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block+heaters+
Numéro de catalogue:
(BNUM1010-50)
Fournisseur:
Biotium
Description:
Cytochrome C is a well-characterized mobile electron transport protein that is essential to energy conversion in all aerobic organisms. In mammalian cells, this highly conserved protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of cytochrome c and to induce cell death. The release of cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3. This MAb recognizes total cytochrome C which includes both apocytochrome (i.e. cytochrome in the cytosol without heme attached) and holocytochrome (i.e cytochrome in the mitochondria with heme attached).
UOM:
1 * 50 µl
Fournisseur:
Biotium
Description:
This MAb reacts with a 28 kDa chain of HLA-DRB1 antigen, a member of MHC class II molecules. It does not cross react with HLA-DP and HLA-DQ. The L243 antibody recognizes a different epitope than the LN3 monoclonal antibody, and these antibodies do not cross-block binding to each other's respective epitopes. HLA-DR is a heterodimeric cell surface glycoprotein comprised of a 36 kDa alpha (heavy) chain and a 28 kDa beta (light) chain. It is expressed on B-cells, activated T-cells, monocytes/macrophages, dendritic cells and other non-professional APCs. In conjunction with the CD3/TCR complex and CD4 molecules, HLA-DR is critical for efficient peptide presentation to CD4 T cells. It is an excellent histiocytic marker in paraffin sections producing intense staining. True histiocytic neoplasms are similarly positive. HLA-DR antigens also occur on a variety of epithelial cells and their corresponding neoplastic counterparts. Loss of HLA-DR expression is related to tumor microenvironment and predicts adverse outcome in diffuse large B-cell lymphoma.
Fournisseur:
Biotium
Description:
This MAb reacts with a 28 kDa chain of HLA-DRB1 antigen, a member of MHC class II molecules. It does not cross react with HLA-DP and HLA-DQ. The L243 antibody recognizes a different epitope than the LN3 monoclonal antibody, and these antibodies do not cross-block binding to each other's respective epitopes. HLA-DR is a heterodimeric cell surface glycoprotein comprised of a 36 kDa alpha (heavy) chain and a 28 kDa beta (light) chain. It is expressed on B-cells, activated T-cells, monocytes/macrophages, dendritic cells and other non-professional APCs. In conjunction with the CD3/TCR complex and CD4 molecules, HLA-DR is critical for efficient peptide presentation to CD4 T cells. It is an excellent histiocytic marker in paraffin sections producing intense staining. True histiocytic neoplasms are similarly positive. HLA-DR antigens also occur on a variety of epithelial cells and their corresponding neoplastic counterparts. Loss of HLA-DR expression is related to tumor microenvironment and predicts adverse outcome in diffuse large B-cell lymphoma.
Numéro de catalogue:
(BOSSBS-12495R-A750)
Fournisseur:
Bioss
Description:
APOBEC proteins inhibit retroviruses by deaminating cytosine residues of viral RNA and DNA. The seven APOBEC3 genes or pseudogenes are found in a cluster thought to result from gene duplication on chromosome 22. Like APOBEC3G, APOBEC3F deaminates deoxycytosine to deoxyuracil in the minus strand of HIV-1 DNA, resulting in G to A hypermutation in the plus strand of DNA. Thus, APOBEC3G and APOBEC3F provide a mechanism for innate immunity to retroviruses, and are also likely contribute to sequence variation observed in many viruses. Viral infectivity factor (Vif) imparts APOBEC3G and APOBEC3F resistance to HIV through impaired translation of their mRNA and accelerated posttranslational degradation of the APOBEC3 proteins by the 26S proteasome. Interestingly, HIV-1 Vif cannot form a complex with APOBEC3G or APOBEC3F of mouse origin as it does with the human protein, and thus mouse APOBEC3G and APOBEC3F function as a potent inhibitors of wildtype HIV-1 replication, where human APOBEC3G and APOBEC3F are only able to inhibit Vif-deficient HIV-1 replication. This implies that induction of APOBEC3G and APOBEC3F activity or a method of blocking their interaction with Vif may provide a method for therapeutic intervention.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12495R-A680)
