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Anticorps
Numéro de catalogue:
(BOSSBS-11233R-A350)
Fournisseur:
Bioss
Description:
The single-stranded-DNA-binding proteins (SSBs) are essential for DNA function in prokaryotic and eukaryotic cells, mitochondria, phages and viruses. Replication protein A (RPA), a highly conserved eukaryotic protein, is a heterotrimeric SSB. RPA plays an important role in DNA replication, recombination and repair. The binding of human RPA (hRPA) to DNA involves molecular polarity in which initial hRPA binding occurs on the 5' side of an ssDNA substrate and then extends in the 3' direction to create a stably bound hRPA. RPA is a major damage-recognition protein involved in the early stages of nucleotide excision repair. It can also play a role in telomere maintenance. The RPA 70 kDa subunit binds to ssDNA and mediates interactions with many cellular and viral proteins. The DNA binding domain lies in the middle of RPA 70 kDa subunit and comprises two structurally homologous subdomains oriented in tandem. RPA contains a conserved four cysteine-type zinc-finger motif, which mediates the transition of RPA-ssDNA interaction to a stable RPA-ssDNA complex in a redox-dependent manner.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11233R-A555)
Fournisseur:
Bioss
Description:
The single-stranded-DNA-binding proteins (SSBs) are essential for DNA function in prokaryotic and eukaryotic cells, mitochondria, phages and viruses. Replication protein A (RPA), a highly conserved eukaryotic protein, is a heterotrimeric SSB. RPA plays an important role in DNA replication, recombination and repair. The binding of human RPA (hRPA) to DNA involves molecular polarity in which initial hRPA binding occurs on the 5' side of an ssDNA substrate and then extends in the 3' direction to create a stably bound hRPA. RPA is a major damage-recognition protein involved in the early stages of nucleotide excision repair. It can also play a role in telomere maintenance. The RPA 70 kDa subunit binds to ssDNA and mediates interactions with many cellular and viral proteins. The DNA binding domain lies in the middle of RPA 70 kDa subunit and comprises two structurally homologous subdomains oriented in tandem. RPA contains a conserved four cysteine-type zinc-finger motif, which mediates the transition of RPA-ssDNA interaction to a stable RPA-ssDNA complex in a redox-dependent manner.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5089R-A680)
Fournisseur:
Bioss
Description:
Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5089R-A750)
Fournisseur:
Bioss
Description:
Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11843R-CY7)
Fournisseur:
Bioss
Description:
Growth/differentiation factors (GDFs) are members of the TGF superfamily (1,2). Members of the TGF superfamily are involved in embryonic development and adult tissue homeostasis (1). GDF-1 expression is almost exclusively restricted to the central nervous system and mediates cell differentiation events during embryonic development (3). Neither GDF-3 (Vgr-2) nor GDF-9 contains the conserved cysteine residue which is found in most other TGF superfamily members. GDF-3 is detectable in bone marrow, spleen, thymus and adipose tissue, whereas GDF-9 has only been detected in ovary (4). GDF-5 (also designated CDMP-1) has been shown to induce activation of plasminogen activator, thereby inducing angiogenesis. It is predominantly expressed in long bones during fetal embryonic development and is involved in bone formation. (5). GDF-5 mutations have been identified in mice with the mutation brachypodism (bp), a mutation which affects the length and number of bones in limbs (6). GDF-6 and GDF-7 are closely related to GDF-5 (6). GDF-8 has been shown to be a negative regulator of skeletal muscle mass (1).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1305R-A647)
Fournisseur:
Bioss
Description:
CCR7 is a member of the G protein coupled receptor family (subfamily : chemokine). This receptor was identified as a gene induced by the Epstein Barr virus (EBV), and is thought to be a mediator of EBV effects on B lymphocytes. CCR7 has been reported to be expressed in blood, bone marrow, lymph node, and intestine. It is particularly expressed in lymphoid tissues and in activated B and T lymphocytes and has been shown to control the migration of memory T cells to inflamed tissues, as well as stimulate dendritic cell maturation. The chemokine (C-C motif) ligand 19 (CCL19/ECL) has been reported to be a specific ligand of this receptor. ESTs have been isolated from blood, embryo, lymph node, and thymus libraries.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11843R-HRP)
Fournisseur:
Bioss
Description:
