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Update to Avantor’s response to the coronavirus (COVID-19) pandemic

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3-Methyl-4-(methylamino)phenol


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Catalog Number: (10750-062)

Supplier:  Prosci
Description:   Cathelicidin Antibody: One component of host defense at mucosal surfaces is epithelial-derived antimicrobial peptides. Cathelicidins are one family of antimicrobial peptides characterized by conserved pro-peptide sequences that have been identified in epithelial tissues and some myeloid cells of humans and animals. LL-37/hCAP-18 is the only Cathelicidin found in humans and is expressed in inflammatory and epithelial cells. The presence of these molecules is essential for defense against invasive bacterial infection in skin. Besides their direct antimicrobial function, Cathelicidins have multiple roles in mediating innate and adaptive immunity, such as endotoxin neutralizing, angiogenesis, wound healing and promoting neutrophil chemotaxis and mast cell recruitment. Finally, Cathelicidin antimicrobial peptides qualify as prototypes of innovative drugs that may be used to treat infection and/or modulate the immune response.
Catalog Number: (10750-844)

Supplier:  Prosci
Description:   DCLK1 Antibody: DCLK1 is one of three doublecortin-like kinases similar to the Ca2+/calmodulin-dependent protein kinase (CaMK) family. DCLK1 mRNA, like that of the homologous DCLK2 and DCLK3, is highly expressed in adult brain, but only DCLK1 and DCLK2 transcripts are present in human fetal brain and the developing mouse embryo, suggesting that DCLK1 and DCLK2 may play roles in cortical development. The DCLK proteins are homologous to Doublecortin (DCX), a gene that is mutated in X-linked human lissencephaly. In mouse models where the DCX gene has been disrupted, DCLK1 expression increases slightly and appears to compensate for the loss of DCX, as mice mutant for both DCX and DCLK1 show a severe phenotype including perinatal lethality, disorganized neocortical layering, and profound hippocampal cytoarchitectural disorganization. Unlike DCLK1, DCLK2 expression does not change in DCX-null mice.
Catalog Number: (10750-918)

Supplier:  Prosci
Description:   APC4 Antibody: Cell cycle regulated protein ubiquitination and degradation within subcellular domains is thought to be essential for the normal progression of mitosis. APC4 is a highly conserved component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. APC/C is responsible for degrading anaphase inhibitors, mitotic cyclins, and spindle-associated proteins ensuring that events of mitosis take place in proper sequence. The individual APC/C components mRNA and protein levels are expressed at approximately the same levels in most tissues and cell lines, suggesting that they perform their functions as part of a complex. While little is known of APC4, it is thought that APC4 associates with other APC/C components APC1, APC5, and CDC23 interdependently, such that loss of any one subunit reduces binding between the remaining three.
Catalog Number: (10751-362)

Supplier:  Prosci
Description:   TMEM88 Antibody: Transmembrane protein 88 (TMEM88) is a two-transmembrane-type protein whose C-terminal tail has been shown to bind the PDZ domain of Dishevelled (Dvl), one of the key components in Wnt signaling pathways. TMEM88 attentuated the Wnt/beta-catenin signaling induced by Wnt-1 ligand in a dose-dependent manner and knockdown of TMEM88 by RNAi increased Wnt activity, suggesting that TMEM88 plays a role in regulating Wnt signaling in a context-dependent manner.
Catalog Number: (10062-016)

Supplier:  Prosci
Description:   The amphoterin-induced gene and ORF (AMIGO1) protein is a brain-enriched, glycosylated transmembrane immunoglobulin (Ig) superfamily protein with six extracellular leucine-rich repeats (LRRs) and one Ig-like domain. It and the related proteins AMIGO2 and AMIGO3 are thought to be cell adhesion molecules expressed on fiber tracts of neuronal tissues and participate in their formation. AMIGO1 has also been suggested to play important roles in dendritic outgrowth during development and could modulate the survival of developing and adult neurons.
Catalog Number: (10749-690)

Supplier:  Prosci
Description:   SARS Matrix Antibody: A novel coronavirus has recently been identified as the causative agent of SARS (Severe Acute Respiratory Syndrome). Coronaviruses are a major cause of upper respiratory diseases in humans. The genomes of these viruses are positive-stranded RNA approximately 27-31kb in length. The M protein (Membrane protein, Matrix protein) is one of the major structural viral proteins. It is an integral membrane protein involved in the budding of the viral particles and interacts with S (Spike) protein and the nucleocapsid protein.
Catalog Number: (10061-990)

