105498 Results for: "MARKET SOURCE PART PROCESS"

Supplier: QIAGEN

FTA® Elute Cards utilise Whatman FTA® technology that simplifies the handling and processing of nucleic acids. DNA is eluted in an easy step, providing DNA in solution ready for amplification.

Supplier: HONEYWELL SAFETY

These gloves, made of a stainless steel chainmail with detachable plastic straps, provide protection against cuts, a common hazard in meat, fish and processing industries. The gloves are also suitable for use in metal industries.

Supplier: Merck

These PTFE white hydrophilic membrane compatible with all commonly used HPLC solvents. The membrane undergoes a special treatment process to remove any residual extractables, to provide clearer analysis results. They are widely used for HPLC mobile phase filtration, clarifying acids, bases and dilute protein solutions and isolation of RNA.

Supplier: Bioss

HPR is a ubiquitous transcription factor required for a diverse set of processes. It is a component of the CCR4 complex involved in the control of gene expression.

Supplier: Bioss

HPR is a ubiquitous transcription factor required for a diverse set of processes. It is a component of the CCR4 complex involved in the control of gene expression.

Supplier: Bioss

HERC1 is a stimulates guanine nucleotide exchange on ARF1 and Rab proteins. This protein may be involved in membrane transport processes.

Supplier: Bioss

Angiotensin I converting Enzyme Inhibitor, ACEI also designated Bradykinin-potentiating peptide. The peptide: PTHIKWGD. Processed active peptide.

Supplier: Bioss

Angiotensin I converting Enzyme Inhibitor, ACEI also designated Bradykinin-potentiating peptide. The peptide: PTHIKWGD. Processed active peptide.

Supplier: Bioss

Matrix metalloproteinase 26 preprotein; gelatinase A; 70kD type IV collagenase; gelatinase neutrophil. Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes as well as in disease processes. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP26 degrades type IV collagen, the major structural component of basement membranes. The enzyme plays a role in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response.Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodelling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP26, also known as Matrilysin 2, was first cloned from human fetal cells, and identified as an MMP most closely related to MMP7 (Matrilysin 1). The homology between MMP7 and MMP26 is low (only 38% identical), thus the functions are unlikely to be similar. Homology is much higher (48% identical) for the comparable region of MMP12, but MMP26 appears to have broader substrate specificity than does MMP12. MMP26, like MMP7, lacks the hemopexin domain common to the other MMPs, but contains a Propeptide domain, cysteine switch activation site, followed by a catalytic domain, and a short vestige of the hinge region. MMP26 is apparently not glycosylated, and is a secreted MMP. Tissue analysis shows MMP26 most strongly in placenta and uterus, but also in kidney cells, lung cells, lymphocytes and lung or endometrial carcinoma cells. MMP26 is proteolytically active, cleaving casein in zymograms, and gelatin, a1PI, fibrinogen, fibronectin, vitronectin, type IV collagen, and apparently activating MMP9.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

Matrix metalloproteinase 26 preprotein; gelatinase A; 70kD type IV collagenase; gelatinase neutrophil. Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes as well as in disease processes. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP26 degrades type IV collagen, the major structural component of basement membranes. The enzyme plays a role in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response.Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodelling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP26, also known as Matrilysin 2, was first cloned from human fetal cells, and identified as an MMP most closely related to MMP7 (Matrilysin 1). The homology between MMP7 and MMP26 is low (only 38% identical), thus the functions are unlikely to be similar. Homology is much higher (48% identical) for the comparable region of MMP12, but MMP26 appears to have broader substrate specificity than does MMP12. MMP26, like MMP7, lacks the hemopexin domain common to the other MMPs, but contains a Propeptide domain, cysteine switch activation site, followed by a catalytic domain, and a short vestige of the hinge region. MMP26 is apparently not glycosylated, and is a secreted MMP. Tissue analysis shows MMP26 most strongly in placenta and uterus, but also in kidney cells, lung cells, lymphocytes and lung or endometrial carcinoma cells. MMP26 is proteolytically active, cleaving casein in zymograms, and gelatin, a1PI, fibrinogen, fibronectin, vitronectin, type IV collagen, and apparently activating MMP9.

