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Supplier:  Bioss
Description:   The androgen receptor gene is more than 90 kb long and codes for a protein that has 3 major functional domains: the N-terminal domain, DNA-binding domain, and androgen-binding domain. The protein functions as a steroid-hormone activated transcription factor. Upon binding the hormone ligand, the receptor dissociates from accessory proteins, translocates into the nucleus, dimerizes, and then stimulates transcription of androgen responsive genes. This gene contains 2 polymorphic trinucleotide repeat segments that encode polyglutamine and polyglycine tracts in the N-terminal transactivation domain of its protein. Expansion of the polyglutamine tract causes spinal bulbar muscular atrophy (Kennedy disease). Mutations in this gene are also associated with complete androgen insensitivity (CAIS). Two alternatively spliced variants encoding distinct isoforms have been described. [provided by RefSeq, Jul 2008]
Supplier:  Bioss
Description:   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. Zinc finger and BTB domain-containing protein 43 (ZBTB43), also known as ZNF297B or ZBTB22B, is a 467 amino acid member of the Krüppel C2H2-type zinc-finger protein family. Localized to the nucleus, ZBTB43 contains a BTB domain, also known as a POZ domain, which inhibits DNA binding and mediates homotypic and heterotypic dimerization. Characteristics of the BTB domain and the interaction of ZBTB43 with BDP1 suggest that ZBTB43 functions as a transcription regulator.
Catalog Number: (10303-070)

Supplier:  Bioss
Description:   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. Zinc finger and BTB domain-containing protein 43 (ZBTB43), also known as ZNF297B or ZBTB22B, is a 467 amino acid member of the Krüppel C2H2-type zinc-finger protein family. Localized to the nucleus, ZBTB43 contains a BTB domain, also known as a POZ domain, which inhibits DNA binding and mediates homotypic and heterotypic dimerization. Characteristics of the BTB domain and the interaction of ZBTB43 with BDP1 suggest that ZBTB43 functions as a transcription regulator.
Catalog Number: (102552-836)

Supplier:  BioVendor
Description:   Trefoil factor 3 (TFF3, also known as intestinal trefoil factor) belongs together with TFF1 and TFF2 to a small group of mucin-associated peptides. TFF3 contains seven cysteine residues, six of which form disulfide bonds to create a characteristic three-leafed structure. Due to its compact structure, TFF3 is extremely resistant toward acids, proteolytical cleavage or heat degradation. Monomeric form of TFF3 consists of 60 amino acids and has 6.7 kDa, while the dimer (13.1 kDa) consists of 118 amino acids. TFF3 is expressed mainly in gastrointestinal tract, in the mucous cells of the small and large intestine, where it maintains the integrity of mucous layer and in cooperation with mucins protects the gastrointestinal epithelial cells against various injurious agents. However, TFF3 was also detected in salivary glands, posterior pituitary gland and in the inner ear. Secretion of TFF3 is triggered by the presence of certain inflammation mediators and neurotransmitters.
Catalog Number: (75932-930)

Supplier:  Rockland Immunochemical
Description:   Toll-like receptors (TLRs) are evolutionarily conserved pattern-recognition molecules resembling the toll proteins that mediate antimicrobial responses in Drosophila. These proteins recognize different microbial products during infection and serve as an important link between the innate and adaptive immune responses. The TLRs act through adaptor molecules such as MyD88 and TIRAP to activate various kinases and transcription factors so the organism can respond to potential infection. TLR6 was first identified as a close homolog of TLR1, sharing 69% sequence identify. Like TLR1, TLR6 can form heterodimers with TLR2, and these TLR6:TLR2 dimers coordinate macrophage activation by Gram-positive bacteria and the yeast cell wall particle zymosan. Activation of these complexes not only initiates pro-inflammatory cascades, but also can lead to apoptotic responses.
Catalog Number: (75932-928)

Supplier:  Rockland Immunochemical
Description:   Toll-like receptors (TLRs) are evolutionarily conserved pattern-recognition molecules resembling the toll proteins that mediate antimicrobial responses in Drosophila. These proteins recognize different microbial products during infection and serve as an important link between the innate and adaptive immune responses. The TLRs act through adaptor molecules such as MyD88 and TIRAP to activate various kinases and transcription factors so the organism can respond to potential infection. TLR6 was first identified as a close homolog of TLR1, sharing 69% sequence identify. Like TLR1, TLR6 can form heterodimers with TLR2, and these TLR6:TLR2 dimers coordinate macrophage activation by Gram-positive bacteria and the yeast cell wall particle zymosan. Activation of these complexes not only initiates pro-inflammatory cascades, but also can lead to apoptotic responses.
Supplier:  Bioss
Description:   Key transcriptional regulator of type I interferon (IFN)-dependent immune responses which plays a critical role in the innate immune response against DNA and RNA viruses. Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters. Acts as a more potent activator of the IFN-beta (IFNB) gene than the IFN-alpha (IFNA) gene and plays a critical role in both the early and late phases of the IFNA/B gene induction. Found in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, is phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization and association with CREB binding protein (CREBBP) to form dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of the type I IFN and ISG genes. Can activate distinct gene expression programs in macrophages and can induce significant apoptosis in primary macrophages.
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. This gene encodes one of the regulatory subunits. This protein was found to be a tissue-specific extinguisher that down-regulates the expression of seven liver genes in hepatoma x fibroblast hybrids. Mutations in this gene cause Carney complex (CNC). This gene can fuse to the RET protooncogene by gene rearrangement and form the thyroid tumor-specific chimeric oncogene known as PTC2. A nonconventional nuclear localization sequence (NLS) has been found for this protein which suggests a role in DNA replication via the protein serving as a nuclear transport protein for the second subunit of the Replication Factor C (RFC40). Three alternatively spliced transcript variants encoding the same protein have been observed. [provided by RefSeq, Jul 2008].

