Purified Rabbit Polyclonal Antibody

BCL11B / CTIP2 Antibody

Purified anti-BCL11B / CTIP2 Antibody

Recombinant Rabbit Monoclonal Antibody

Zinc Finger Protein GLI1 is a member of the Kruppel family of zinc finger proteins. It is thought that it may regulate the transcription of specific genes during normal development and may play a role in craniofacial development and digital development. It also may be involved in the development of the central nervous system and gastrointestinal tract. This protein mediates SHH signaling and thus cell proliferation and differentiation. It has been localized to the cytoplasm and nucleus. It is tethered in the cytoplasm by binding to SUFU and activation and translocalization to the nucleus is promoted by interation with STK36. Protein expression is amplified in glioblastoma cells. Defects in the GLI1 protein may be a cause of breast cancer.

Zinc Finger Protein GLI1 is a member of the Kruppel family of zinc finger proteins. It is thought that it may regulate the transcription of specific genes during normal development and may play a role in craniofacial development and digital development. It also may be involved in the development of the central nervous system and gastrointestinal tract. This protein mediates SHH signaling and thus cell proliferation and differentiation. It has been localized to the cytoplasm and nucleus. It is tethered in the cytoplasm by binding to SUFU and activation and translocalization to the nucleus is promoted by interation with STK36. Protein expression is amplified in glioblastoma cells. Defects in the GLI1 protein may be a cause of breast cancer.

Zinc Finger Protein GLI1 is a member of the Kruppel family of zinc finger proteins. It is thought that it may regulate the transcription of specific genes during normal development and may play a role in craniofacial development and digital development. It also may be involved in the development of the central nervous system and gastrointestinal tract. This protein mediates SHH signaling and thus cell proliferation and differentiation. It has been localized to the cytoplasm and nucleus. It is tethered in the cytoplasm by binding to SUFU and activation and translocalization to the nucleus is promoted by interation with STK36. Protein expression is amplified in glioblastoma cells. Defects in the GLI1 protein may be a cause of breast cancer.

Vesicle-associated membrane protein 2 is essential for cAMP-regulated exocytosis. VAMP (also know as synaptobrevin) is part of the synaptic vesicle docking and fusion complex and plays a central role in neuroexocytosis. Two VAMP (vesicle-associated membrane protein) isoforms are expressed in the nervous system and are differently distributed among the specialized parts of the tissue. VAMP-1 and -2 are present in all tissues tested, including kidney, adrenal gland, liver, pancreas, thyroid, heart, and smooth muscle. The two isoforms are differentially expressed in various tissues and their level may depend on differentiation. VAMP-1 is restricted to exocrine pancreas and to kidney tubular cells, whereas VAMP-2 is the predominant isoform present in Langerhans islets and in glomerular cells. Both isoforms show a patchy vesicular intracellular distribution in confocal microscopy. Evidence for the importance of neuronal VAMPproteins in the physiology of all cells is indicated.

Recognizes a protein of 110kDa, identified as CD106 (also known as vascular cell adhesion molecule-1 (VCAM-1) and INCAM-110). CD106 is a member of the Ig superfamily of adhesion molecules and is expressed at high levels on cytokine stimulated vascular endothelial cells, and at minimal levels on unstimulated endothelial cells. It is also present on follicular and interfollicular dendritic cells of lymph nodes, myoblasts, and some macrophages. CD106 serves as a ligand for leukocyte integrin 4 1 (VLA-4 or CD49d/CD29) and mediates cell adhesion of leukocytes to activated endothelium. It plays a role in various immunological and inflammatory responses.

The immunogen used for the anti-human Vav-2 SHD region was a his tagged fusion protein Vav-2 corresponding to amino acid sequence 578 - 878 and having a molecular weight of 100kD. Vav-2 has a molecular weight of 100 kD and shares over a 50% homology at the amino acid and nucleic acid level with Vav. Vav-2 is a ubiquitously expressed structural homolog of the Vav protooncogene that is expressed preferentially in hematopoetic cells. Both proteins are comprised of a Dbl- homology ((DH) domain with guanosine nucleotide exchange (GEF) activity exclusively directed towards Rho/Rac GTPases, a pleckstrin homology (PH) domain, a calponin-homology (CH) region, an acidic domain (AD) a zinc finger butterfly motif, two SH3 regions and one SH2 domain. GEF activity of RhoA family G proteins is induced by tyrosine phosphorylation in wild type vav-2, and is constitutively activated in N terminus deleted oncogene forms. Constitutive expression of a Vav-2 oncoprotein may result in morphological alterations including highly enlarged cells in which karyokinesis and cytokinesis frequently are uncoupled.

