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


125,134  results were found

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Supplier:  Bioss
Description:   CBLL1, also known as HAKAI (meaning destruction? in Japanese), or RNF188 (RING finger protein 188), is a 491 amino acid protein that contains one C2H2-type zinc finger and one RING-type zinc finger. CBLL1 is believed to function as an E3 ubiquitin-protein ligase that accepts a ubiquitin residue from an E2 ubiquitin-conjugating enzyme and immediately transfers that residue to a protein that is targeted for degradation. More specifically, upon activation of c-Src, CBLL1 interacts with and ubiquitinates tyrosine-phosphorylated E-cadherin, thereby targeting the E-cadherin complex for endocytosis and disrupting epithelial cell-cell contacts. Via its role as an E-cadherin regulator, CBLL1 participates in cell adhesion and may also be involved in the regulation of epithelial-mesenchymal transitions.

Supplier:  Bioss
Description:   CBLL1, also known as HAKAI (meaning ‘destruction’ in Japanese), or RNF188 (RING finger protein 188), is a 491 amino acid protein that contains one C2H2-type zinc finger and one RING-type zinc finger. CBLL1 is believed to function as an E3 ubiquitin-protein ligase that accepts a ubiquitin residue from an E2 ubiquitin-conjugating enzyme and immediately transfers that residue to a protein that is targeted for degradation. More specifically, upon activation of c-Src, CBLL1 interacts with and ubiquitinates tyrosine-phosphorylated E-cadherin, thereby targeting the E-cadherin complex for endocytosis and disrupting epithelial cell-cell contacts. Via its role as an E-cadherin regulator, CBLL1 participates in cell adhesion and may also be involved in the regulation of epithelial-mesenchymal transitions.
Supplier:  Bioss
Description:   SNF2L, also known as SMARCA1 (SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1), SWI or ISWI, is a 1,054 amino acid protein that localizes to the nucleus and contains one helicase C-terminal domain, one helicase ATP-binding domain and two SANT domains. Expressed as multiple alternatively spliced isoforms, SNF2L exists as a component of the nucleosome-remodeling factor (NURF) complex where it helps to facilitate the ATP-dependent perturbation of chromatin structure and may also be involved in brain development and neurite outgrowth. The gene encoding SNF2L maps to human chromosome X, which contains nearly 153 million base pairs and houses over 1,000 genes.
Catalog Number: (10459-086)

Supplier:  Bioss
Description:   The Brn family of transcription factors are found in a highly restricted subset of neurons and are critical to the early embryonic development of the central nervous system. Brn-1 and Brn-2 are class III POU (Pit-Oct-Unc) domain proteins, whereas Brn-3 is a class IV POU domain protein. Three Brn-3 proteins have been described and are designated Brn-3a, Brn-3b and Brn-3c. While Brn-3a and Brn-3c stimulate transcription, Brn-3b generally functions as a transcriptional repressor. However, Brn-3b, but not Brn-3a, has been shown to regulate the expression of the acetylcholine receptor. Interestingly, Brn-3a has two functional transactivating domains, one at the amino-terminus and one at the carboxy-terminus. Brn-2 is thought to be involved in smooth muscle cell development and differentiation.

Supplier:  Bioss
Description:   Ubiquitination is an important mechanism through which three classes of enzymes act in concert to target short-lived or abnormal proteins for destruction. The three classes of enzymes involved in ubiquitination are the ubiquitin-activating enzymes (E1s), the ubiquitin-conjugating enzymes (E2s) and the ubiquitin-protein ligases (E3s). Ubr2 (Ubiquitin-protein ligase E3-alpha-2), also known as N-recognin-2, is a 1755 amino acid protein that contains one UBR-type zinc finger and one RING-type zinc finger. Participating in protein modification events within the N-end rule pathway, Ubr2 functions as an E3 ubiquitin-protein ligase that recognizes and binds proteins that contain destabilizing N-terminal residues, thereby leading to their ubiquitination and subsequent degradation. Mice lacking Ubr2 are infertile due to defects in male meiosis.
Supplier:  Bioss
Description:   The death domain (DD) superfamily of proteins share one or more of the following domains: the DD, DED (death-effector domain), CARD (caspase-recruitment domain) and PYD (Pyrin domain). Each of these domains is characterized by a canonical death domain fold, which consists of a bundle of five or six antiparallel α-helices. As their names suggest, these domains play prominent roles in programmed cell death. ASC2 (apoptosis-associated speck-like protein containing a CARD 2), also known as Pyrin-only protein 1 or PADD-only protein 1, is an 89 amino acid member of the DD superfamily that contains one Pyrin domain. Localized to the cytoplasm, ASC2 interacts with ASC to modulate NF-κB and pro-caspase-1 regulation. ASC2 is predominantly expressed in monocytes, macrophages and granulocytes.

