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Human T-cell leukemia virus enhancer factor (HTLF) may be a forkhead domain binding protein. It may function in the transcriptional regulation of the human T-cell leukemia virus long terminal repeat.Human T-cell leukemia virus enhancer factor (HTLF) may be a forkhead domain binding protein. It may function in the transcriptional regulation of the human T-cell leukemia virus long terminal repeat.

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The nerve growth factor-induced clone C (NGFI-C/EGR4) gene is a zinc-finger transcription factor that is rapidly induced by nerve growth factor in rat pheochromocytoma PC12 cells and by seizure in brain. NGFI-C/EGR4 is closely related to the previously described early response genes, nerve growth factor-induced clone A (NGFI-A or EGR1), EGR2, and EGR3. These four early response (immediate early) proteins all contain very similar zinc-finger DNA binding domains and five highly homologous subdomains. EGR-4 functionally cooperate with NFAT proteins and induce expression of IL-2 and TNFalpha. Early growth response proteins (EGR) and nuclear factors of activated T cells (NFAT) form heterodimers and regulate proinflammatory cytokine gene expression.

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FOXO1A belongs to the forkhead family of transcription factors which are characterized by a distinct forkhead domain. The specific function of FOXO1A has not yet been determined; however, it may play a role in myogenic growth and differentiation. Translocation of FOXO1A gene with PAX3 has been associated with alveolar rhabdomyosarcoma.

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The c-Jun proto-oncogene was first identified as the cellular homolog of the avian sarcoma virus v-Jun oncogene. The c-Jun protein, along with c-Fos, is a component of the AP-1 transcriptional complex. c-Jun can form either Jun/Jun homodimers or Jun/Fos heterodimers via the leucine repeats in both proteins. Jun B and Jun D, have been shown to be almost identical to c-Jun 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 involved in many types of human carcinoma including T-cell lymphomas, CML,primary cutaneous lymphomas. Aberrantly expressed c-Jun and JunB are a hallmark of Hodgkin lymphoma cells, stimulate proliferation and synergize with NF-kappa B. JunB potentiates function of BRCA1 activation domain 1 (AD1) through a coiled-coil-mediated interaction.JunB is an important regulator of erythroid Differentiation.

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Anti-Hepatitis C Mouse Monoclonal Antibody

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CBX4 Antibody: Polycomb group (PcG) proteins are chromatin-associated proteins which are important for embryonic and adult stem cell self-renewal and maintenance. At least two distinct human PcG complexes have been identified. Polycomb repressive complex I (PRC1) contains CBX4/Pc2, HPH1 and RING domain-containing proteins (RING1, RING2 and BMI1). CBX4 (Chromobox protein homolog 4 or PC2), which functions as a transcriptional suppressor, is a candidate of KyoT2-binding proteins. It is a E3 SUMO-protein ligase which facilitates SUMO1 conjugation. Depletion of CBX4 results in decreased cellular resistance to ionizing radiation. CBX4 is directly involved in the cellular response to DNA damage.

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Kin is a nuclear protein that forms intranuclear foci during proliferation and is redistributed in the nucleoplasm during the cell cycle. Short-wave ultraviolet light provokes the relocalization of the protein, suggesting its participation in the cellular response to DNA damage. Originally selected based on protein-binding with RecA antibodies, the mouse protein presents a limited similarity with a functional domain of the bacterial RecA protein, a characteristic shared by the human ortholog.

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18 amino acids near the center of human TRIM33.

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19 amino acid peptide near the amino terminus of human RNF20.

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16 amino acid peptide near the amino terminus of human TLX1.

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The exact function of C20orf195 remains unknown.

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FUNCTION: Binds as a monomer with high affinity to interleukin 13 (IL13), but not to IL4.
SIMILARITY: Contains 1 fibronectin type-III domain.
SUBCELLULAR LOCATION: Membrane; single-pass type I membrane protein.
DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.
DOMAIN: The box 1 motif is required for JAK interaction and/or activation.

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Smad3 encoded by this gene belongs to the SMAD, a family of proteins similar to the gene products of the Drosophila gene 'mothers against decapentaplegic' (Mad) and the C. elegans gene Sma. SMAD proteins are signal transducers and transcriptional modulators that mediate multiple signaling pathways. This protein functions as a transcriptional modulator activated by transforming growth factor-beta and is thought to play a role in the regulation of carcinogenesis.