The immunogen used for the anti-human Vav-2 DPH region was a his tagged fusion protein Vav-2 corresponding to amino acid sequence 287-578 and having a molecular weight of 100kD. Vav-2 has a molecular weight of 100 kD and shares over a 50% homology at the amino acid and nucleic acid level with Vav. Vav-2 is a ubiquitously expressed structural homolog of the Vav protooncogene that is expressed preferentially in hematopoetiic cells. Both proteins are comprised of a Dbl- homology ((DH) domain with guanosine nucleotide exchange (GEF) activity exclusively directed towards Rho/Rac GTPases, a pleckstrin homology (PH) domain, a calponin-homology (CH) region, an acidic domain (AD) a zinc finger butterfly motif, two SH3 regions and one SH2 domain. GEF activity of RhoA family G proteins is induced by tyrosine phosphorylation in wild type vav-2, and is constitutively activated in N terminus deleted oncogene forms. Constitutive expression of a Vav-2 oncoprotein may result in morphological alterations including highly enlarged cells in which karyokinesis and cytokenesis frequently are uncoupled.

Ubiquitin-conjugating enzyme E2 (UEV1) was initially discovered as a protein similar in sequence and structure to the E2 ubiquitin-conjugating enzymes but lacking their enzymatic activity (1). There are at least two variants and multiple isoforms of UEV1. In particular, UEV1A (Ubiquitin-conjugating enzyme E2 variant 1 isoform A) has recently been shown to be an important component of the Toll-like receptor and IL-1R signaling pathway (reviewed in 2). Signals from these pathways are relayed by a number of downstream molecules such as MyD88 and tumor necrosis factor receptor associated factor (TRAF6), ultimately activating various kinases and transcription factors (2,3). UEV1A is part of a dimeric ubiquitin-conjugating enzyme complex also containing Ubc13 (ubiquitin-conjugating enzyme 13) that together with TRAF6 activates TAK1, a member of the mitogen-activated protein kinase kinase kinase family (4-6). The Ubc13-UEV1A complex also mediates the Lys-63 ubiquitination of TRAF-6, and this ubiquitination is essential for TAK1 activation (5).

RYK (Receptor like Tyrosine kinase 1) is in the Tyrosine family of receptor kinases. It is found in the plasma membrane of heart, prostate and kidney cells. RYK contains 604 amino acids and it contains one WIF domain. It functions as a potential growth factor receptor protein tyrosine kinase. RYK are divergent from those of other classic receptor tyrosine kinases. It is an orphan receptor that contains a catalytically inactive tyrosine kinase related domain. RYK is expressed in nestin positive progenitor cells and neurons, and in a certain population of oligodendrocytes, O2A progenitor cells, and type 2 astrocytes in developing CNS.

Tyrosine Hydroxylase (TH) is the rate-limiting enzyme in the synthesis of the catecholamines Dopamine and Norepinephrine. TH antibodies can therefore be used as markers for dopaminergic and noradrenergic neurons in a variety of applications including depression, schizophrenia, ParkinsonÕs disease and drug abuse (Kish et al., 2001; Zhu et al., 2000; Zhu et al., 1999). TH antibodies can also be used to explore basic mechanisms of dopamine and norepinephrine signaling (Witkovsky et al., 2000; Salvatore et al., 2001; Dunkley et al., 2004). The activity of TH is also regulated by phosphorylation (Haycock et al., 1982; Haycock et al., 1992; Jedynak et al., 2002). Phospho-specific antibodies for the phosphorylation sites on TH can be used to great effect in studying this regulation and in identifying the cells in which TH phosphorylation occurs.

Tyrosine Hydroxylase (TH) is the rate-limiting enzyme in the synthesis of the catecholamines Dopamine and Norepinephrine. TH antibodies can therefore be used as markers for dopaminergic and noradrenergic neurons in a variety of applications including depression, schizophrenia, ParkinsonÕs disease and drug abuse (Kish et al., 2001; Zhu et al., 2000; Zhu et al., 1999). TH antibodies can also be used to explore basic mechanisms of dopamine and norepinephrine signaling (Witkovsky et al., 2000; Salvatore et al., 2001; Dunkley et al., 2004). The activity of TH is also regulated by phosphorylation (Haycock et al., 1982; Haycock et al., 1992; Jedynak et al., 2002). Phospho-specific antibodies for the phosphorylation sites on TH can be used to great effect in studying this regulation and in identifying the cells in which TH phosphorylation occurs.