Supplier:  Prosci
Description:   Estrogen receptor (ER) is an important regulator of growth and differentiation in the mammary gland. It is found in two forms, alpha and beta. Both forms are widely expressed, however, alpha is the predominant form in endometrium and breast cancer cells, and beta is more highly expressed in brain, kidney, heart, lung and bone. Activated Estrogen receptor dimerizes and forms both homo- and heterodimers. ER contains five domains: A-F. The A and B domain are able to weakly activate ER in the absence of ligand. The C domain binds DNA and the E domain contains the ligand binding site. Presence of ER in breast tumors indicates an increased likelihood of response to anti-estrogen (e.g. tamoxifen) therapy. This antibody is specific to estrogen receptor alpha and shows minimal cross-reaction with other members of the family.

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.

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.
Supplier:  Bioss
Description:   Crystallins are the major proteins of the vertebrate eye lens, where they maintain the transparency and refractive index of the lens. Crystallins are divided into a, b, and g families, and the b- and g-crystallins also comprise a superfamily. Crystallins usually contain seven distinctive protein regions, including four homologous motifs, a connecting peptide, and N- and C-terminal extensions. b-crystallins constitute the major lens structural proteins. They associate into dimers, tetramers, and higher order aggregates. The b-crystallin subfamily is composed of several gene products, including bA1-, bA2-, bA3-, bA4-, bB1-, bB2- and bB3-crystallin. The bA1- and bA3-crystallin proteins are encoded by a single mRNA. They differ by only 17 amino acids, and bA1-crystallin is generated by use of an alternate translation initiation site. The genes for bA4-, bB1-, bB2- and bB3-crystallin are clustered on human chromosome 22q11, while the genes for bA3/A1- and bA2-crystallin map to human chromosomes 17q11 and 2q34, respectively.

Supplier:  Bioss
Description:   Wnt-induced secreted protein (WISP)-1, WISP-2 and WISP-3 are members of the CCN family of growth factors, which include connective tissue growth factor (CTGF) and Cyr61. WISP-1, WISP-2 and WISP-3 share significant sequence similarity, including four conserved cysteine-rich domains, and they are believed to function as dimers in their active forms. WISP-1 expression is observed in various tissues including adult heart, kidney and spleen, while WISP-2 expression predominates in skeletal muscle, colon and ovary. Both WISP-1 and WISP-2 are upregulated in cells transformed with the proto-oncogene Wnt-1, and they are also more highly expressed in human colon tumors, suggesting that these proteins may participate in tumor development. WISP-3 is involved in normal post-natal skeletal growth, and it is also implicated in the development of the autosomal recessive skeletal disorder progressive pseudorheumatoid dysplasia, which affects cartilage homeostasis by disrupting the growth of chondrocyte and normal cell columnar organization.
Supplier:  Bioss
Description:   Wnt-induced secreted protein (WISP)-1, WISP-2 and WISP-3 are members of the CCN family of growth factors, which include connective tissue growth factor (CTGF) and Cyr61. WISP-1, WISP-2 and WISP-3 share significant sequence similarity, including four conserved cysteine-rich domains, and they are believed to function as dimers in their active forms. WISP-1 expression is observed in various tissues including adult heart, kidney and spleen, while WISP-2 expression predominates in skeletal muscle, colon and ovary. Both WISP-1 and WISP-2 are upregulated in cells transformed with the proto-oncogene Wnt-1, and they are also more highly expressed in human colon tumors, suggesting that these proteins may participate in tumor development. WISP-3 is involved in normal post-natal skeletal growth, and it is also implicated in the development of the autosomal recessive skeletal disorder progressive pseudorheumatoid dysplasia, which affects cartilage homeostasis by disrupting the growth of chondrocyte and normal cell columnar organization.
Catalog Number: (75931-578)

Supplier:  Rockland Immunochemical
Description:   Rheb (Ras homolog enriched in brain) is an evolutionarily conserved member of the Ras family of small GTP-binding proteins originally found to be rapidly induced by synaptic activity in the hippocampus following seizure. While it is expressed at relatively high levels in the brain, Rheb is widely expressed in other tissues and may be induced by growth factor stimulation. Similar to other family members, Rheb triggers activation of the Raf-MEK-MAPK pathway. Biochemical and genetic studies demonstrate that Rheb has an important role in regulating the insulin/Target of rapamycin (TOR) signaling pathway. TOR is a serine/threonine protein kinase that acts as a sensor for ATP and amino acids, balancing the availability of nutrients with protein translation and cell growth. A dimeric protein complex termed TSC1/TSC2 indirectly inhibits TOR activity by inhibiting Rheb via the GAP activity of TSC2.

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.
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