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The NFKB complex consists of NFKB1 or NFKB2 bound to REL, RELA, or RELB. The NFKB complex is inhibited by I kappa B proteins (NFKBIA, or NFKBIB), which inactivate NF kappa B by trapping it in the cytoplasm. Phosphorylation of serine residues on the I kappa B proteins by kinases (IKBKA, or IKBKB,) marks them for destruction via the ubiquitination pathway, thereby allowing activation of the NF kappa B complex.

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DOCK 4 is a cytoplasmic peripheral membrane protein that belongs to the DOCK family of cytokinesis-regulating proteins. Expressed ubiquitously with highest expression in prostate, ovary and skeletal muscle, DOCK 4 functions as a guanine nucleotide exchange factor (GEF) that activates the small GTPase Rap 1 and, via this activation, plays a role in the regulation of adherens junctions between cells. Similar to other DOCK family members, DOCK 4 contains an N-terminal SH3 domain, a C-terminal proline-rich region and two internal DOCK homology regions designated DHR1 and DHR2. Defects in the gene encoding DOCK 4 result in the inactivation of Rap 1 and are, thus, implicated in the pathogenesis of various cancers such as ovarian, prostate, glioma and colorectal carcinomas. Four isoforms of DOCK 4 are expressed due to alternative splicing events.

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Integrin alpha-5/beta-1 is a receptor for fibronectin and fibrinogen. It recognizes the sequence R-G-D in its ligands. In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions.

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May induce necrosis and apoptosis. May play a role in cell viability.

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Semaphorins are a family of cell surface and secreted proteins that are conserved from insects to humans. Members of this family of proteins are approximately 750 amino acids in length (including signal sequences) and are defined by a conserved extracellular “semaphorin” domain of approximately 500 amino acids containing 14-16 cysteines, blocks of conserved sequences and no obvious repeats. The transmembrane semaphorins are characterized by an additional 80 amino acid transmembrane domain and an 80-110 amino acid cytoplasmic domain. Secreted and cell-bound semaphorins chemically attract and repel the growth of neural axons, guiding the development of intricate networks of neural tissue. SEMA4B (semaphorin-4B), also known as SemC or SEMAC, is an 832 amino acid single-pass type I membrane protein that belongs to the semaphorin family and exists as two alternatively spliced isoforms. Containing one Ig-like C2-type (immunoglobulin-like) domain, a PSI domain and a single sema domain, SEMA4B is encoded by a gene located on human chromosome 15.

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Centrosomes are dynamic organelles involved in many aspects of cell function and growth. Centrosomes act as microtubule organizing centers, and provide a site for concerted regulation of cell cycle progression. Duplication of centrosomes occurs once during each cell cycle and requires proper mitotic spindle formation and chromosome segregation. Defects in centrosome duplication or function are linked to many human diseases, including various forms of cancer. The centrosome and spindle pole-associated protein 1 (CSPP1) interacts with centrosomes and microtubules and may play a role in the regulation of G(1)/S-phase progression and spindle assembly. Two isoforms of CSPP1 exist as a result of alternative splicing events. Isoform 1 expression increases throughout the cell cycle and peaks in G2/M phase, whereas isoform 2 expression is highest in G1 phase and decreases thereafter.

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DDAH, a dimethylarginine dimethylaminohydrolase, hydrolyzes dimethyl arginine (ADMA) and monomethyl arginine (MMA), both inhibitors of nitric oxide synthases, and may be involved in in-vivo modulation of nitric oxide production (1,2). Impairment of DDAH causes ADMA accumulation and a reduction in cGMP generation (3). DDAH II, the predominant DDAH isoform in endothelial cells, facilitates the induction of nitric oxide synthesis by all-trans-Retinoic acid (atRA) (4). DDAH proteins are highly expressed in colon, kidney, stomach and liver tissues (1).

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The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. RNF141 (ring finger protein 141), also known as ZFP26 or ZNF230, is a 230 amino acid protein that contains one RING-type zinc finger. Expressed as two isoforms (isoform 1 and isoform 2) due to alternative splicing events, RNF141 is thought to function as a transcription factor during spermatogenesis. While isoform 2 is expressed in brain, heart, pancreas, kidney and skeletal muscle, isoform 1 is expressed primarily in testis, suggesting that isoform 1 functions during spermatogenesis. In addition, RNF141 is not expressed in azoospermic (infertile) men, further implicating an important role for RNF141 in testis development and male fertility.