Fournisseur:
Bioss
Description:
APOBEC proteins inhibit retroviruses by deaminating cytosine residues of viral RNA and DNA. The seven APOBEC3 genes or pseudogenes are found in a cluster thought to result from gene duplication on chromosome 22. Like APOBEC3G, APOBEC3F deaminates deoxycytosine to deoxyuracil in the minus strand of HIV-1 DNA, resulting in G to A hypermutation in the plus strand of DNA. Thus, APOBEC3G and APOBEC3F provide a mechanism for innate immunity to retroviruses, and are also likely contribute to sequence variation observed in many viruses. Viral infectivity factor (Vif) imparts APOBEC3G and APOBEC3F resistance to HIV through impaired translation of their mRNA and accelerated posttranslational degradation of the APOBEC3 proteins by the 26S proteasome. Interestingly, HIV-1 Vif cannot form a complex with APOBEC3G or APOBEC3F of mouse origin as it does with the human protein, and thus mouse APOBEC3G and APOBEC3F function as a potent inhibitors of wildtype HIV-1 replication, where human APOBEC3G and APOBEC3F are only able to inhibit Vif-deficient HIV-1 replication. This implies that induction of APOBEC3G and APOBEC3F activity or a method of blocking their interaction with Vif may provide a method for therapeutic intervention.
UOM:
1 * 100 µl
Numéro de catalogue:
(BNUM0057-50)
Fournisseur:
Biotium
Description:
This MAb reacts with a 28 kDa chain of HLA-DRB1 antigen, a member of MHC class II molecules. It does not cross react with HLA-DP and HLA-DQ. The L243 antibody recognizes a different epitope than the LN3 monoclonal antibody, and these antibodies do not cross-block binding to each other's respective epitopes. HLA-DR is a heterodimeric cell surface glycoprotein comprised of a 36 kDa alpha (heavy) chain and a 28 kDa beta (light) chain. It is expressed on B-cells, activated T-cells, monocytes/macrophages, dendritic cells and other non-professional APCs. In conjunction with the CD3/TCR complex and CD4 molecules, HLA-DR is critical for efficient peptide presentation to CD4 T cells. It is an excellent histiocytic marker in paraffin sections producing intense staining. True histiocytic neoplasms are similarly positive. HLA-DR antigens also occur on a variety of epithelial cells and their corresponding neoplastic counterparts. Loss of HLA-DR expression is related to tumor microenvironment and predicts adverse outcome in diffuse large B-cell lymphoma.
UOM:
1 * 50 µl
Numéro de catalogue:
(BOSSBS-12495R-A555)
Fournisseur:
Bioss
Description:
APOBEC proteins inhibit retroviruses by deaminating cytosine residues of viral RNA and DNA. The seven APOBEC3 genes or pseudogenes are found in a cluster thought to result from gene duplication on chromosome 22. Like APOBEC3G, APOBEC3F deaminates deoxycytosine to deoxyuracil in the minus strand of HIV-1 DNA, resulting in G to A hypermutation in the plus strand of DNA. Thus, APOBEC3G and APOBEC3F provide a mechanism for innate immunity to retroviruses, and are also likely contribute to sequence variation observed in many viruses. Viral infectivity factor (Vif) imparts APOBEC3G and APOBEC3F resistance to HIV through impaired translation of their mRNA