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Catalog Number: (89361-312)
Supplier: Genetex
Description: Transcription factor that specifically recognizes and binds E-box sequences (3'-CANNTG-5'). Efficient DNA-binding requires dimerization with itself or with another MiT/TFE family member such as TFE3 or MITF. In association with TFE3, activates the expression of CD40L in T-cells, thereby playing a role in T-cell-dependent antibody responses in activated CD4(+) T-cells and thymus-dependent humoral immunity. Specifically recognizes and binds the CLEAR-box sequence (5'-GTCACGTGAC-3') present in the regulatory region of many lysosomal genes, leading to activate their expression. It thereby plays a central role in expression of lysosomal genes. Specifically recognizes the gamma-E3 box, a subset of E-boxes, present in the heavy-chain immunoglobulin enhancer. Plays a role in the signal transduction processes required for normal vascularization of the placenta.


Catalog Number: (10782-510)
Supplier: Biosensis
Description: TrkC is a member of the neurotrophic tyrosine receptor kinase family. TrkC is a membrane-bound receptor that upon neurotrophin binding, phosphorylates itself and members of the MAPK pathway. TrkC is the receptor for neurotrophin-3 (NT-3).  Signalling through TrkC leads to cell differentiation and may play a role in the development of proprioceptive neurons that sense body position. SUBUNIT: Exists in a dynamic equilibrium between monomeric (low affinity) and dimeric (high affinity) structures. SUBCELLULAR LOCATION: Membrane; single-pass type I membrane protein. ALTERNATIVE PRODUCTS: 4 named isoforms produced by alternative splicing. Additional isoforms seem to exist. Mutations in TrkC have been associated with medulloblastomas, secretory breast carcinomas and other cancers.


Catalog Number: (10394-472)
Supplier: Bioss
Description: cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase, which transduces the signal through phosphorylation of different target proteins. The inactive kinase holoenzyme is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Four different regulatory subunits and three catalytic subunits have been identified in humans. The protein encoded by this gene is a member of the Ser/Thr protein kinase family and is a catalytic subunit of cAMP-dependent protein kinase. Several alternatively spliced transcript variants encoding distinct isoforms have been observed.


Catalog Number: (CA101410-450)
Supplier: Enzo Life Sciences
Description: Mitogenic platelet derived growth factor (PDGF) signaling is mediated by the PDGF tyrosine kinase receptors PDGFRα and PDGFRβ, which exist as homo- or heterodimer isoforms (αα, ββ, αβ). Secretion of PDGFs and expression of PDGFRs in a broad distribution of cell types contributes to regulation of cellular processes including cell growth, actin reorganization, prevention of apoptosis, and chemotaxis. Structurally, the transmembrane PDGFRs are composed of an N-terminal extracellular domain with five immunoglobulin repeats, and an intracellular domain containing two spaced tyrosine kinase domains. PDGF ligands display preferential affinity to PDGFRα and PDGFRβ, with PDGFRβ activation restricted to binding by PDGF BB and PDGF DD. Growth factor binding initiates receptor dimerization and activates the cytosolic tyrosine kinase domains.


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: (10668-278)
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.


Catalog Number: (75794-206)
Supplier: Prosci
Description: CD27 (TNFRSF7) is a member of the TNF-receptor superfamily limited to cells of the lymphoid lineage and exists as both a dimeric glycoprotein on the cell surface and as a soluble protein in serum. As a T and B cell co-stimulatory molecule, the activity of CD27 is governed by its TNF-like ligand CD70 on lymphocytes and dendritic cells. The CD27-CD70 interaction is required for Th1 generation responses to differentiation signals and long-term maintenance of T cell immunity, and meanwhile, plays a key role in regulating B cell differentiation, activation and immunoglobulin synthesis. The CD27 receptor transduces signals and subsequently leads to the activation of NF-kappaB and MAPK8/JNK, mediated by the adaptor proteins TRAF2 and TRAF5. In addition, the proapoptotic protein SIVA is capable of binding the cytoplasmic tail of CD27 and exerts action in the process of apoptosis.


Catalog Number: (10672-038)
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: (10093-796)
Supplier: Proteintech
Description: RNF17 also termed as ring finger protein 17 is a 1623 amino acid protein, which contains 1 ring type zinc finger and 4 tudor domains. RNF17 is specifically expressed in testis. The RING finger motif presents in many ubiquitin E3 ligases. RNF17 interacts with all four members of the Mad family (Mad1, Mxi1, Mad3 and Mad4), which are basic-helix-loop-helix-leucine zipper transcription factors of the Myc oncoprotein network. RNF17 is component of the tectonic-like complex, which is required for ciliogenesis and sonic hedgehog/SHH signaling. RNF17 is able to form dimers or polymers both in vitro and in vivo, indicating that it may play a role in the assembly of RNF17 granules. RNF17 encodes a novel key regulator of spermiogenesis.


Catalog Number: (10668-284)
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: (10668-282)
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: (10463-348)
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.


Catalog Number: (10463-350)
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.


Supplier: Tonbo Biosciences
Description: The ACK2 antibody is specific for CD117, also called c-Kit, a 145 kDa cytokine receptor important in the development of hematopoietic stem cells, in oogenesis, and for functional activity of immune cells such as NK and mast cells. c-Kit binds to a ligand known as stem cell factor (SCF), or alternatively as mast cell growth factor. Ligand binding promotes the activation (dimerization) and subsequent tyrosine kinase activity of the c-Kit receptor and triggers key survival, expansion and maturation signals during hematopoietic progenitor cell development. Conversely, shedding of extracellular domain of c-Kit receptor is reported to induce inactivation or apoptosis within these cells. The survival signaling activity of c-Kit confers a proto-oncogenic attribute to the receptor, as overexpression or mutations in this protein are associated with tumor development.

Catalog Number: (10463-358)
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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