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Image Unavailable-BOSSBS-1194R-A488

Anti-NFkB p105/p50 Rabbit Polyclonal Antibody (Alexa Fluor® 488)

Catalog Number: (BOSSBS-1194R-A488)
Supplier: Bioss
Description: NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and RelB-p50 complexes are transcriptional activators. The NF-kappa-B p50-p50 homodimer is a transcriptional repressor, but can act as a transcriptional activator when associated with BCL3. NFKB1 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p105 and generation of p50 by a cotranslational processing. The proteasome-mediated process ensures the production of both p50 and p105 and preserves their independent function, although processing of NFKB1/p105 also appears to occur post-translationally.
UOM: 1 * 100 µl
Image Unavailable-BOSSBS-1194R-A350

Anti-NFkB p105/p50 Rabbit Polyclonal Antibody (Alexa Fluor® 350)

Catalog Number: (BOSSBS-1194R-A350)
Supplier: Bioss
Description: NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and RelB-p50 complexes are transcriptional activators. The NF-kappa-B p50-p50 homodimer is a transcriptional repressor, but can act as a transcriptional activator when associated with BCL3. NFKB1 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p105 and generation of p50 by a cotranslational processing. The proteasome-mediated process ensures the production of both p50 and p105 and preserves their independent function, although processing of NFKB1/p105 also appears to occur post-translationally.
UOM: 1 * 100 µl
Image Unavailable-BOSSBS-1194R-A680

Anti-NFkB p105 / p50 Rabbit Polyclonal Antibody (Alexa Fluor® 680)

Catalog Number: (BOSSBS-1194R-A680)
Supplier: Bioss
Description: NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalisation as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and RelB-p50 complexes are transcriptional activators. The NF-kappa-B p50-p50 homodimer is a transcriptional repressor, but can act as a transcriptional activator when associated with BCL3. NFKB1 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p105 and generation of p50 by a cotranslational processing. The proteasome-mediated process ensures the production of both p50 and p105 and preserves their independent function, although processing of NFKB1/p105 also appears to occur post-translationally.
UOM: 1 * 100 µl
Image Unavailable-BOSSBS-1194R-CY7

Anti-NFkB p105/p50 Rabbit Polyclonal Antibody (Cy7®)

Catalog Number: (BOSSBS-1194R-CY7)
Supplier: Bioss
Description: NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and RelB-p50 complexes are transcriptional activators. The NF-kappa-B p50-p50 homodimer is a transcriptional repressor, but can act as a transcriptional activator when associated with BCL3. NFKB1 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p105 and generation of p50 by a cotranslational processing. The proteasome-mediated process ensures the production of both p50 and p105 and preserves their independent function, although processing of NFKB1/p105 also appears to occur post-translationally.
UOM: 1 * 100 µl
Image Unavailable-BOSSBS-5980R-A647

Anti-N-Myc Rabbit Polyclonal Antibody (Alexa Fluor® 647)

Catalog Number: (BOSSBS-5980R-A647)
Supplier: Bioss
Description: This gene is a member of the MYC family and encodes a protein with a basic helix-loop-helix (bHLH) domain. This protein is located in the nucleus and must dimerize with another bHLH protein in order to bind DNA. Amplification of this gene is associated with a variety of tumors, most notably neuroblastomas. [provided by RefSeq, Jul 2008].
UOM: 1 * 100 µl
Product Image-BOSSBS-5662R

Anti-RELA Rabbit Polyclonal Antibody

Catalog Number: (BOSSBS-5662R)
Supplier: Bioss
Description: NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and p65-c-Rel complexes are transcriptional activators. The NF-kappa-B p65-p65 complex appears to be involved in invasin-mediated activation of IL-8 expression. The inhibitory effect of I-kappa-B upon NF-kappa-B the cytoplasm is exerted primarily through the interaction with p65. p65 shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappa-B complex. Associates with chromatin at the NF-kappa-B promoter region via association with DDX1. Essential for cytokine gene expression in T-cells (PubMed:15790681).
UOM: 1 * 100 µl
Image Unavailable-BOSSBS-5662R-HRP

Anti-RELA Rabbit Polyclonal Antibody (HRP (Horseradish Peroxidase))

Catalog Number: (BOSSBS-5662R-HRP)
Supplier: Bioss
Description: NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and p65-c-Rel complexes are transcriptional activators. The NF-kappa-B p65-p65 complex appears to be involved in invasin-mediated activation of IL-8 expression. The inhibitory effect of I-kappa-B upon NF-kappa-B the cytoplasm is exerted primarily through the interaction with p65. p65 shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappa-B complex. Associates with chromatin at the NF-kappa-B promoter region via association with DDX1. Essential for cytokine gene expression in T-cells (PubMed:15790681).
UOM: 1 * 100 µl
Image Unavailable-BOSSBS-5662R-FITC

