277 Results for: "hydrophobic interaction"

Supplier: Proteintech

Killer cell immunoglobulin-like receptors (KIRs) are a diverse family of inhibitory and activating receptors expressed on NK cells and a subset of T cells . These polymorphic receptors interact with specific motifs on HLA class I molecules, modulate NK cytolytic activity and are encoded by genes located on chromosome 19q13.4 . KIR2DL3, also known as CD158B2 or NKAT2, is an inhibitory receptor that is specific for HLA-C alleles (HLA-Cw1, HLA-Cw3 and HLA-Cw7) . It is a 341-amino acid transmembrane glycoprotein consisting of an extracellular region containing two C2-type Ig-like domains, a 19-amino acid hydrophobic transmembrane region, and a long cytoplasmic tail with two immunoreceptor tyrosine-based inhibitory motifs (ITIMs). KIR2DL3 inhibits the cytolytic activity of NK cells thus preventing cell lysis .

Supplier: Bioss

Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with H at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis (By similarity).

Supplier: Bioss

This endogenous retroviral envelope protein has retained its original fusogenic properties and participates in trophoblast fusion and the formation of a syncytium during placenta morphogenesis. The interaction with MFSD2A is apparently important for this process. Endogenous envelope proteins may have kept, lost or modified their original function during evolution but this one can still make pseudotypes with MLV, HIV-1 or SIV-1 virions and confer infectivity. Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. The surface protein mediates receptor recognition, while the transmembrane protein anchors the envelope heterodimer to the viral membrane through one transmembrane domain. The other hydrophobic domain, called fusion peptide, mediates fusion of the viral membrane with the target cell membrane.

Supplier: Bioss

This endogenous retroviral envelope protein has retained its original fusogenic properties and participates in trophoblast fusion and the formation of a syncytium during placenta morphogenesis. The interaction with MFSD2A is apparently important for this process. Endogenous envelope proteins may have kept, lost or modified their original function during evolution but this one can still make pseudotypes with MLV, HIV-1 or SIV-1 virions and confer infectivity. Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. The surface protein mediates receptor recognition, while the transmembrane protein anchors the envelope heterodimer to the viral membrane through one transmembrane domain. The other hydrophobic domain, called fusion peptide, mediates fusion of the viral membrane with the target cell membrane.

Supplier: Bioss

This endogenous retroviral envelope protein has retained its original fusogenic properties and participates in trophoblast fusion and the formation of a syncytium during placenta morphogenesis. The interaction with MFSD2A is apparently important for this process. Endogenous envelope proteins may have kept, lost or modified their original function during evolution but this one can still make pseudotypes with MLV, HIV-1 or SIV-1 virions and confer infectivity. Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. The surface protein mediates receptor recognition, while the transmembrane protein anchors the envelope heterodimer to the viral membrane through one transmembrane domain. The other hydrophobic domain, called fusion peptide, mediates fusion of the viral membrane with the target cell membrane.

Supplier: Bioss

The leucine-rich (LRR) repeat is a 20-30 amino acid motif that forms a hydrophobic å/∫ horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. The primary function of these motifs is to provide a versatile structural framework to mediate the formation of protein-protein interactions. LRRs are present in a variety of proteins with diverse structure and function, including innate immunity and nervous system development. Several human diseases are associated with mutations in genes encoding LRR-containing proteins. The leucine-rich repeat-containing protein 39 (LRRC39) is a 335 amino acid protein that contains nine LRR repeats and exists as two alternatively spliced isoforms.

Supplier: Bioss

The leucine-rich (LRR) repeat is a 20-30 amino acid motif that forms a hydrophobic å/∫ horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. The primary function of these motifs is to provide a versatile structural framework to mediate the formation of protein-protein interactions. LRRs are present in a variety of proteins with diverse structure and function, including innate immunity and nervous system development. Several human diseases are associated with mutations in genes encoding LRR-containing proteins. The leucine-rich repeat-containing protein 39 (LRRC39) is a 335 amino acid protein that contains nine LRR repeats and exists as two alternatively spliced isoforms.

Supplier: Bioss

The leucine-rich (LRR) repeat is a 20-30 amino acid motif that forms a hydrophobic å/∫ horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. The primary function of these motifs is to provide a versatile structural framework to mediate the formation of protein-protein interactions. LRRs are present in a variety of proteins with diverse structure and function, including innate immunity and nervous system development. Several human diseases are associated with mutations in genes encoding LRR-containing proteins. The leucine-rich repeat-containing protein 39 (LRRC39) is a 335 amino acid protein that contains nine LRR repeats and exists as two alternatively spliced isoforms.

