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4-Amino-1-phenylpyrrolidin-2-one+hydrochloride


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Supplier:  Bioss
Description:   The BTB (broad-complex, Tramtrack and Bric a brac) domain, also known as the POZ (Poxvirus and zinc finger) domain, is an N-terminal homodimerization domain that contains multiple copies of kelch repeats and/or C2H2-type zinc fingers. Proteins that contain BTB domains are thought to be involved in transcriptional regulation via control of chromatin structure and function. BTBD17 (BTB/POZ domain-containing protein 17), also known as BTBD17A, galectin-3-binding protein-like or LGALS3BPL, is a 478 amino acid protein that contains one BTB (POZ) domain and a BACK (BTB/Kelch associated) domain. The gene encoding BTBD17 maps to human chromosome 17, which comprises over 2.5% of the human genome and encodes over 1,200 genes. Two key tumor suppressor genes are associated with chromosome 17, namely, p53 and BRCA1. Malfunction or loss of p53 expression is associated with malignant cell growth and Li-Fraumeni syndrome.
Supplier:  Bioss
Description:   RNA polymerase II (Pol II) is an enzyme that is composed of twelve subunits and is responsible for the transcription of protein-coding genes. Transcription initiation requires Pol II-mediated recruitment of transcription machinery to a target promoter, thereby allowing transcription to begin. The largest subunit of Pol II (referred to as RPB1 or RPB205) is a 1,840 amino acid protein that contains one C2H2-type zinc finger and a C-terminal domain comprised of several heptapeptide repeats. Although Pol II function requires the cooperation of all twelve subunits, the largest subunit conveys Pol II catalytic activity and, together with the second largest subunit, forms the active center of the Pol II enzyme. Additionally, the large subunit participates in forming the DNA-binding domain of Pol II, a groove that is necessary for transcription of the DNA template. Without proper function of the large subunit, mRNA synthesis and subsequent transcription elongation cannot occur.
Catalog Number: (10332-632)

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.
Catalog Number: (10207-000)

Supplier:  Boster Biological Technology
Description:   Rabbit IgG polyclonal antibody for WNT1-inducible-signaling pathway protein 1(WISP1) detection. Tested with WB, IHC-P, IHC-F, ICC in Human;Mouse;Rat.
Catalog Number: (10075-618)

Supplier:  Prosci
Description:   The three Mitogen-Activated Protein Kinases (MAPKs) are evolutionarily conserved protein kinases that control a vast array of cellular processes. p38 MAPK is one these kinases and it is activated by both inflammatory cytokines and by stress. The p38 MAPK is thought to be particularly important in diseases like asthma and autoimmunity but it also plays important roles in the stress response of the nervous system. Like the other MAPKs, p38 is activated by a dual specificity kinase that phosphorylates Thr180 and Tyr182.
Catalog Number: (10751-248)

Supplier:  Prosci
Description:   BAPX1 Antibody: BAPX1 is the mammalian homolog of the Drosophila bagpipe homeobox gene and is expressed in the splanchnic mesoderm and embryonic skeleton. It is one of the earliest developmental markers for the sclerotome portion of the somite and the gut mesentery. BAPX1 is required for normal skeletal development; homozygous inactivating mutations in the BAPX1 gene result in spodylo-megaepiphyseal-metaphyseal dysplasia (SMMD). It has also been suggested to play a role in the proper development of the mammalian gut and is required for distal stomach development as part of a BARX1-dependent pathway.
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.
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: (10749-242)

Supplier:  Prosci
Description:   SLCO1B1 is a transmembrane receptor that mediates the sodium-independent uptake of numerous endogenous compounds including bilirubin, 17-beta-glucuronosyl estradiol and may play an important role in the clearance of bile acids and organic anions from the liver. It contains one Kazal-like domain and belongs to the organo-anion transporter family. SLCO1B1 is highly expressed in liver and is localized to the basolateral hepatocyte membrane. It is responsible for the hepatic uptake of the liver-specific hydroxymethylglutaryl-CoA reductase inhibitor in mouse, rat and human.
Catalog Number: (10751-944)

Supplier:  Prosci
Description:   CNRIP1 Antibody: The CNRIP1 (cannabinoid receptor interacting protein 1) protein is a G-protein coupled receptor which interacts with the C-terminal tail of cannabinoid receptor 1 (CB1) and is thought to play a role in synaptic plasticity, analgesia, appetite, and neuroprotection. One isoform of CNRIP1, CNRIP1a, modulates the constitutive CB1 receptor activity in the central nervous system (CNS), while the role of the shorter isoform CNRIP1b is yet unknown. CNRIP1 has been suggested as a potential target for CNS drug discovery.
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.
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: (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: (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.
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