Supplier:  Prosci
Description:   IL-1RL2 is a member of the interleukin 1 receptor family, but it is incapable of binding to interleukin 1 alpha and interleukin 1 beta with high affinity. Together with IL-1RAcP, it can bind members of the IL-36 cytokine family, leading to activation of the NF-kappaB pathway. IL-1RL2 can also bind to IL-1F10, resulting in a decreased product of Th17 cytokines in response to immunological or LPS challenge, suggesting that one potential role of IL-1RL2 may be to modulate the immune and inflammation response.
Catalog Number: (10752-052)

Supplier:  Prosci
Description:   CD160, also known as BY55, is a lipid-anchored cell membrane glycoprotein that contains one immunoglobulin-like domain. It is expressed in small intestine, spleen and functional NK and T cytotoxic lymphocytes. CD160 exists as a disulfide-linked homomultimer that functions as a receptor for MHC (major histocompatability complex) molecules and is thought to regulate the function of NK cells. Additionally, CD160 interacts with TNFRSF14 and, via this interaction, is able to negatively regulate CD4+ T cell activation, indicating a role in immune system regulation.
Catalog Number: (10750-364)

Supplier:  Prosci
Description:   PIG-Y Antibody: Glycosylphosphatidylinositol (GPI) lipid anchoring is an important post-translational modification of proteins that takes place in the endoplasmic reticulum. The synthesis of GPI is initiated by GPI-N-acetylglucosaminyltransferase (GPI-GnT), a complex of proteins including PIG-A, PIG-H, PIG-C, GPI1, and DPM2. PIG-Y, the mammalian homolog to yeast Eri1p, is also thought to be involved in the biosynthesis of GPI. The PIG-Y gene encodes two proteins, one of which arises from leaky scanning of the mRNA.
Catalog Number: (10749-940)

Supplier:  Prosci
Description:   Carabin Antibody: Antigen binding by the T-cell receptor (TCR) is one of the critical first steps in the immune response, triggering a cascade of signaling pathways that ultimately lead to T-cell activation. Screening a yeast two-hybrid screen of a human T-cell cDNA library with calcineurin, a protein phosphatase involved in multiple signaling pathways including T-cell activation, resulted in the identification of Carabin, a member of the TBC1 domain family of proteins, as a calcineurin-binding protein. Unlike other members of the TBC1 domain protein family which are thought to have a role in regulating cell growth and differentiation, further experiments demonstrated that Carabin is part of a negative regulatory loop for the intracellular TCR signaling pathway as well as an inhibitor of the Ras signaling pathway, suggesting that Carabin may also mediate crosstalk between calcineurin and Ras. Carabin antibody does not recognize TBC1D10A or TBC1D10B. Carabin is known to exist in multiple isoforms.
Catalog Number: (76009-692)

Supplier:  Prosci
Description:   Tight junctions represent one mode of cell-to-cell adhesion in epithelial or endothelial cell sheets, forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the paracellular space. These junctions are comprised of sets of continuous networking strands in the outwardly facing cytoplasmic leaflet, with complementary grooves in the inwardly facing extracytoplasmic leaflet. This gene encodes a component of tight junction strands, which is a member of the claudin family. The protein is an integral membrane protein and is one of the entry cofactors for hepatitis C virus. The gene methylation may be involved in esophageal tumorigenesis. This gene is adjacent to another family member CLDN9 on chromosome 16.
Catalog Number: (10751-030)

Supplier:  Prosci
Description:   CCDC106 Antibody: The coiled-coil domain is a common protein motif that is often involved in protein oligomerization and is found in proteins such as transcription factors and intermediate filaments. CCDC106 was initially identified as a p53-interacting protein by yeast two-hybrid screening. Other experiments demonstrated that CCDC106 co-localizes and interacts with p53 in the nucleus, inhibiting the transcriptional activity of p53 and stimulating p53 protein degradation, indicating that at least one of the functions of CCDC106 is acting as a negative regulator of p53.
Catalog Number: (10750-320)