Supplier: Bioss

The leucine-rich (LRR) repeat is a 20-30 amino acid motif that forms a hydrophobic å/∫ horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. The primary function of these motifs is to provide a versatile structural framework to mediate the formation of protein-protein interactions. LRRs are present in a variety of proteins with diverse structure and function, including innate immunity and nervous system development. Several human diseases are associated with mutations in genes encoding LRR-containing proteins. The leucine-rich repeat-containing protein 39 (LRRC39) is a 335 amino acid protein that contains nine LRR repeats and exists as two alternatively spliced isoforms.

Supplier: Bioss

The leucine-rich (LRR) repeat is a 20-30 amino acid motif that forms a hydrophobic å/∫ horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. The primary function of these motifs is to provide a versatile structural framework to mediate the formation of protein-protein interactions. LRRs are present in a variety of proteins with diverse structure and function, including innate immunity and nervous system development. Several human diseases are associated with mutations in genes encoding LRR-containing proteins. The leucine-rich repeat-containing protein 39 (LRRC39) is a 335 amino acid protein that contains nine LRR repeats and exists as two alternatively spliced isoforms.

Supplier: Bioss

The leucine-rich (LRR) repeat is a 20-30 amino acid motif that forms a hydrophobic å/∫ horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. The primary function of these motifs is to provide a versatile structural framework to mediate the formation of protein-protein interactions. LRRs are present in a variety of proteins with diverse structure and function, including innate immunity and nervous system development. Several human diseases are associated with mutations in genes encoding LRR-containing proteins. The leucine-rich repeat-containing protein 39 (LRRC39) is a 335 amino acid protein that contains nine LRR repeats and exists as two alternatively spliced isoforms.

Supplier: Bioss

The leucine-rich (LRR) repeat is a 20-30 amino acid motif that forms a hydrophobic å/∫ horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. The primary function of these motifs is to provide a versatile structural framework to mediate the formation of protein-protein interactions. LRRs are present in a variety of proteins with diverse structure and function, including innate immunity and nervous system development. Several human diseases are associated with mutations in genes encoding LRR-containing proteins. LRRC23 (leucine-rich repeat-containing protein 23), also known as leucine-rich protein B7, is a 343 amino acid protein that contains eight LRR (leucine-rich) repeasts and one LRRCT domain. LRRC23 exists as two alternatively spliced isoforms and is encoded by a gene mapping to chromosome 12.

Supplier: Bioss

The adenovirus E1B protein is a viral homolog of the Bcl-2 family of proteins that are involved in regulating cell death. A family of interacting proteins, which are designated Nip or Bnip and include BNIP-1, BNIP-2, BNIP-3 and Nix, associate with both the E1B protein and Bcl-2 proteins to mediate apoptotic signaling. BNIP-1 contains a hydrophobic transmembrane domain, which enables its localization to the nuclear envelope, endoplasmic recticulum and mitochondria. BNIP-2, (previously designated Nip2 and Nip21 in human and mouse respectively), shares homology with the non-catalytic domain of Cdc42 GTPase-activating protein (Cdc42GAP). Through binding to Cdc42GAP, BNIP-2 enhances the GTPase activity of Cdc42GAP, facilitating the hydrolysis of GTP bound to Cdc42 and thereby, mediating the signaling pathways involving receptor kinases, small GTPases and apoptotic proteins. Nix, which is also designated Nip3L or Bnip3L, is highly related to BNIP-3, and both proteins localize to the mitochondria where they associate with Bcl-2 proteins. BNIP-3 preferentially binds to Bcl-xL and induces apoptosis by suppressing the anti-apoptosis activity of Bcl-xL.

Supplier: Bioss

The adenovirus E1B protein is a viral homolog of the Bcl-2 family of proteins that are involved in regulating cell death. A family of interacting proteins, which are designated Nip or Bnip and include BNIP-1, BNIP-2, BNIP-3 and Nix, associate with both the E1B protein and Bcl-2 proteins to mediate apoptotic signaling. BNIP-1 contains a hydrophobic transmembrane domain, which enables its localization to the nuclear envelope, endoplasmic recticulum and mitochondria. BNIP-2, (previously designated Nip2 and Nip21 in human and mouse respectively), shares homology with the non-catalytic domain of Cdc42 GTPase-activating protein (Cdc42GAP). Through binding to Cdc42GAP, BNIP-2 enhances the GTPase activity of Cdc42GAP, facilitating the hydrolysis of GTP bound to Cdc42 and thereby, mediating the signaling pathways involving receptor kinases, small GTPases and apoptotic proteins. Nix, which is also designated Nip3L or Bnip3L, is highly related to BNIP-3, and both proteins localize to the mitochondria where they associate with Bcl-2 proteins. BNIP-3 preferentially binds to Bcl-xL and induces apoptosis by suppressing the anti-apoptosis activity of Bcl-xL.