Anti-RELA Rabbit Polyclonal Antibody (FITC (Fluorescein Isothiocyanate))

Catalog Number: (BOSSBS-5662R-FITC)
Supplier: Bioss
Description: NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and p65-c-Rel complexes are transcriptional activators. The NF-kappa-B p65-p65 complex appears to be involved in invasin-mediated activation of IL-8 expression. The inhibitory effect of I-kappa-B upon NF-kappa-B the cytoplasm is exerted primarily through the interaction with p65. p65 shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappa-B complex. Associates with chromatin at the NF-kappa-B promoter region via association with DDX1. Essential for cytokine gene expression in T-cells (PubMed:15790681).
UOM: 1 * 100 µl
Image Unavailable-BOSSBS-5662R-A647

Anti-RELA Rabbit Polyclonal Antibody (Alexa Fluor® 647)

Catalog Number: (BOSSBS-5662R-A647)
Supplier: Bioss
Description: NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and p65-c-Rel complexes are transcriptional activators. The NF-kappa-B p65-p65 complex appears to be involved in invasin-mediated activation of IL-8 expression. The inhibitory effect of I-kappa-B upon NF-kappa-B the cytoplasm is exerted primarily through the interaction with p65. p65 shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappa-B complex. Associates with chromatin at the NF-kappa-B promoter region via association with DDX1. Essential for cytokine gene expression in T-cells (PubMed:15790681).
UOM: 1 * 100 µl
Image Unavailable-BNC400023-100

Anti-TG Mouse Monoclonal Antibody (CF640R) [clone: 2H11]

Supplier: Biotium
Description: MAb 2H11 reacts with a partially defined epitope of human thyroglobulin. This epitope is different form the epitope recognized by MAb 6E1. Thyroglobulin is a 660 kDa dimeric pre-protein with mutiple glycosylation sites. It is produced by and processed within the thyroid gland to produce the hormone thyroxine and triiodothyronine. Prior to forming dimers, thyroglobulin monomers undergo conformational maturation in the endoplasmic reticulation. The vast majority of follicular carcinomas of the thyroid will give positive immunoreactivity for anti-thyroglobulin even though sometimes only focally. Poorly differentiated carcinomas of the thyroid are frequently anti-thyroglobulin negative. Adenocarcinomas of other-than-thyroid origin do not react with this antibody. This antibody is useful in identification of thyroid carcinoma of the papillary and follicular types. Presence of thyroglobulin in metastatic lesions establishes the thyroid origin of tumor. Anti-thyroglobulin, combined with anti-calcitonin, can identify medullary carcinomas of the thyroid. Furthermore, anti-thyroglobulin, combined with anti-TTF1, can be a reliable marker to differentiate between primary thyroid and lung neoplasms.

Image Unavailable-ENZOADISPA830488D

Anti-HSP90 Mouse Monoclonal Antibody (DyLight® 488)

Supplier: ENZO LIFE SCIENCES
Description: The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress, and includes cytoplasmic (Hsp90-alpha/beta), ER (grp94), and mitochondrial (TRAP1) localized members. Structurally, Hsp90 is characterized by an N-terminal ATP-binding domain, a medial substrate-binding domain, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones (e.g. Hsp40, Hsp70, Hop, p23) to stabilize a multitude of client protein substrates, including steroid hormone receptors, protein kinases, and transcription factors. The essential binding and hydrolysis of ATP by Hsp90 is inhibited by ansamycin drugs (e.g. geldanamycin, 17-AAG) which occupy the N-terminal Hsp90 nucleotide-binding pocket. Many Hsp90 client proteins such as erbB2/Her-2, c-raf, bcr-abl, p53, and hTERT, are members of well characterized oncogenic pathways, making Hsp90 inhibitors useful anticancer agents.

Image Unavailable-BNC680761-500

Anti-IGHA1 & IGHA2 Mouse Monoclonal Antibody (CF568) [clone: IA761]

Supplier: Biotium
Description: This MAb is specific to heavy chain of IgA and shows minimal cross-reaction with heavy chains of other immunoglobulins. It is reactive with all subclasses of Alpha heavy chain. Immunoglobulins are four-chain, Y-shaped, monomeric structures comprised of two identical heavy chains and two identical light chains held together through inter-chain disulfide bonds. The chains form two domains, the Fab (antigen binding) fragment and the Fc (constant) fragment. Immunoglobulin A (IgA) is the main protein of the mucosal immune system. It is generated by B-cells in gut-associated lymphoid tissues. Daily production of IgA exceeds that of any of the other immunoglobulins.IgA exists mainly in dimers but can also exist as polymers or as monomers. Dimers and polymers contain a joining (J) chain that can be bound by the polymeric immunoglobulin receptor (pIgR) for transportation of the molecule to mucosal surfaces. The most common feature of plasmacytomas, and certain non-Hodgkin's lymphomas is the restricted expression of a single heavy chain class. Demonstration of clonality in lymphoid infiltrates indicates that the infiltrate is clonal and therefore malignant.

