277 Results for: "hydrophobic interaction"

Supplier: Prosci

The protein encoded by this gene is an unusual orphan receptor that contains a putative ligand-binding domain but lacks a conventional DNA-binding domain. The gene product is a member of the nuclear hormone receptor family, a group of transcription factors regulated by small hydrophobic hormones, a subset of which do not have known ligands and are referred to as orphan nuclear receptors. The protein has been shown to interact with retinoid and thyroid hormone receptors, inhibiting their ligand-dependent transcriptional activation. In addition, interaction with estrogen receptors has been demonstrated, leading to inhibition of function. Studies suggest that the protein represses nuclear hormone receptor-mediated transactivation via two separate steps: competition with coactivators and the direct effects of its transcriptional repressor function.

Supplier: Prosci

Leukocyte antigen CD37 (CD37) is also known as Tetraspanin-26 (Tspan-26) and TSPAN26,which is a member of the transmembrane 4 superfamily or tetraspanin family. Most of these members are cell-surface proteins that are characterized by the presence of four hydrophobic domains. The proteins encoded by CD37 gene mediate signal transduction events that play a role in the regulation of cell development, activation, growth and motility. CD37 is a cell surface glycoprotein that is known to complex with integrins and other transmembrane 4 superfamily proteins. CD37 may play a role in T-cell-B-cell interactions.

Supplier: Genetex

Influenza A and B are the two types of influenza viruses that cause epidemic human disease. Influenza type C infections cause a mild respiratory illness and are not thought to cause epidemics. Influenza A viruses are further categorized into subtypes on the basis of two surface antigens: hemagglutinin (H) and neuraminidase (N). Strains are also described by geographic origin, strain number and year of isolation. This protein forms a continuous shell on the inner side of the lipid bilayer. Maintains the structural integrity of the virus particle through hydrophobic interactions. Also mediates the encapsidation of RNA nucleoprotein cores into the membrane envelope.

Supplier: Genetex

Influenza A and B are the two types of influenza viruses that cause epidemic human disease. Influenza type C infections cause a mild respiratory illness and are not thought to cause epidemics. Influenza A viruses are further categorized into subtypes on the basis of two surface antigens: hemagglutinin (H) and neuraminidase (N). Strains are also described by geographic origin, strain number and year of isolation. This protein forms a continuous shell on the inner side of the lipid bilayer. Maintains the structural integrity of the virus particle through hydrophobic interactions. Also mediates the encapsidation of RNA nucleoprotein cores into the membrane envelope.

Supplier: Genetex

Influenza A and B are the two types of influenza viruses that cause epidemic human disease. Influenza type C infections cause a mild respiratory illness and are not thought to cause epidemics. Influenza A viruses are further categorized into subtypes on the basis of two surface antigens: hemagglutinin (H) and neuraminidase (N). Strains are also described by geographic origin, strain number and year of isolation.This protein forms a continuous shell on the inner side of the lipid bilayer. Maintains the structural integrity of the virus particle through hydrophobic interactions. Also mediates the encapsidation of RNA nucleoprotein cores into the membrane envelope.

Supplier: Proteintech

The cell-surface molecule CD9, a member of the transmembrane-4 superfamily, interacts with the integrin family and other membrane proteins, and is postulated to participate in cell migration and adhesion. Expression of CD9 enhances membrane fusion between muscle cells and promotes viral infection in some cells . It is often used as a mesenchymal stem cell marker . CD9 is also known as the p24 antigen besides MIC3, TSPAN29 because it is a protein of molecular weight 24 kD. The CD9 antigen appears to be a 227-amino acid molecule with 4 hydrophobic domains and 1 N-glycosylation site.

Supplier: Proteintech

The cell-surface molecule CD9, a member of the transmembrane-4 superfamily, interacts with the integrin family and other membrane proteins, and is postulated to participate in cell migration and adhesion. Expression of CD9 enhances membrane fusion between muscle cells and promotes viral infection in some cells . It is often used as a mesenchymal stem cell marker . CD9 is also known as the p24 antigen besides MIC3, TSPAN29 because it is a protein of molecular weight 24 kD. The CD9 antigen appears to be a 227-amino acid molecule with 4 hydrophobic domains and 1 N-glycosylation site.