Supplier: Bioss

The leucine-rich (LRR) repeat is a 20-30 amino acid motif that forms a hydrophobic å/∫ horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. The primary function of these motifs is to provide a versatile structural framework to mediate the formation of protein-protein interactions. LRRs are present in a variety of proteins with diverse structure and function, including innate immunity and nervous system development. Several human diseases are associated with mutations in genes encoding LRR-containing proteins. LRRC23 (leucine-rich repeat-containing protein 23), also known as leucine-rich protein B7, is a 343 amino acid protein that contains eight LRR (leucine-rich) repeasts and one LRRCT domain. LRRC23 exists as two alternatively spliced isoforms and is encoded by a gene mapping to chromosome 12.

Supplier: Bioss

The leucine-rich (LRR) repeat is a 20-30 amino acid motif that forms a hydrophobic å/∫ horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. The primary function of these motifs is to provide a versatile structural framework to mediate the formation of protein-protein interactions. LRRs are present in a variety of proteins with diverse structure and function, including innate immunity and nervous system development. Several human diseases are associated with mutations in genes encoding LRR-containing proteins. LRRC23 (leucine-rich repeat-containing protein 23), also known as leucine-rich protein B7, is a 343 amino acid protein that contains eight LRR (leucine-rich) repeasts and one LRRCT domain. LRRC23 exists as two alternatively spliced isoforms and is encoded by a gene mapping to chromosome 12.

Supplier: Bioss

The leucine-rich (LRR) repeat is a 20-30 amino acid motif that forms a hydrophobic å/∫ horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. The primary function of these motifs is to provide a versatile structural framework to mediate the formation of protein-protein interactions. LRRs are present in a variety of proteins with diverse structure and function, including innate immunity and nervous system development. Several human diseases are associated with mutations in genes encoding LRR-containing proteins. LRRC23 (leucine-rich repeat-containing protein 23), also known as leucine-rich protein B7, is a 343 amino acid protein that contains eight LRR (leucine-rich) repeasts and one LRRCT domain. LRRC23 exists as two alternatively spliced isoforms and is encoded by a gene mapping to chromosome 12.

Supplier: Bioss

The leucine-rich (LRR) repeat is a 20-30 amino acid motif that forms a hydrophobic å/∫ horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. The primary function of these motifs is to provide a versatile structural framework to mediate the formation of protein-protein interactions. LRRs are present in a variety of proteins with diverse structure and function, including innate immunity and nervous system development. Several human diseases are associated with mutations in genes encoding LRR-containing proteins. LRRC23 (leucine-rich repeat-containing protein 23), also known as leucine-rich protein B7, is a 343 amino acid protein that contains eight LRR (leucine-rich) repeasts and one LRRCT domain. LRRC23 exists as two alternatively spliced isoforms and is encoded by a gene mapping to chromosome 12.

Supplier: Bioss

The adenovirus E1B protein is a viral homolog of the Bcl-2 family of proteins that are involved in regulating cell death. A family of interacting proteins, which are designated Nip or Bnip and include BNIP-1, BNIP-2, BNIP-3 and Nix, associate with both the E1B protein and Bcl-2 proteins to mediate apoptotic signaling. BNIP-1 contains a hydrophobic transmembrane domain, which enables its localization to the nuclear envelope, endoplasmic recticulum and mitochondria. BNIP-2, (previously designated Nip2 and Nip21 in human and mouse respectively), shares homology with the non-catalytic domain of Cdc42 GTPase-activating protein (Cdc42GAP). Through binding to Cdc42GAP, BNIP-2 enhances the GTPase activity of Cdc42GAP, facilitating the hydrolysis of GTP bound to Cdc42 and thereby, mediating the signaling pathways involving receptor kinases, small GTPases and apoptotic proteins. Nix, which is also designated Nip3L or Bnip3L, is highly related to BNIP-3, and both proteins localize to the mitochondria where they associate with Bcl-2 proteins. BNIP-3 preferentially binds to Bcl-xL and induces apoptosis by suppressing the anti-apoptosis activity of Bcl-xL.