Growth/differentiation factors (GDFs) are members of the TGF superfamily (1,2). Members of the TGF superfamily are involved in embryonic development and adult tissue homeostasis (1). GDF-1 expression is almost exclusively restricted to the central nervous system and mediates cell differentiation events during embryonic development (3). Neither GDF-3 (Vgr-2) nor GDF-9 contains the conserved cysteine residue which is found in most other TGF superfamily members. GDF-3 is detectable in bone marrow, spleen, thymus and adipose tissue, whereas GDF-9 has only been detected in ovary (4). GDF-5 (also designated CDMP-1) has been shown to induce activation of plasminogen activator, thereby inducing angiogenesis. It is predominantly expressed in long bones during fetal embryonic development and is involved in bone formation. (5). GDF-5 mutations have been identified in mice with the mutation brachypodism (bp), a mutation which affects the length and number of bones in limbs (6). GDF-6 and GDF-7 are closely related to GDF-5 (6). GDF-8 has been shown to be a negative regulator of skeletal muscle mass (1).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-0988R-A350)
Fournisseur:
Bioss
Description:
Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes. Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system (By similarity). A second ligand, the heditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-0908R-A350)
Fournisseur:
Bioss
Description:
Non-receptor tyrosine kinase involved in various processes such as cell growth, development, differentiation or histone modifications. Mediates essential signaling events in both innate and adaptive immunity. In the cytoplasm, plays a pivotal role in signal transduction via its association with type I receptors such as growth hormone (GHR), prolactin (PRLR), leptin (LEPR), erythropoietin (EPOR), thrombopoietin (THPO); or type II receptors including IFN-alpha, IFN-beta, IFN-gamma and multiple interleukins. Following ligand-binding to cell surface receptors, phosphorylates specific tyrosine residues on the cytoplasmic tails of the receptor, creating docking sites for STATs proteins. Subsequently, phosphorylates the STATs proteins once they are recruited to the receptor. Phosphorylated STATs then form homodimer or heterodimers and translocate to the nucleus to activate gene transcription. For example, cell stimulation with erythropoietin (EPO) during erythropoiesis leads to JAK2 autophosphorylation, activation, and its association with erythropoietin receptor (EPOR) that becomes phosphorylated in its cytoplasmic domain. Then, STAT5 (STAT5A or STAT5B) is recruited, phosphorylated and activated by JAK2. Once activated, dimerized STAT5 translocates into the nucleus and promotes the transcription of several essential genes involved in the modulation of erythropoiesis. In addition, JAK2 mediates angiotensin-2-induced ARHGEF1 phosphorylation. Plays a role in cell cycle by phosphorylating CDKN1B. Cooperates with TEC through reciprocal phosphorylation to mediate cytokine-driven activation of FOS transcription. In the nucleus, plays a key role in chromatin by specifically mediating phosphorylation of 'Tyr-41' of histone H3 (H3Y41ph), a specific tag that promotes exclusion of CBX5 (HP1 alpha) from chromatin.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-6411R-FITC)
Fournisseur:
Bioss
Description:
CDK5 (Cyclin Dependent Kinase 5) is serine/threonine kinase involved in synaptic regulation and neuronal development; phosphorylates synaptic protein Pctaire1; regulates acetylcholine receptor expression. CDK5 is a member of the cyclindependent kinase family of serine/threonine kinases. It is present in numerous mammalian tissues including kidney, testes, and ovary. Its activity is detected almost exclusively in brain extracts. Neuronal and muscle cells contain the highest amount of this protein. Similar to other Cdks, monomeric Cdk5 displays no enzymatic activity, but Cdk5 is not activated by cyclins. Instead, the p35 protein, which is expressed solely in the brain, activates Cdk5. Cdk5 interacts with D1 and D3 type G1 cyclins and can phosphorylate histone H1, TAU, MAP2 and NF-H and NF-M. Cdk5 activity is involved in terminal differentiation of neurons and muscle cells.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-6411R-CY7)
Fournisseur:
Bioss
Description:
CDK5 (Cyclin Dependent Kinase 5) is serine/threonine kinase involved in synaptic regulation and neuronal development; phosphorylates synaptic protein Pctaire1; regulates acetylcholine receptor expression. CDK5 is a member of the cyclindependent kinase family of serine/threonine kinases. It is present in numerous mammalian tissues including kidney, testes, and ovary. Its activity is detected almost exclusively in brain extracts. Neuronal and muscle cells contain the highest amount of this protein. Similar to other Cdks, monomeric Cdk5 displays no enzymatic activity, but Cdk5 is not activated by cyclins. Instead, the p35 protein, which is expressed solely in the brain, activates Cdk5. Cdk5 interacts with D1 and D3 type G1 cyclins and can phosphorylate histone H1, TAU, MAP2 and NF-H and NF-M. Cdk5 activity is involved in terminal differentiation of neurons and muscle cells.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-0988R-A555)