Supplier:  Bioss
Description:   The death domain (DD) superfamily of proteins share one or more of the following domains: the DD, DED (death-effector domain), CARD (caspase-recruitment domain) and PYD (Pyrin domain). Each of these domains is characterized by a canonical death domain fold, which consists of a bundle of five or six antiparallel α-helices. As their names suggest, these domains play prominent roles in programmed cell death. ASC2 (apoptosis-associated speck-like protein containing a CARD 2), also known as Pyrin-only protein 1 or PADD-only protein 1, is an 89 amino acid member of the DD superfamily that contains one Pyrin domain. Localized to the cytoplasm, ASC2 interacts with ASC to modulate NF-κB and pro-caspase-1 regulation. ASC2 is predominantly expressed in monocytes, macrophages and granulocytes.

Supplier:  Bioss
Description:   Ubiquitination is an important mechanism through which three classes of enzymes act in concert to target short-lived or abnormal proteins for destruction. The three classes of enzymes involved in ubiquitination are the ubiquitin-activating enzymes (E1s), the ubiquitin-conjugating enzymes (E2s) and the ubiquitin-protein ligases (E3s). Ubr2 (Ubiquitin-protein ligase E3-alpha-2), also known as N-recognin-2, is a 1755 amino acid protein that contains one UBR-type zinc finger and one RING-type zinc finger. Participating in protein modification events within the N-end rule pathway, Ubr2 functions as an E3 ubiquitin-protein ligase that recognizes and binds proteins that contain destabilizing N-terminal residues, thereby leading to their ubiquitination and subsequent degradation. Mice lacking Ubr2 are infertile due to defects in male meiosis.
Supplier:  Bioss
Description:   Ubiquitination is an important mechanism through which three classes of enzymes act in concert to target short-lived or abnormal proteins for destruction. The three classes of enzymes involved in ubiquitination are the ubiquitin-activating enzymes (E1s), the ubiquitin-conjugating enzymes (E2s) and the ubiquitin-protein ligases (E3s). Ubr2 (Ubiquitin-protein ligase E3-alpha-2), also known as N-recognin-2, is a 1755 amino acid protein that contains one UBR-type zinc finger and one RING-type zinc finger. Participating in protein modification events within the N-end rule pathway, Ubr2 functions as an E3 ubiquitin-protein ligase that recognizes and binds proteins that contain destabilizing N-terminal residues, thereby leading to their ubiquitination and subsequent degradation. Mice lacking Ubr2 are infertile due to defects in male meiosis.
Catalog Number: (76012-688)

Supplier:  Prosci
Description:   Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha-chain (By similarity).

Supplier:  Bioss
Description:   HILI is a 973 amino acid protein encoded by the human gene PIWIL2. HILI belongs to the argonaute family and contains one PAZ domain and one PIWI domain. HILI is a cytoplasmic protein that is expressed in adult testis and in most tumors. It regulates spermatogenesis and primordial germ cell production and has an essential role in meiotic differentiation of spermatocytes and in self-renewal of spermatogonial stem cells. Expression of HILI can modulate expression of genes involved in stem cell proliferation (such as PDGFR-b), in energy metabolism (such as Glut1), in cell-cell interaction (such as Integrin a6, GJA7, THY-1 and CD9), and in germ cell differentiation (such as STRA8). It may also play a role as a regulatory factor of Stat3/Bcl-xS/L/CCND1 pathway. Repression of HILI can inhibit tumor cell growth. HILI acts as an oncogene by inhibition of apoptosis and promotion of proliferation in tumors.
Catalog Number: (10483-050)