Supplier: Bioss

The adenovirus E1B protein is a viral homolog of the Bcl-2 family of proteins that are involved in regulating cell death. A family of interacting proteins, which are designated Nip or Bnip and include BNIP-1, BNIP-2, BNIP-3 and Nix, associate with both the E1B protein and Bcl-2 proteins to mediate apoptotic signaling. BNIP-1 contains a hydrophobic transmembrane domain, which enables its localization to the nuclear envelope, endoplasmic recticulum and mitochondria. BNIP-2, (previously designated Nip2 and Nip21 in human and mouse respectively), shares homology with the non-catalytic domain of Cdc42 GTPase-activating protein (Cdc42GAP). Through binding to Cdc42GAP, BNIP-2 enhances the GTPase activity of Cdc42GAP, facilitating the hydrolysis of GTP bound to Cdc42 and thereby, mediating the signaling pathways involving receptor kinases, small GTPases and apoptotic proteins. Nix, which is also designated Nip3L or Bnip3L, is highly related to BNIP-3, and both proteins localize to the mitochondria where they associate with Bcl-2 proteins. BNIP-3 preferentially binds to Bcl-xL and induces apoptosis by suppressing the anti-apoptosis activity of Bcl-xL.

Supplier: Bioss

The adenovirus E1B protein is a viral homolog of the Bcl-2 family of proteins that are involved in regulating cell death. A family of interacting proteins, which are designated Nip or Bnip and include BNIP-1, BNIP-2, BNIP-3 and Nix, associate with both the E1B protein and Bcl-2 proteins to mediate apoptotic signaling. BNIP-1 contains a hydrophobic transmembrane domain, which enables its localization to the nuclear envelope, endoplasmic recticulum and mitochondria. BNIP-2, (previously designated Nip2 and Nip21 in human and mouse respectively), shares homology with the non-catalytic domain of Cdc42 GTPase-activating protein (Cdc42GAP). Through binding to Cdc42GAP, BNIP-2 enhances the GTPase activity of Cdc42GAP, facilitating the hydrolysis of GTP bound to Cdc42 and thereby, mediating the signaling pathways involving receptor kinases, small GTPases and apoptotic proteins. Nix, which is also designated Nip3L or Bnip3L, is highly related to BNIP-3, and both proteins localize to the mitochondria where they associate with Bcl-2 proteins. BNIP-3 preferentially binds to Bcl-xL and induces apoptosis by suppressing the anti-apoptosis activity of Bcl-xL.

Supplier: Bioss

The adenovirus E1B protein is a viral homolog of the Bcl-2 family of proteins that are involved in regulating cell death. A family of interacting proteins, which are designated Nip or Bnip and include BNIP-1, BNIP-2, BNIP-3 and Nix, associate with both the E1B protein and Bcl-2 proteins to mediate apoptotic signaling. BNIP-1 contains a hydrophobic transmembrane domain, which enables its localization to the nuclear envelope, endoplasmic recticulum and mitochondria. BNIP-2, (previously designated Nip2 and Nip21 in human and mouse respectively), shares homology with the non-catalytic domain of Cdc42 GTPase-activating protein (Cdc42GAP). Through binding to Cdc42GAP, BNIP-2 enhances the GTPase activity of Cdc42GAP, facilitating the hydrolysis of GTP bound to Cdc42 and thereby, mediating the signaling pathways involving receptor kinases, small GTPases and apoptotic proteins. Nix, which is also designated Nip3L or Bnip3L, is highly related to BNIP-3, and both proteins localize to the mitochondria where they associate with Bcl-2 proteins. BNIP-3 preferentially binds to Bcl-xL and induces apoptosis by suppressing the anti-apoptosis activity of Bcl-xL.

Supplier: Bioss

The leucine-rich (LRR) repeat is a 20-30 amino acid motif that forms a hydrophobic å/∫ horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. The primary function of these motifs is to provide a versatile structural framework to mediate the formation of protein-protein interactions. LRRs are present in a variety of proteins with diverse structure and function, including innate immunity and nervous system development. Several human diseases are associated with mutations in genes encoding LRR-containing proteins. LRRC23 (leucine-rich repeat-containing protein 23), also known as leucine-rich protein B7, is a 343 amino acid protein that contains eight LRR (leucine-rich) repeasts and one LRRCT domain. LRRC23 exists as two alternatively spliced isoforms and is encoded by a gene mapping to chromosome 12.