and accelerated posttranslational degradation of the APOBEC3 proteins by the 26S proteasome. Interestingly, HIV-1 Vif cannot form a complex with APOBEC3G or APOBEC3F of mouse origin as it does with the human protein, and thus mouse APOBEC3G and APOBEC3F function as a potent inhibitors of wildtype HIV-1 replication, where human APOBEC3G and APOBEC3F are only able to inhibit Vif-deficient HIV-1 replication. This implies that induction of APOBEC3G and APOBEC3F activity or a method of blocking their interaction with Vif may provide a method for therapeutic intervention.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3088R-A750)
Fournisseur:
Bioss
Description:
Key downstream component of the canonical Wnt signaling pathway. In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes. Involved in the regulation of cell adhesion. Acts as a negative regulator of centrosome cohesion. Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2. Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-2781R-A750)
Fournisseur:
Bioss
Description:
Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1G gives rise to T-type calcium currents. T-type calcium channels belong to the 'low-voltage activated (LVA)' group and are strongly blocked by mibefradil. A particularity of this type of channel is an opening at quite negative potentials and a voltage-dependent inactivation. T-type channels serve pacemaking functions in both central neurons and cardiac nodal cells and support calcium signaling in secretory cells and vascular smooth muscle. They may also be involved in the modulation of firing patterns of neurons which is important for information processing as well as in cell growth processes.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11483R-A647)
Fournisseur:
Bioss
Description:
Semaphorins are a family of cell surface and secreted proteins involved in neural development that are conserved from insects to humans. Members of this family are approximately 750 amino acids in length (including signal sequences) and are defined by a conserved extracellular “semaphorin†domain of approximately 500 amino acids containing 14-16 cysteines, blocks of conserved sequences and no obvious repeats. The transmembrane semaphorins are characterized by an additional 80 amino acid transmembrane domain and an 80-110 amino acid cytoplasmic domain. SEMA6C, also known as SEMA Y, is a transmembrane protein expressed in fetal brain and adult skeletal muscle. Three isoforms of this semaphorin exist due to alternative splicing: SEMA6C 1, SEMA6C 2 and SEMA6C 3. The extracellular domain of SEMA6C induces growth cone collapse of dorsal root ganglion and plays a role in generation or stability of entorhino-hippocampal synapses.
UOM:
1 * 100 µl
Fournisseur:
Biotium
Description:
This MAb reacts with a CD32 (FcgRII) epitope (cluster-4). It displays a stronger reaction with Daudi than with U937 cells. The epitope is located in domain 2 of FcgRIIa. Its Fab'2 fragments block immune complex binding. CD32 (FcgRII) is a type 1 transmembrane glycoprotein that mediates several functions including phagocytosis, cytotoxicity, and immunomodulation as well as platelet aggregation. Three genes (A, B, and C) encode CD32 and at least 6 isoforms are generated via alternative mRNA splicing, i.e., IIa1, IIa2, IIb1, IIb2, IIb3 and IIc. Monocytes/macrophages, placental trophoblasts and endothelial cells express all isoforms. In addition, the IIb isoform is expressed by B cells, and the IIa isoform by platelets, granulocytes and, weakly, by B cells. NK cells and neutrophils express Isoform IIc. CD32 binds weakly to the Fc region of monomeric IgG but more strongly to IgG aggregates and immune complexes.