Supplier:  Bioss
Description:   CBLL1, also known as HAKAI (meaning ‘destruction’ in Japanese), or RNF188 (RING finger protein 188), is a 491 amino acid protein that contains one C2H2-type zinc finger and one RING-type zinc finger. CBLL1 is believed to function as an E3 ubiquitin-protein ligase that accepts a ubiquitin residue from an E2 ubiquitin-conjugating enzyme and immediately transfers that residue to a protein that is targeted for degradation. More specifically, upon activation of c-Src, CBLL1 interacts with and ubiquitinates tyrosine-phosphorylated E-cadherin, thereby targeting the E-cadherin complex for endocytosis and disrupting epithelial cell-cell contacts. Via its role as an E-cadherin regulator, CBLL1 participates in cell adhesion and may also be involved in the regulation of epithelial-mesenchymal transitions.
Supplier:  Bioss
Description:   CBLL1, also known as HAKAI (meaning destruction? in Japanese), or RNF188 (RING finger protein 188), is a 491 amino acid protein that contains one C2H2-type zinc finger and one RING-type zinc finger. CBLL1 is believed to function as an E3 ubiquitin-protein ligase that accepts a ubiquitin residue from an E2 ubiquitin-conjugating enzyme and immediately transfers that residue to a protein that is targeted for degradation. More specifically, upon activation of c-Src, CBLL1 interacts with and ubiquitinates tyrosine-phosphorylated E-cadherin, thereby targeting the E-cadherin complex for endocytosis and disrupting epithelial cell-cell contacts. Via its role as an E-cadherin regulator, CBLL1 participates in cell adhesion and may also be involved in the regulation of epithelial-mesenchymal transitions.
Supplier:  Bioss
Description:   The death domain (DD) superfamily of proteins share one or more of the following domains: the DD, DED (death-effector domain), CARD (caspase-recruitment domain) and PYD (Pyrin domain). Each of these domains is characterized by a canonical death domain fold, which consists of a bundle of five or six antiparallel -helices. As their names suggest, these domains play prominent roles in programmed cell death. ASC2 (apoptosis-associated speck-like protein containing a CARD 2), also known as Pyrin-only protein 1 or PADD-only protein 1, is an 89 amino acid member of the DD superfamily that contains one Pyrin domain. Localized to the cytoplasm, ASC2 interacts with ASC to modulate NF-B and pro-caspase-1 regulation. ASC2 is predominantly expressed in monocytes, macrophages and granulocytes.
Supplier:  Bioss
Description:   The death domain (DD) superfamily of proteins share one or more of the following domains: the DD, DED (death-effector domain), CARD (caspase-recruitment domain) and PYD (Pyrin domain). Each of these domains is characterized by a canonical death domain fold, which consists of a bundle of five or six antiparallel -helices. As their names suggest, these domains play prominent roles in programmed cell death. ASC2 (apoptosis-associated speck-like protein containing a CARD 2), also known as Pyrin-only protein 1 or PADD-only protein 1, is an 89 amino acid member of the DD superfamily that contains one Pyrin domain. Localized to the cytoplasm, ASC2 interacts with ASC to modulate NF-B and pro-caspase-1 regulation. ASC2 is predominantly expressed in monocytes, macrophages and granulocytes.
Supplier:  Bioss
Description:   The death domain (DD) superfamily of proteins share one or more of the following domains: the DD, DED (death-effector domain), CARD (caspase-recruitment domain) and PYD (Pyrin domain). Each of these domains is characterized by a canonical death domain fold, which consists of a bundle of five or six antiparallel α-helices. As their names suggest, these domains play prominent roles in programmed cell death. ASC2 (apoptosis-associated speck-like protein containing a CARD 2), also known as Pyrin-only protein 1 or PADD-only protein 1, is an 89 amino acid member of the DD superfamily that contains one Pyrin domain. Localized to the cytoplasm, ASC2 interacts with ASC to modulate NF-κB and pro-caspase-1 regulation. ASC2 is predominantly expressed in monocytes, macrophages and granulocytes.
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