Image Unavailable-BNC940761-100

Anti-IGHA1 & IGHA2 Mouse Monoclonal Antibody (CF594) [clone: IA761]

Supplier: Biotium
Description: This MAb is specific to heavy chain of IgA and shows minimal cross-reaction with heavy chains of other immunoglobulins. It is reactive with all subclasses of Alpha heavy chain. Immunoglobulins are four-chain, Y-shaped, monomeric structures comprised of two identical heavy chains and two identical light chains held together through inter-chain disulfide bonds. The chains form two domains, the Fab (antigen binding) fragment and the Fc (constant) fragment. Immunoglobulin A (IgA) is the main protein of the mucosal immune system. It is generated by B-cells in gut-associated lymphoid tissues. Daily production of IgA exceeds that of any of the other immunoglobulins.IgA exists mainly in dimers but can also exist as polymers or as monomers. Dimers and polymers contain a joining (J) chain that can be bound by the polymeric immunoglobulin receptor (pIgR) for transportation of the molecule to mucosal surfaces. The most common feature of plasmacytomas, and certain non-Hodgkin's lymphomas is the restricted expression of a single heavy chain class. Demonstration of clonality in lymphoid infiltrates indicates that the infiltrate is clonal and therefore malignant.

Image Unavailable-BNC470761-100

Anti-IGHA1 & IGHA2 Mouse Monoclonal Antibody (CF647) [clone: IA761]

Supplier: Biotium
Description: This MAb is specific to heavy chain of IgA and shows minimal cross-reaction with heavy chains of other immunoglobulins. It is reactive with all subclasses of Alpha heavy chain. Immunoglobulins are four-chain, Y-shaped, monomeric structures comprised of two identical heavy chains and two identical light chains held together through inter-chain disulfide bonds. The chains form two domains, the Fab (antigen binding) fragment and the Fc (constant) fragment. Immunoglobulin A (IgA) is the main protein of the mucosal immune system. It is generated by B-cells in gut-associated lymphoid tissues. Daily production of IgA exceeds that of any of the other immunoglobulins.IgA exists mainly in dimers but can also exist as polymers or as monomers. Dimers and polymers contain a joining (J) chain that can be bound by the polymeric immunoglobulin receptor (pIgR) for transportation of the molecule to mucosal surfaces. The most common feature of plasmacytomas, and certain non-Hodgkin's lymphomas is the restricted expression of a single heavy chain class. Demonstration of clonality in lymphoid infiltrates indicates that the infiltrate is clonal and therefore malignant.

Image Unavailable-BNC400761-100

Anti-IGHA1 & IGHA2 Mouse Monoclonal Antibody (CF640R) [clone: IA761]

Supplier: Biotium
Description: This MAb is specific to heavy chain of IgA and shows minimal cross-reaction with heavy chains of other immunoglobulins. It is reactive with all subclasses of Alpha heavy chain. Immunoglobulins are four-chain, Y-shaped, monomeric structures comprised of two identical heavy chains and two identical light chains held together through inter-chain disulfide bonds. The chains form two domains, the Fab (antigen binding) fragment and the Fc (constant) fragment. Immunoglobulin A (IgA) is the main protein of the mucosal immune system. It is generated by B-cells in gut-associated lymphoid tissues. Daily production of IgA exceeds that of any of the other immunoglobulins.IgA exists mainly in dimers but can also exist as polymers or as monomers. Dimers and polymers contain a joining (J) chain that can be bound by the polymeric immunoglobulin receptor (pIgR) for transportation of the molecule to mucosal surfaces. The most common feature of plasmacytomas, and certain non-Hodgkin's lymphomas is the restricted expression of a single heavy chain class. Demonstration of clonality in lymphoid infiltrates indicates that the infiltrate is clonal and therefore malignant.

Image Unavailable-BOSSBS-0465R-A350

Anti-RELA Rabbit Polyclonal Antibody (Alexa Fluor® 350)

Catalog Number: (BOSSBS-0465R-A350)
Supplier: Bioss
Description: NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p15, NFKB1/p5, REL and NFKB2/p52 and the heterodimeric p65-p5 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p5 and p65-c-Rel complexes are transcriptional activators. The NF-kappa-B p65-p65 complex appears to be involved in invasin-mediated activation of IL-8 expression. The inhibitory effect of I-kappa-B upon NF-kappa-B the cytoplasm is exerted primarily through the interaction with p65. p65 shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappa-B complex. Associates with chromatin at the NF-kappa-B promoter region via association with DDX1.
UOM: 1 * 100 µl
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