Numéro de catalogue:
(BOSSBS-9022R-CY3)
Fournisseur:
Bioss
Description:
IQCG is a 443 amino acid protein containing one IQ domain. Widely distributed in nature, the IQ domain forms an amphiphilic seven-turn α-helix capable of binding calmodulin in a Ca2+-independent manner. The level of intracellular calcium is tightly regulated in all eukaryotic cells. A modest increase in this level can result in a myriad of physiological responses, most of which are mediated by calmodulin (CaM), the universal calcium sensor. In acute T-lymphoid/myeloid leukemia, IQCG forms a complex with Nup98, an O-linked glycoprotein and a component of the nuclear pore complex. NUP98-IQCG complex bind co-activators and/or co-repressors, which suggest a role in transcriptional regulation.Nup98-IQCG complex inhibits 32Dcl3 cell apoptosis induced by Arabinofuranosylcytosine (Ara-C) and partially blocks granulocyte differentiation induced by G-CSF. IQCG exists as two isoforms due to alternatively splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-9022R-CY5)
Fournisseur:
Bioss
Description:
IQCG is a 443 amino acid protein containing one IQ domain. Widely distributed in nature, the IQ domain forms an amphiphilic seven-turn α-helix capable of binding calmodulin in a Ca2+-independent manner. The level of intracellular calcium is tightly regulated in all eukaryotic cells. A modest increase in this level can result in a myriad of physiological responses, most of which are mediated by calmodulin (CaM), the universal calcium sensor. In acute T-lymphoid/myeloid leukemia, IQCG forms a complex with Nup98, an O-linked glycoprotein and a component of the nuclear pore complex. NUP98-IQCG complex bind co-activators and/or co-repressors, which suggest a role in transcriptional regulation.Nup98-IQCG complex inhibits 32Dcl3 cell apoptosis induced by Arabinofuranosylcytosine (Ara-C) and partially blocks granulocyte differentiation induced by G-CSF. IQCG exists as two isoforms due to alternatively splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5220R-A750)
Fournisseur:
Bioss
Description:
BCL2 is an integral outer mitochondrial membrane protein that blocks the apoptotic death of some cells such as lymphocytes. Constitutive expression of BCL2, such as in the case of translocation of BCL2 to Ig heavy chain locus, is thought to be the cause of follicular lymphoma. Two transcript variants (alpha and beta) produced by alternate splicing, differ in their C-terminal ends. BCL2 suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. It regulates cell death by controlling the mitochondrial membrane permeability. It appears to function in a feedback loop system with caspases. BCL2 inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF1). It can form homodimers, and heterodimers with BAX, BAD, BAK and BclX(L). Heterodimerization with BAX requires intact BH1 and BH2 domains, and is necessary for anti-apoptotic activity.
UOM:
1 * 100 µl
Fournisseur:
Biotium
Description:
This MAb reacts with a CD32 (FcgRII) epitope (cluster-4). It displays a stronger reaction with Daudi than with U937 cells. The epitope is located in domain 2 of FcgRIIa. Its Fab'2 fragments block immune complex binding. CD32 (FcgRII) is a type 1 transmembrane glycoprotein that mediates several functions including phagocytosis, cytotoxicity, and immunomodulation as well as platelet aggregation. Three genes (A, B, and C) encode CD32 and at least 6 isoforms are generated via alternative mRNA splicing, i.e., IIa1, IIa2, IIb1, IIb2, IIb3 and IIc. Monocytes/macrophages, placental trophoblasts and endothelial cells express all isoforms. In addition, the IIb isoform is expressed by B cells, and the IIa isoform by platelets, granulocytes and, weakly, by B cells. NK cells and neutrophils express Isoform IIc. CD32 binds weakly to the Fc region of monomeric IgG but more strongly to IgG aggregates and immune complexes.
Fournisseur:
Biotium
Description:
This MAb reacts with a CD32 (FcgRII) epitope (cluster-4). It displays a stronger reaction with Daudi than with U937 cells. The epitope is located in domain 2 of FcgRIIa. Its Fab'2 fragments block immune complex binding. CD32 (FcgRII) is a type 1 transmembrane glycoprotein that mediates several functions including phagocytosis, cytotoxicity, and immunomodulation as well as platelet aggregation. Three genes (A, B, and C) encode CD32 and at least 6 isoforms are generated via alternative mRNA splicing, i.e., IIa1, IIa2, IIb1, IIb2, IIb3 and IIc. Monocytes/macrophages, placental trophoblasts and endothelial cells express all isoforms. In addition, the IIb isoform is expressed by B cells, and the IIa isoform by platelets, granulocytes and, weakly, by B cells. NK cells and neutrophils express Isoform IIc. CD32 binds weakly to the Fc region of monomeric IgG but more strongly to IgG aggregates and immune complexes.
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