Supplier: Prosci

The protein encoded by this gene is a member of the transmembrane 4 superfamily, also known as the tetraspanin family. Most of these members are cell-surface proteins that are characterized by the presence of four hydrophobic domains. The proteins mediate signal transduction events that play a role in the regulation of cell development, activation, growth and motility. This encoded protein is a cell surface glycoprotein that is known to complex with integrins and other transmembrane 4 superfamily proteins. It may play a role in T-cell-B-cell interactions. Alternate splicing results in multiple transcript variants encoding different isoforms.

Supplier: Bioss

FGFRL1 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 would consist 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. A marked difference between FGFRL1 and the other family members is its lack of a cytoplasmic tyrosine kinase domain. The result is a transmembrane receptor that could interact with other family members and potentially inhibit signaling. Multiple alternatively spliced transcript variants encoding the same isoform have been found.

Supplier: Bioss

FGFRL1 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 would consist 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. A marked difference between FGFRL1 and the other family members is its lack of a cytoplasmic tyrosine kinase domain. The result is a transmembrane receptor that could interact with other family members and potentially inhibit signaling. Multiple alternatively spliced transcript variants encoding the same isoform have been found.

Supplier: Bioss

FGFRL1 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 would consist 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. A marked difference between FGFRL1 and the other family members is its lack of a cytoplasmic tyrosine kinase domain. The result is a transmembrane receptor that could interact with other family members and potentially inhibit signaling. Multiple alternatively spliced transcript variants encoding the same isoform have been found.

Supplier: Rockland Immunochemical

Uroplakin-1B (UPK1B) is a member of the transmembrane 4 superfamily, also known as the tetraspanin family. Most of these members are cell-surface proteins that are characterized by the presence of four hydrophobic domains. The proteins mediate signal transduction events that play a role in the regulation of cell development, activation, growth and motility. UPK1B is found in the asymmetrical unit membrane (AUM) where it can form a complex with other transmembrane 4 superfamily proteins and may play a role in normal bladder epithelial physiology, possibly in regulating membrane permeability of superficial umbrella cells or in stabilizing the apical membrane through AUM/cytoskeletal interactions.

Supplier: Bioss

FGFRL1 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 would consist 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. A marked difference between FGFRL1 and the other family members is its lack of a cytoplasmic tyrosine kinase domain. The result is a transmembrane receptor that could interact with other family members and potentially inhibit signaling. Multiple alternatively spliced transcript variants encoding the same isoform have been found.

Supplier: Bioss

FGFRL1 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 would consist 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. A marked difference between FGFRL1 and the other family members is its lack of a cytoplasmic tyrosine kinase domain. The result is a transmembrane receptor that could interact with other family members and potentially inhibit signaling. Multiple alternatively spliced transcript variants encoding the same isoform have been found.

Supplier: Bioss

FGFRL1 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 would consist 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. A marked difference between FGFRL1 and the other family members is its lack of a cytoplasmic tyrosine kinase domain. The result is a transmembrane receptor that could interact with other family members and potentially inhibit signaling. Multiple alternatively spliced transcript variants encoding the same isoform have been found.

Supplier: Prosci

The protein encoded by this gene is a member of the fibroblast growth factor receptor 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.

Supplier: Prosci

UPK1B Antibody: Uroplakin-1B (UPK1B) is a member of the transmembrane 4 superfamily, also known as the tetraspanin family. Most of these members are cell-surface proteins that are characterized by the presence of four hydrophobic domains. The proteins mediate signal transduction events that play a role in the regulation of cell development, activation, growth and motility. UPK1B is found in the asymmetrical unit membrane (AUM) where it can form a complex with other transmembrane 4 superfamily proteins and may play a role in normal bladder epithelial physiology, possibly in regulating membrane permeability of superficial umbrella cells or in stabilizing the apical membrane through AUM/cytoskeletal interactions.

Supplier: Bioss

FGFRL1 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 would consist 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. A marked difference between FGFRL1 and the other family members is its lack of a cytoplasmic tyrosine kinase domain. The result is a transmembrane receptor that could interact with other family members and potentially inhibit signaling. Multiple alternatively spliced transcript variants encoding the same isoform have been found.

Supplier: Bioss

FGFRL1 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 would consist 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. A marked difference between FGFRL1 and the other family members is its lack of a cytoplasmic tyrosine kinase domain. The result is a transmembrane receptor that could interact with other family members and potentially inhibit signaling. Multiple alternatively spliced transcript variants encoding the same isoform have been found.

