSD 93 in vitro through a pseudo-homotypic PDZ-PDZ interaction.

Supplier: Bioss

Catalytic component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. V(D)J recombination assembles a diverse repertoire of immunoglobulin and T-cell receptor genes in developing B and T lymphocytes through rearrangement of different V (variable), in some cases D (diversity), and J (joining) gene segments. In the RAG complex, RAG1 mediates the DNA-binding to the conserved recombination signal sequences (RSS) and catalyzes the DNA cleavage activities by introducing a double-strand break between the RSS and the adjacent coding segment. RAG2 is not a catalytic component but is required for all known catalytic activities. DNA cleavage occurs in 2 steps: a first nick is introduced in the top strand immediately upstream of the heptamer, generating a 3'-hydroxyl group that can attack the phosphodiester bond on the opposite strand in a direct transesterification reaction, thereby creating 4 DNA ends: 2 hairpin coding ends and 2 blunt, 5'-phosphorylated ends. The chromatin structure plays an essential role in the V(D)J recombination reactions and the presence of histone H3 trimethylated at 'Lys-4' (H3K4me3) stimulates both the nicking and haipinning steps. The RAG complex also plays a role in pre-B cell allelic exclusion, a process leading to expression of a single immunoglobulin heavy chain allele to enforce clonality and monospecific recognition by the B-cell antigen receptor (BCR) expressed on individual B lymphocytes. The introduction of DNA breaks by the RAG complex on one immunoglobulin allele induces ATM-dependent repositioning of the other allele to pericentromeric heterochromatin, preventing accessibility to the RAG complex and recombination of the second allele. In addition to its endonuclease activity, RAG1 also acts as a E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H3. Histone H3 monoubiquitination is required for the joining step of V(D)J recombination.

Supplier: Bioss

Essential for the control of the cell cycle at the G1/S (start) and the G2/M (mitosis) transitions.

Supplier: Bioss

In mammalian cells, transcription is regulated in part by high molecular weight coactivating complexes that mediate signaling between transcriptional activators and initiation factors. These complexes include the thyroid hormone receptor-associated protein (TRAP) complex, which interacts with thyroid receptors (TR), vitamin D receptors and other steroid receptors to facilitate hormone induced transcriptional activation. The TRAP complex consists of numerous proteins ranging in size including TRAP95, TRAP100, TRAP150, TRAP220 and TRAP230, that are characterized by the presence of a nuclear receptor recognition motif which mediates the ligand-dependent binding of TRAP proteins to the nuclear receptors. TRAP220 and TRAP100 are widely expressed and most abundantly detected in skeletal muscle, heart and placenta. TRAP95, TRAP150 and TRAP230 facilitate TR induced transcription by associating with an additional transcriptional coactivating complex SMCC (SRB and MED protein cofactor complex), which consists of various subunits that share homology with several components of the yeast transcriptional mediator complexes.

Supplier: Bioss

Anti-IL6 Rabbit Polyclonal Antibody

Supplier: Bioss

Anti-C3IP1 Rabbit Polyclonal Antibody

Supplier: Bioss

As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Plays also a role in base excision repair (BER) probably through interaction with UNG. Through RFWD3 may activate CHEK1 and play a role in replication checkpoint control. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance.

Supplier: Bioss

CREB3L3 is a 461 amino acid single-pass type II membrane protein that localizes to the endoplasmic reticulum (ER) and, in response to ER stress, is cleaved and translocated to the nucleus. Expressed exclusively in liver, CREB3L3 functions as a transcription factor that, during ER stress, is thought to activate genes that are involved in both the unfolded protein response and the acute phase response (APR). Additionally, CREB3L3 is underexpressed in hepatocellular carcinoma, suggesting a possible role as a tumor suppressor. CREB3L3 functions as a dimer and contains one leucine zipper domain, a KDEL-like sequence and a bZIP domain, through which it conveys its DNA binding ability. Three isoforms of CREB3L3 exist due to alternative splicing events.