Supplier:  Prosci
Description:   Dact2 Antibody: The Wnt signaling cascade is a conserved process in multicellular animals that plays important roles during development and can contribute to cancer and other diseases. Many members of this pathway are also expressed in the postnatal tissues such as brain. One such protein is Dact2, a member of the Dact protein family that was initially identified through binding to Disheveled (Dvl), a cytoplasmic protein essential to Wnt signaling. Dact2 is most prominent during the development of the thymus kidneys, and salivary gland. Dact2 is thought to play a role distinct from that of Dact1 with Dact2 having a greater impact on a beta-catenin-independent process termed planar cell polarity/convergent-extension signaling. Furthermore, Dact2 but not Dact1 can inhibit Nodal signaling by promoting the endocytic degradation of TGF-beta receptors. At least two isoforms of Dact2 are known to exist.
Supplier:  Bioss
Description:   Matrix Metalloproteinase 8 (MMP8) is also known as neutrophil collagenase and collagenase 2. MMP8 degrades fibrillar collagens types I, II, III, aggrecan, serpins and alpha 2 macroglobulin. All collagenases cleave fibrillar collagens at one specific site resulting in generation of N terminal three quarter and C terminal one quarter fragments, which then denature to gelatin at body temperature. The substrate specificity of collagenases is variable: MMP1 degrades type III collagen more efficiently than type I or type II collagen, whereas MMP8 is more potent in degrading type I collagen than type III or type II collagen. MMP13, in turn degrades type II collagen 6 fold more efficiently than type I and type II collagens and displays almost 50 fold stronger gelatinolytic activity than MMP1 and MMP8. MMP8 is very similar to MMP1, sharing 57 % amino acid identity. Most cell types do not produce MMP8. Until recently, it was thought that MMP8 was produced exclusively by neutrophils, but it has also been detected in other cell types including arthritic chondrocytes and gingival fibroblasts. The human MMP8 gene has the chromosomal location of 11q22.2-22.3. MMP8 is heavily glycosylated, and the zymogen has a mass of 85 Kd. The zymogen is quickly activated to the 64 Kd form, and this breaks down to a cascade of active forms.

Supplier:  Bioss
Description:   Matrix Metalloproteinase 8 (MMP8) is also known as neutrophil collagenase and collagenase 2. MMP8 degrades fibrillar collagens types I, II, III, aggrecan, serpins and alpha 2 macroglobulin. All collagenases cleave fibrillar collagens at one specific site resulting in generation of N terminal three quarter and C terminal one quarter fragments, which then denature to gelatin at body temperature. The substrate specificity of collagenases is variable: MMP1 degrades type III collagen more efficiently than type I or type II collagen, whereas MMP8 is more potent in degrading type I collagen than type III or type II collagen. MMP13, in turn degrades type II collagen 6 fold more efficiently than type I and type II collagens and displays almost 50 fold stronger gelatinolytic activity than MMP1 and MMP8. MMP8 is very similar to MMP1, sharing 57 % amino acid identity. Most cell types do not produce MMP8. Until recently, it was thought that MMP8 was produced exclusively by neutrophils, but it has also been detected in other cell types including arthritic chondrocytes and gingival fibroblasts. The human MMP8 gene has the chromosomal location of 11q22.2-22.3. MMP8 is heavily glycosylated, and the zymogen has a mass of 85 Kd. The zymogen is quickly activated to the 64 Kd form, and this breaks down to a cascade of active forms.
Supplier:  Bioss
Description:   Matrix Metalloproteinase 8 (MMP8) is also known as neutrophil collagenase and collagenase 2. MMP8 degrades fibrillar collagens types I, II, III, aggrecan, serpins and alpha 2 macroglobulin. All collagenases cleave fibrillar collagens at one specific site resulting in generation of N terminal three quarter and C terminal one quarter fragments, which then denature to gelatin at body temperature. The substrate specificity of collagenases is variable: MMP1 degrades type III collagen more efficiently than type I or type II collagen, whereas MMP8 is more potent in degrading type I collagen than type III or type II collagen. MMP13, in turn degrades type II collagen 6 fold more efficiently than type I and type II collagens and displays almost 50 fold stronger gelatinolytic activity than MMP1 and MMP8. MMP8 is very similar to MMP1, sharing 57 % amino acid identity. Most cell types do not produce MMP8. Until recently, it was thought that MMP8 was produced exclusively by neutrophils, but it has also been detected in other cell types including arthritic chondrocytes and gingival fibroblasts. The human MMP8 gene has the chromosomal location of 11q22.2-22.3. MMP8 is heavily glycosylated, and the zymogen has a mass of 85 Kd. The zymogen is quickly activated to the 64 Kd form, and this breaks down to a cascade of active forms.
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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us at 1-800-932-5000.
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