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The protein encoded by this gene is a dual specificity protein kinase that belongs to the MAP kinase kinase family. This kinase specifically activates MAPK8/JNK1 and MAPK9/JNK2, and this kinase itself is phosphorylated and activated by MAP kinase kinase kinases including MAP3K1/MEKK1, MAP3K2/MEKK2,MAP3K3/MEKK5, and MAP4K2/GCK. This kinase is involved in the signal transduction mediating the cell responses to proinflammatory cytokines, and environmental stresses. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found, but only one transcript variant has been supported and defined. [provided by RefSeq].Hsp27, also referred to as the Estrogen regulated 24K protein and HSP28, is one of several small heat shock proteins (HSP) produced by all organisms studied. Hsp27 synthesis is induced by elevated temperature, as well as estrogen in hormone responsive cells. This protein is involved in stress resistance and actin organization. Interestingly, human HSP27 also shares greater than 50% homology with low molecular weight Drosophila HSP's and mammalian a-crystalline lens protein. Because of the estrogen responsive nature of Hsp27, this protein has been studied extensively in human estrogen responsive tissues such as cervix, endometrium and breast tissue. This work has led to the suggestion that Hsp27 may be a useful marker in classifying various hormone sensitive tumors.

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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. As a member of the krueppel C2H2-type zinc-finger protein family, ZNF449 is a 518 amino acid protein that contains one SCAN box domain and seven C2H2-type zinc fingers. ZNF449 is ubiquitously expressed and localizes to the nucleus. There are three isoforms of ZNF449 that are produced as a result of alternative splicing events.

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Phosphatidic acid and lysophosphatidic acid are phospholipids involved in lipid biosynthesis and signal transduction. LPAAT-epsilon (lysophosphatidic acid acyltransferase epsilon, also designated 1-AGP acyltransferase 5 (AGPAT5)) catalyzes the synthesis of phosphatidic acid from lysophosphatidic acid. LPAAT-epsilon is a membrane-bound protein belonging to the LPAAT family. Members of the LPAAT family have a well-known role in lipid biosynthesis and they may also play a role in tumor progression. LPAAT-epsilon is expressed in a tissue-specific manner in prostate and testis. LPAAT-epsilon is most closely related to AGPAT8, which is highly expressed in heart.

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Major histocompatibility complex (MHC) molecules form an integral part of the immune response system. They are cell-surface receptors that bind peptides and present them to T lymphocytes. Human leukocyte antigens (HLAs) are polymorphic members of the MHC family that are specifically involved in the presentation of antigens to the T cell receptor. There are two classes of HLA antigens: class I (HLA-A, HLA-B and HLA-C) and class II (HLA-D). Class I molecules are expressed in nearly all cells and play a central role in the immune system by presenting peptides derived from the endoplasmic reticulum. The differential structural properties of MHC class I and class II molecules account for their respective roles in activating different populations of T lymphocytes. HLA-B encodes a membrane anchored heavy chain which hetero-dimerizes with a light chain (∫-2-Microglobulin) to form MHC-I. Polymorphisms yield hundreds of HLA-B alleles. The HLA-B27 allele appears with increased frequency in uveitis patients.

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The protein encoded by this gene is a member of the MAP kinase family. MAP kinases, also known as extracellular signal-regulated kinases (ERKs), act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation and development. The activation of this kinase requires its phosphorylation by upstream kinases. Upon activation, this kinase translocates to the nucleus of the stimulated cells, where it phosphorylates nuclear targets. Two alternatively spliced transcript variants encoding the same protein, but differing in the UTRs, have been reported for this gene.

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Anti-NLRX1 Rabbit Polyclonal Antibody

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postsynaptic density protein 95 is a molecular scaffolding protein that binds and clusters N-methyl-D-aspartate receptors at neuronal synapses; may be involved in guanine nucleotide-mediated signal transduction pathway. This gene encodes a member of the membrane-associated guanylate kinase (MAGUK) family. It heteromultimerizes with DLG2. With DLG2 it is recruited into the same NMDA receptor and potassium channel clusters. These two MAGUK proteins may interact at postsynaptic sites to form a multimeric scaffold for the clustering of receptors, ion channels, and associated signaling proteins.

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KCNK9 or TASK-3 (TWIK-related Acid sensitive K+ channel) is a member of the potassium channel family of proteins that contain two-pore domain and four transmembrane domains. These channels are characterized as leak K+ channels that are sensitive to changes in the extracellular pH. The physiological functions of TASK channels are largely unknown; it has been proposed that they may be involved in the regulation of breathing, aldosterone secretion and anesthetic-mediated neuronal activity. They were found to act in neurons' membrane potential and in resting K+ currents.