Supplier: Bioss

FGFRL1 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 would consist 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. A marked difference between FGFRL1 and the other family members is its lack of a cytoplasmic tyrosine kinase domain. The result is a transmembrane receptor that could interact with other family members and potentially inhibit signaling. Multiple alternatively spliced transcript variants encoding the same isoform have been found.

Supplier: Prosci

UPK1B Antibody: Uroplakin-1B (UPK1B) is a member of the transmembrane 4 superfamily, also known as the tetraspanin family. Most of these members are cell-surface proteins that are characterized by the presence of four hydrophobic domains. The proteins mediate signal transduction events that play a role in the regulation of cell development, activation, growth and motility. UPK1B is found in the asymmetrical unit membrane (AUM) where it can form a complex with other transmembrane 4 superfamily proteins and may play a role in normal bladder epithelial physiology, possibly in regulating membrane permeability of superficial umbrella cells or in stabilizing the apical membrane through AUM/cytoskeletal interactions.

Supplier: Prosci

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 would consist 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. A marked difference between this gene product and the other family members is its lack of a cytoplasmic tyrosine kinase domain. The result is a transmembrane receptor that could interact with other family members and potentially inhibit signaling. Multiple alternatively spliced transcript variants encoding the same isoform have been found for this gene.

Supplier: Prosci

CD64, also known as Fc-gamma receptor 1 (Fc gamma RI), is a type of integral membrane glycoprotein that binds monomeric IgG-type antibodies with high affinity. After binding IgG, CD64 interacts with an accessory chain known as the common gamma chain ( gamma chain), which possesses an ITAM motif that is necessary for triggering cellular activation. CD64 is composed of a signal peptide, three extracellular immunoglobulin domains of the C2-type used to bind antibody, a hydrophobic transmembrane domain, and a short cytoplasmic tail. CD64 mediates endocytosis, phagocytosis, antibody-dependent cellular cytotoxicity, cytokine release, and superoxide production. It is normally expressed on the surfaces of monocytes and macrophages.

Supplier: Bioss

Tetraspanins are a group of hydrophobic membrane proteins that interact with a wide variety of proteins including intracellular signaling molecules, integrins and membrane receptors. TSPAN7 (tetraspanin 7), also known as MXS1 (membrane component chromosome X surface marker 1) or TM4SF2 (transmembrane 4 superfamily member 2), is a 249 amino acid multi-pass membrane protein belonging to the tetraspanin (TM4SF) family of transmembrane proteins. TSPAN7 is believed to play a role in cell motility and cell proliferation. The gene that encodes TSPAN7 maps to human chromosome X and defects in this gene are a cause of mental retardation X-linked type 58 (MRX58), which is characterized by dramatically below average general intellectual functioning.

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: Adipogen

Non-toxic, pH-sensitive fluorescent dye (blue-green range) for live imaging of pH alteration in acidic organelles, vesicles, cells, tissue and even small whole animals over several days without side effects. Stronger fluorescent intensity under acidic conditions and barely detectable in alkaline solutions (wide range from pH 4 to pH 8). Highly cell/membrane permeable. Trapped within the cells and acidic organelles through hydrophobic interactions with the inner side of the membranes. Barely metabolized and long-term stable, thus slow photobleaching. Angiogenesis inhibitor. Inhibitor of matrix metalloproteinases MMP-1,-2,-8,-9,-12,-13. TYK2, DYRK2,Dyrk1A, YSK4 and RPS6KA1/2 inhibitor.

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: Anaspec

This is a heptapeptide from the N-terminal prion-determining domain of the yeast protein Sup35 that forms amyloid fibrils. The availability of its detailed atomic oligomeric structure makes it a good model for studying the early stage of aggregation. The GNNQQNY dimer forms three stable sheet structures. in-register parallel, off-register parallel, and anti-parallel. The in-register parallel dimer, which is close to the amyloid beta-sheet structure, has few interpeptide hydrogen bonds, making hydrophobic interactions more important and increasing the conformational entropy compared to the anti-parallel sheet.
Sequence: GNNQQNY
Molecular Weight: 836.8 Da
% Peak Area by HPLC: ≥95
Peptide Content: ≥ 60%
Storage condition: -20°C

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

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.