Tryptophan hydroxylase (TPH) catalyzes the 5-hydroxylation of tryptophan, which is the first step in the biosynthesis of indoleamines (serotonin and melatonin). In mammals, serotonin biosynthesis occurs predominantly in neurons which originate in the raphe nuclei of the brain, and melatonin synthesis takes place within the pineal gland. Although TPH catalyzes the same reaction within the raphe nuclei and the pineal gland, TPH activity is rate-limiting for serotonin but not melatonin biosynthesis. Serotonin functions mainly as a neurotransmitter, whereas melatonin is the principal hormone secreted by the pineal gland. The activity of TPH is enhanced by phosphorylation by cAMP-dependent protein kinase (PKA) and Ca2+/calmodulin kinase II (CAM K II). Both PKA and CAM K II phosphorylate Ser58 which lies within the regulatory domain of TPH.

The expression of the cancer-testis antigen Taxol resistance-associated gene-3 (TRAG-3) is associated with acquired paclitaxel (Taxol) resistance, and is expressed in a variety of cancers - e.g., breast cancer, leukemia, and melanoma. Overexpressed in taxol-resistant breast cancer line MDA 435(TR) and the doxorubicin-resistant multiple myelanoma lines 8226/Dox(40) and 8226/MDR(10)V. Weakly expressed in kidney. TRAG-3 is an attractive target for immunotherapy of cancer._x000B__x000B_First identified as a novel cancer/testis antigen, TRAG-3, (Taxol Resistance Associated Gene-3) was initially discovered in a search for new genes involved in drug resistance. Early studies of TRAG-3 revealed a minimal to absent expression in normal tissues and a marked over-expression in many carcinoma cell lines including several melanoma lines. By RT-PCR evaluation of TRAG-3 two transcripts are seen in many carcinoma cell lines with products in the the 799 bp and a second alternatively spliced transcript.

The expression of the cancer-testis antigen Taxol resistance-associated gene-3 (TRAG-3) is associated with acquired paclitaxel (Taxol) resistance, and is expressed in a variety of cancers - e.g., breast cancer, leukemia, and melanoma. Overexpressed in taxol-resistant breast cancer line MDA 435(TR) and the doxorubicin-resistant multiple myelanoma lines 8226/Dox(40) and 8226/MDR(10)V. Weakly expressed in kidney. TRAG-3 is an attractive target for immunotherapy of cancer._x000B__x000B_First identified as a novel cancer/testis antigen, TRAG-3, (Taxol Resistance Associated Gene-3) was initially discovered in a search for new genes involved in drug resistance. Early studies of TRAG-3 revealed a minimal to absent expression in normal tissues and a marked over-expression in many carcinoma cell lines including several melanoma lines. By RT-PCR evaluation of TRAG-3 two transcripts are seen in many carcinoma cell lines with products in the the 799 bp and a second alternatively spliced transcript.

TIRP is a member of the Toll/interleukin-1 receptor (TIR) family, a group of proteins that include the Toll-like receptors (TLRs) (1-3). TLRs are signaling molecules that recognize different pathogen-associated molecular patterns (PAMPs) and serve as an important link between the innate and adaptive immune responses (4). TIRP, along with other molecules such as TRIF, MAL, and MyD88, serves as an adaptor protein that allows for the interaction and activation of the IL-1R-associated kinase (IRAK) family, the subsequent activation of TNF receptor associated factor (TRAF)-6, and ultimately the activation of NF-?B (5). Expression of TIRP appears to be essential for TLR4 signalling (6). **Cat.No. 3206

Toll-like receptors (TLRs) are signaling molecules that recognize different microbial products during infection and serve as an important link between the innate and adaptive immune responses (1-3). These proteins act through adaptor molecules such as TIRAP and MyD88 to activate various kinases and transcription factors (4,5). In TIRAP-deficient mice, TLR signaling in response to TLR2 ligands (using either TLR1 and TLR6 as co-receptors) is totally abolished, suggesting that MyD88 and TIRAP work together and are both required for TLR2 signaling (6). Furthermore, these mice are also resistant to the toxic effects of LPS and show defects in NF-κB and MAP kinase activation, suggesting that TIRAP is also involed in TLR4 signaling (6,7)

Toll-like receptors (TLRs) are signaling molecules that recognize different microbial products during infection and serve as an important link between the innate and adaptive immune responses (1-3). These proteins act through adaptor molecules such as TIRAP and MyD88 to activate various kinases and transcription factors (4,5). In TIRAP-deficient mice, TLR signaling in response to TLR2 ligands (using either TLR1 and TLR6 as co-receptors) is totally abolished, suggesting that MyD88 and TIRAP work together and are both required for TLR2 signaling (6). Furthermore, these mice are also resistant to the toxic effects of LPS and show defects in NF-?B and MAP kinase activation, suggesting that TIRAP is also involed in TLR4 signaling (6,7) **Cat.No. 3157