Supplier: Adipogen

Activation of cells by LPS is mediated by the Toll-like receptor 4 (TLR4). For optimal interaction with LPS, TLR4 requires association with myeloid differentiation protein 2 (MD-2). According to current consensus activation of TLR4 is preceded by the transfer of LPS to membrane-bound (m) or soluble (s) CD14 by LPS-binding protein (LBP). Re-form LPS and lipid A, but not S-form LPS, are capable of inducing TNF-alpha responses also in the absence of CD14. LPS, synthesized by most wild-type (WT) Gram-negative bacteria (S-form LPS), consists of three regions, the O-polysaccharide chain, which is made up of repeating oligosaccharide units, the core oligosaccharide and the lipid A, which harbors the endotoxic activity of the entire molecule. R-form LPS synthesized by the so-called rough (R) mutants of Gram-negative bacteria lacks the O-specific chain. Furthermore, the core-oligosaccharide may be present in different degrees of completion, depending on the class (Ra to Re) to which the mutant belongs. LPS are amphipathic molecules whose hydrophobicity decreases with increasing length of the sugar part. Based upon these differences, S- and R-form LPS show marked differences in the kinetics of their blood clearance and cellular uptake as well as in the ability to induce oxidative burst in human granulocytes and to activate the host complement system.

Supplier: Adipogen

Activation of cells by LPS is mediated by the Toll-like receptor 4 (TLR4). For optimal interaction with LPS, TLR4 requires association with myeloid differentiation protein 2 (MD-2). According to current consensus activation of TLR4 is preceded by the transfer of LPS to membrane-bound (m) or soluble (s) CD14 by LPS-binding protein (LBP). Re-form LPS and lipid A, but not S-form LPS, are capable of inducing TNF-alpha responses also in the absence of CD14. LPS, synthesized by most wild-type (WT) Gram-negative bacteria (S-form LPS), consists of three regions, the O-polysaccharide chain, which is made up of repeating oligosaccharide units, the core oligosaccharide and the lipid A, which harbors the endotoxic activity of the entire molecule. R-form LPS synthesized by the so-called rough (R) mutants of Gram-negative bacteria lacks the O-specific chain. Furthermore, the core-oligosaccharide may be present in different degrees of completion, depending on the class (Ra to Re) to which the mutant belongs. LPS are amphipathic molecules whose hydrophobicity decreases with increasing length of the sugar part. Based upon these differences, S- and R-form LPS show marked differences in the kinetics of their blood clearance and cellular uptake as well as in the ability to induce oxidative burst in human granulocytes and to activate the host complement system.

Supplier: Genetex

The protein encoded by this gene is a member of the fibroblast growth factor receptor (FGFR) family, where amino acid sequence is highly conserved between members and throughout evolution. FGFR family members differ from one another in their ligand affinities and tissue distribution. A full-length representative protein consists of an extracellular region, composed of three immunoglobulin-like domains, a single hydrophobic membrane-spanning segment and a cytoplasmic tyrosine kinase domain. The extracellular portion of the protein interacts with fibroblast growth factors, setting in motion a cascade of downstream signals, ultimately influencing mitogenesis and differentiation. This particular family member binds both acidic and basic fibroblast growth factors and is involved in limb induction. Mutations in this gene have been associated with Pfeiffer syndrome, Jackson-Weiss syndrome, Antley-Bixler syndrome, osteoglophonic dysplasia, and autosomal dominant Kallmann syndrome 2. Chromosomal aberrations involving this gene are associated with stem cell myeloproliferative disorder and stem cell leukemia lymphoma syndrome. Alternatively spliced variants which encode different protein isoforms have been described; however, not all variants have been fully characterized. [provided by RefSeq]

Supplier: Adipogen

Activation of cells by LPS is mediated by the Toll-like receptor 4 (TLR4). For optimal interaction with LPS, TLR4 requires association with myeloid differentiation protein 2 (MD-2). According to current consensus activation of TLR4 is preceded by the transfer of LPS to membrane-bound (m) or soluble (s) CD14 by LPS-binding protein (LBP). Re-form LPS and lipid A, but not S-form LPS, are capable of inducing TNF-alpha responses also in the absence of CD14. LPS, synthesized by most wild-type (WT) Gram-negative bacteria (S-form LPS), consists of three regions, the O-polysaccharide chain, which is made up of repeating oligosaccharide units, the core oligosaccharide and the lipid A, which harbors the endotoxic activity of the entire molecule. R-form LPS synthesized by the so-called rough (R) mutants of Gram-negative bacteria lacks the O-specific chain. Furthermore, the core-oligosaccharide may be present in different degrees of completion, depending on the class (Ra to Re) to which the mutant belongs. LPS are amphipathic molecules whose hydrophobicity decreases with increasing length of the sugar part. Based upon these differences, S- and R-form LPS show marked differences in the kinetics of their blood clearance and cellular uptake as well as in the ability to induce oxidative burst in human granulocytes and to activate the host complement system.