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Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, copper homeostasis, mitogenic kinase signaling, cell proliferation, as well as cell invasion and metastasis. Acts as a direct caspase inhibitor. Directly bind to the active site pocket of CASP3 and CASP7 and obstructs substrate entry. Inactivates CASP9 by keeping it in a monomeric, inactive state.

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Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter. Probably has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such SRR.

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Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to hepatocyte growth factor/HGF ligand. Regulates many physiological processes including proliferation, scattering, morphogenesis and survival. Ligand binding at the cell surface induces autophosphorylation of MET on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1, SRC, GRB2, STAT3 or the adapter GAB1.

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The specific function of this protein remains unknown.

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Anti-DDA1 Goat Polyclonal Antibody

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Calcium-dependent membrane-binding proteins may regulate molecular events at the interface of the cell membrane and cytoplasm. CPNE1 is a calcium-dependent protein that also contains two N-terminal type II C2 domains and an integrin A domain-like sequence in the C-terminus. However, the protein does not contain a predicted signal sequence or transmembrane domains. This protein has a broad tissue distribution and it may function in membrane trafficking.Calcium-dependent membrane-binding proteins may regulate molecular events at the interface of the cell membrane and cytoplasm. This gene encodes a calcium-dependent protein that also contains two N-terminal type II C2 domains and an integrin A domain-like sequence in the C-terminus. However, the encoded protein does not contain a predicted signal sequence or transmembrane domains. This protein has a broad tissue distribution and it may function in membrane trafficking. This gene and the gene for RNA binding motif protein 12 overlap at map location 20q11.21. Sequence analysis identified multiple alternatively spliced variants in the 5' UTR. All variants encode the same protein.

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The specific function of this protein remains unknown.

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Anti-POU4F3 Goat Polyclonal Antibody

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Anti-POU2F3 Goat Polyclonal Antibody

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SFRS10 contains 1 RRM (RNA recognition motif) domain and belongs to the splicing factor SR family. It is a sequence-specific RNA-binding protein which participates in the control of pre-mRNA splicing.

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EIF4E2 belongs to the eukaryotic initiation factor 4E family. It recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures.

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Anti-HOXA9 Goat Polyclonal Antibody

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Anti-HPGD Goat Polyclonal Antibody

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Sonic Hedgehog Homolog (SHH) belongs to a three-protein family called Hedgehog. The other two family members are Indian Hedgehog (IHH) and Desert Hedgehog (DHH). Hedgehog proteins are key signaling molecules in embryonic development. SHH is expressed in various embryonic tissues and plays critical roles in regulating the patterning of many systems, such as limbs and brain. SHH also plays an important role in adult, including the division of adult stem cells and the development of certain cancers and other diseases. Human SHH is expressed as a 45kDa precursor, and undergoes a series of processing during secretion. After the removal of the signal peptide, a protease within the C-terminal domain catalyzes the cleavage of SHH into a 20 kDa N-terminal signaling domain (SHH-N) and a 25 kDa C-terminal domain (SHH-C). SHH-N has the “all signaling” capability. SHH-N binds to the 12 pass transmembrane protein Patched (Ptc) on cell surface, which releases the repression of the activity of Smoothened (Smo), a G-protein coupled receptor, by Ptc.

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The function remains unknown.

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SLC9A9 may act in electroneutral exchange of protons for Na (+) across membranes.

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C1D is a DNA binding and apoptosis-inducing protein and is localized in the nucleus. It is also a Rac3-interacting protein which acts as a corepressor for the thyroid hormone receptor. C1D is thought to regulate TRAX/Translin complex formation. The protein encoded by this gene is a DNA binding and apoptosis-inducing protein and is localized in the nucleus. It is also a Rac3-interacting protein which acts as a corepressor for the thyroid hormone receptor. This protein is thought to regulate TRAX/Translin complex formation. Several alternatively spliced transcript variants of this gene have been described, but the full length nature of some of these variants has not been determined.The protein encoded by this gene is a DNA binding and apoptosis-inducing protein and is localized in the nucleus. It is also a Rac3-interacting protein which acts as a corepressor for the thyroid hormone receptor. This protein is thought to regulate TRAX/Translin complex formation. Several alternatively spliced transcript variants of this gene have been described, but the full length nature of some of these variants has not been determined.