Supplier: ProSci Inc.

The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. PSMB2 is a member of the proteasome B-type family, also known as the T1B family, that is a 20S core beta subunit.The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the proteasome B-type family, also known as the T1B family, that is a 20S core beta subunit. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Supplier: ProSci Inc.

HSPB1, like the other heat shock proteins, is part of a complex system of molecular chaperones in epidermal keratinocytes.

Supplier: ProSci Inc.

Part of the d4 family of zinc finger proteins, DPF1 has been localized on chromosome 19.

Supplier: Bioss

Phosphatase enzymes catalyse hydrolysis of phosphoric acid esters of various alcohols, e.g. a hexose phosphate, to yield the alcohol and free inorganic phosphate. This may be a way of recycling phosphate in the cell, and the level of phosphate may be elevated under conditions of phosphate starvation (in algae for example). Acid phosphatases have pH optima below 7, whereas alkaline phosphatases are most active above pH 7. Commercial quantities of acid phosphatase are obtained from plant sources e.g. potato and wheat germ, whereas similar quantities of alkaline phosphatase are obtained from animal intestine and bacteria.

Supplier: Bioss

Cytochrome P450 4A22 (CYP4A22) is a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This gene is part of a cluster of cytochrome P450 genes on chromosome 1p33.

Supplier: Bioss

Cytochrome P450 4A22 (CYP4A22) is a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This gene is part of a cluster of cytochrome P450 genes on chromosome 1p33.

Supplier: Bioss

Cytochrome P450 4A22 (CYP4A22) is a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This gene is part of a cluster of cytochrome P450 genes on chromosome 1p33.

Supplier: Bioss

Cytochrome P450 4A22 (CYP4A22) is a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This gene is part of a cluster of cytochrome P450 genes on chromosome 1p33.

Supplier: Bioss

Cytochrome P450 4A22 (CYP4A22) is a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyse many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This gene is part of a cluster of cytochrome P450 genes on chromosome 1p33.

Supplier: Bioss

Binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. Acts as a cytokine involved in enhancing production of interferon-gamma and interleukin-12 and reducing production of interleukin-1 and is essential in the pathway that leads to type I immunity.

Supplier: Bioss

Binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. Acts as a cytokine involved in enhancing production of interferon-gamma and interleukin-12 and reducing production of interleukin-1 and is essential in the pathway that leads to type I immunity.

Supplier: Bioss

Part of the host defense system of polymorphonuclear leukocytes. It is responsible for microbicidal activity against a wide range of organisms. In the stimulated PMN, MPO catalyzes the production of hypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediates that greatly enhance PMN microbicidal activity.

Supplier: Bioss

CDCA3 (Cell division cycle associated 3) is an F-box-like protein which is required for entry into mitosis. It is associated with SKP1 as part of a SCF (SKP1-cullin-F-box) protein ligase complex, and is required for the ubiquitination and degradation of the CDK1 inhibitory tyrosine kinase WEE1 at G2/M phase.

Supplier: Bioss

CDCA3 (Cell division cycle associated 3) is an F-box-like protein which is required for entry into mitosis. It is associated with SKP1 as part of a SCF (SKP1-cullin-F-box) protein ligase complex, and is required for the ubiquitination and degradation of the CDK1 inhibitory tyrosine kinase WEE1 at G2/M phase.

Supplier: Bioss

CDCA3 (Cell division cycle associated 3) is an F-box-like protein which is required for entry into mitosis. It is associated with SKP1 as part of a SCF (SKP1-cullin-F-box) protein ligase complex, and is required for the ubiquitination and degradation of the CDK1 inhibitory tyrosine kinase WEE1 at G2/M phase.

Supplier: Bioss

Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. M-cadherin is part of the myogenic program and may provide a trigger for terminal muscle differentiation.

Supplier: Bioss

Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin.

Supplier: IKA

Modular laboratory reactor for the optimisation and reproduction of various chemical reactions, mixing and homogenisation processes on a lab scale. The system is characterised by the agitator mounting, which allows a safe transfer of the higher motor torque.