Fournisseur:
Bioss
Description:
Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes. Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system (By similarity). A second ligand, the heditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-0908R-A488)
Fournisseur:
Bioss
Description:
Non-receptor tyrosine kinase involved in various processes such as cell growth, development, differentiation or histone modifications. Mediates essential signaling events in both innate and adaptive immunity. In the cytoplasm, plays a pivotal role in signal transduction via its association with type I receptors such as growth hormone (GHR), prolactin (PRLR), leptin (LEPR), erythropoietin (EPOR), thrombopoietin (THPO); or type II receptors including IFN-alpha, IFN-beta, IFN-gamma and multiple interleukins. Following ligand-binding to cell surface receptors, phosphorylates specific tyrosine residues on the cytoplasmic tails of the receptor, creating docking sites for STATs proteins. Subsequently, phosphorylates the STATs proteins once they are recruited to the receptor. Phosphorylated STATs then form homodimer or heterodimers and translocate to the nucleus to activate gene transcription. For example, cell stimulation with erythropoietin (EPO) during erythropoiesis leads to JAK2 autophosphorylation, activation, and its association with erythropoietin receptor (EPOR) that becomes phosphorylated in its cytoplasmic domain. Then, STAT5 (STAT5A or STAT5B) is recruited, phosphorylated and activated by JAK2. Once activated, dimerized STAT5 translocates into the nucleus and promotes the transcription of several essential genes involved in the modulation of erythropoiesis. In addition, JAK2 mediates angiotensin-2-induced ARHGEF1 phosphorylation. Plays a role in cell cycle by phosphorylating CDKN1B. Cooperates with TEC through reciprocal phosphorylation to mediate cytokine-driven activation of FOS transcription. In the nucleus, plays a key role in chromatin by specifically mediating phosphorylation of 'Tyr-41' of histone H3 (H3Y41ph), a specific tag that promotes exclusion of CBX5 (HP1 alpha) from chromatin.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13699R-CY3)
Fournisseur:
Bioss
Description:
Sam 68 is a protein that is phosphorylated on tyrosine and functions as a substrate for Src family tyrosine kinases during mitosis. Sam 68 also associates with several SH2 and SH3 domain-containing signaling proteins, such as GRB2 and PLC ?. Originally cloned as Ras GAP-associated p62, further investigations have shown that Sam 68 and Ras GAP-associated p62 are not antigenically related, nor are they encoded by the same gene. Like Sam 68, the Sam 68-like mammalian proteins, SLM-1 and SLM-2, demonstrate RNA binding activity. Also like Sam 68, SLM-1 is tyrosine phosphorylated and functions as an adapter protein for signaling molecules, including GRB2, PLC ?, Fyn and Ras GAP. SLM-2 is not tyrosine phosphorylated, nor does it appear to associate with GRB2, PLC ?, Fyn or Ras GAP, indicating that SLM-2 may not be an adapter protein for these proteins.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13699R-A750)
Fournisseur:
Bioss
Description:
Sam 68 is a protein that is phosphorylated on tyrosine and functions as a substrate for Src family tyrosine kinases during mitosis. Sam 68 also associates with several SH2 and SH3 domain-containing signaling proteins, such as GRB2 and PLC ?. Originally cloned as Ras GAP-associated p62, further investigations have shown that Sam 68 and Ras GAP-associated p62 are not antigenically related, nor are they encoded by the same gene. Like Sam 68, the Sam 68-like mammalian proteins, SLM-1 and SLM-2, demonstrate RNA binding activity. Also like Sam 68, SLM-1 is tyrosine phosphorylated and functions as an adapter protein for signaling molecules, including GRB2, PLC ?, Fyn and Ras GAP. SLM-2 is not tyrosine phosphorylated, nor does it appear to associate with GRB2, PLC ?, Fyn or Ras GAP, indicating that SLM-2 may not be an adapter protein for these proteins.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-9671R-A488)
Fournisseur:
Bioss
Description:
ASH1L is a 2,969 amino acid protein encoded by the human gene ASH1L. ASH1L belongs to the histone-lysine methyltransferase family (SET2 subfamily) and contains three AT hook DNA-binding domains, one AWS domain, one BAH domain, one bromodomain, one PHD-type zinc finger, one post-SET domain and one SET domain. It is a widely expressed nuclear protein with highest expression found in brain, heart and kidney. ASH1L is a histone methyltransferase and is believed to methylate 'Lys-4' of Histone H3, which is a specific tag for epigenetic transcriptional activation.
UOM:
1 * 100 µl
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