Supplier: Adipogen

Activation of cells by LPS is mediated by the Toll-like receptor 4 (TLR4). For optimal interaction with LPS, TLR4 requires association with myeloid differentiation protein 2 (MD-2). According to current consensus activation of TLR4 is preceded by the transfer of LPS to membrane-bound (m) or soluble (s) CD14 by LPS-binding protein (LBP). Re-form LPS and lipid A, but not S-form LPS, are capable of inducing TNF-alpha responses also in the absence of CD14. LPS, synthesized by most wild-type (WT) Gram-negative bacteria (S-form LPS), consists of three regions, the O-polysaccharide chain, which is made up of repeating oligosaccharide units, the core oligosaccharide and the lipid A, which harbors the endotoxic activity of the entire molecule. R-form LPS synthesized by the so-called rough (R) mutants of Gram-negative bacteria lacks the O-specific chain. Furthermore, the core-oligosaccharide may be present in different degrees of completion, depending on the class (Ra to Re) to which the mutant belongs. LPS are amphipathic molecules whose hydrophobicity decreases with increasing length of the sugar part. Based upon these differences, S- and R-form LPS show marked differences in the kinetics of their blood clearance and cellular uptake as well as in the ability to induce oxidative burst in human granulocytes and to activate the host complement system.

Supplier: Adipogen

Activation of cells by LPS is mediated by the Toll-like receptor 4 (TLR4). For optimal interaction with LPS, TLR4 requires association with myeloid differentiation protein 2 (MD-2). According to current consensus activation of TLR4 is preceded by the transfer of LPS to membrane-bound (m) or soluble (s) CD14 by LPS-binding protein (LBP). Re-form LPS and lipid A, but not S-form LPS, are capable of inducing TNF-alpha responses also in the absence of CD14. LPS, synthesized by most wild-type (WT) Gram-negative bacteria (S-form LPS), consists of three regions, the O-polysaccharide chain, which is made up of repeating oligosaccharide units, the core oligosaccharide and the lipid A, which harbors the endotoxic activity of the entire molecule. R-form LPS synthesized by the so-called rough (R) mutants of Gram-negative bacteria lacks the O-specific chain. Furthermore, the core-oligosaccharide may be present in different degrees of completion, depending on the class (Ra to Re) to which the mutant belongs. LPS are amphipathic molecules whose hydrophobicity decreases with increasing length of the sugar part. Based upon these differences, S- and R-form LPS show marked differences in the kinetics of their blood clearance and cellular uptake as well as in the ability to induce oxidative burst in human granulocytes and to activate the host complement system.

Supplier: Adipogen

Activation of cells by LPS is mediated by the Toll-like receptor 4 (TLR4). For optimal interaction with LPS, TLR4 requires association with myeloid differentiation protein 2 (MD-2). According to current consensus activation of TLR4 is preceded by the transfer of LPS to membrane-bound (m) or soluble (s) CD14 by LPS-binding protein (LBP). Re-form LPS and lipid A, but not S-form LPS, are capable of inducing TNF-alpha responses also in the absence of CD14. LPS, synthesized by most wild-type (WT) Gram-negative bacteria (S-form LPS), consists of three regions, the O-polysaccharide chain, which is made up of repeating oligosaccharide units, the core oligosaccharide and the lipid A, which harbors the endotoxic activity of the entire molecule. R-form LPS synthesized by the so-called rough (R) mutants of Gram-negative bacteria lacks the O-specific chain. Furthermore, the core-oligosaccharide may be present in different degrees of completion, depending on the class (Ra to Re) to which the mutant belongs. LPS are amphipathic molecules whose hydrophobicity decreases with increasing length of the sugar part. Based upon these differences, S- and R-form LPS show marked differences in the kinetics of their blood clearance and cellular uptake as well as in the ability to induce oxidative burst in human granulocytes and to activate the host complement system.