Keep my session open?
Ending In 
The session is expired
Your session has expired. For your security, we have logged you out.
Would you like to log in again?

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

  • Product Results
  • Product Category
  • Criteria
  • Supplier
  • Refine by Suppliers
    Sort by:

  • Search Within Results

You Searched For:

4-(Cbz-amino)piperidine+Hydrochloride


27,384  results were found

SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-HORIZONTAL
 
 
SearchResultCount:"27384"
  List View Searching Easy View BETA(new)
Sort by:
 
 
 
 

Supplier:  Bioss
Description:   Actin polymerization is required for a variety of cell functions, including chemotaxis, cell migration, cell adhesion, and platelet activation. Cells trigger actin polymerization through either the de novo nucleation of filaments from monomeric actin, the severing of existing filaments to create uncapped barbed ends, or the uncapping of existing barbed ends. The nucleation of actin is a rate-limiting and unfavorable reaction in actin polymerization and therefore requires the involvement of the Arp2/3 complex, which helps create new filaments and promotes the end-to-side cross-linking of actin filaments into the branching meshwork. The Arp2/3 complex consists of the actin-related proteins Arp2 and Arp3, and various other accessory proteins. The Arp2/3 complex promotes actin nucleation by binding the pointed end of actin filaments, or by associating with the side of an existing filament, and nucleates growth in the barbed direction. In addition, the Arp2/3 complex also mediates actin cytoskeletal outgrowths that are regulated by the Rho family of small GTPases. In response to GTP-binding Cdc42, the Arp2/3 complex binds the Cdc42 substrates, namely the WASP proteins, and initiates the formation of lamellipodia and filopodia.
Catalog Number: (10255-394)

Supplier:  Bioss
Description:   In mammalian cells, transcription is regulated in part by high molecular weight coactivating complexes that mediate signals between transcriptional activators and RNA polymerase (1). These complexes include the SMCC (SRB and MED protein cofactor complex), which consists of various subunits that share homology with several components of the yeast transcriptional mediator complexes, and including the human proteins Srb7, Med6 (also designated DRIP33) and Med7 (also designated DRIP34) (2,3). SMCC associates with the RNAPII (RNA polymerase II) holoenzyme through Srb7 and, in turn, enhances gene-specific activation or repression induced by DNA-binding transcription factors (4). Med6 and Med7, as well as other components of SMCC, associate with coactivator proteins from the TRAP (thyroid hormone receptor-activating protein) complex and DRIP (for vitamin D receptor interacting protein) complex to facilitate steroid receptor dependent transcriptional activation (4,5). Additionally, SMCC associates with PC4 (positive cofactor 4) to repress basal transcription independent of RNAPII activity (6).

Supplier:  Bioss
Description:   In mammalian cells, transcription is regulated in part by high molecular weight coactivating complexes that mediate signals between transcriptional activators and RNA polymerase (1). These complexes include the SMCC (SRB and MED protein cofactor complex), which consists of various subunits that share homology with several components of the yeast transcriptional mediator complexes, and including the human proteins Srb7, Med6 (also designated DRIP33) and Med7 (also designated DRIP34) (2,3). SMCC associates with the RNAPII (RNA polymerase II) holoenzyme through Srb7 and, in turn, enhances gene-specific activation or repression induced by DNA-binding transcription factors (4). Med6 and Med7, as well as other components of SMCC, associate with coactivator proteins from the TRAP (thyroid hormone receptor-activating protein) complex and DRIP (for vitamin D receptor interacting protein) complex to facilitate steroid receptor dependent transcriptional activation (4,5). Additionally, SMCC associates with PC4 (positive cofactor 4) to repress basal transcription independent of RNAPII activity (6).

Supplier:  Bioss
Description:   In mammalian cells, transcription is regulated in part by high molecular weight coactivating complexes that mediate signals between transcriptional activators and RNA polymerase (1). These complexes include CRSP (for cofactor required for Sp1 activation), which is required, in conjunction with TAFIIs, for transcriptional activation by Sp1 (2). CRSP is ubiquitously expressed in various tissues and functions as a multimeric complex that consists of nine distinct subunits (3). Several members of the CRSP family share sequence similarity with multiple components of the yeast transcriptional mediator proteins, including CRSP150, which is related to yeast Rgr1, and CRSP70, which is similar to the elongation factor TFIIS (4). CRSP77 and CRSP150 are also related to proteins within the putative murine mediator complex, while CRSP130 and CRSP34 are largely unrelated to either murine or yeast proteins (2,5). CRSP subunits also associate with larger multimeric coactivaor complexes, including ARC/DRI, which binds directly to SREBP and nuclear hormone receptors to facilitate transcription, and with NAT, a polymerase II-interacting complex that represses activated transcription (6,7).
Supplier:  Bioss
Description:   Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for cell division. BCR E3 ubiquitin ligase complexes mediate the ubiquitination of target proteins.

Supplier:  Enzo Life Sciences
Description:   C5b-9, also known as the terminal complement complex (TCC), consists of C5b, C6, C7, C8 and C9, and it forms the membrane attack complex (MAC) as well as the non-lytic fluid-phase SC5b-9 complex (with protein S). The MAC forms channels in target cell membranes leading to cell lysis by osmotic leakage. The complexes contain neoantigens absent from the individual native components from which they are formed, and the antibody is directed against a neoepitope exposed on C9 when incorporated into the TCC.

Supplier:  Bioss
Description:   Pinch is a focal adhesion protein that is a component of the ILK-PINCH complex. This complex is a major part of the growth factor and integrin signaling pathway. Pinch is involved in cell differentiation, proliferation and survival by acting as an effector of integrin and growth factor signaling. It is a cytoplasmic protein expressed in most tissues and consists of five LIM domains, a nuclear localization signal and a nuclear export signal. The PINCH-1/ILK complex is regulated by another member of the Pinch family, PINCH-2, which also forms a complex with ILK.

Supplier:  Bioss
Description:   Pinch is a focal adhesion protein that is a component of the ILK-PINCH complex. This complex is a major part of the growth factor and integrin signaling pathway. Pinch is involved in cell differentiation, proliferation and survival by acting as an effector of integrin and growth factor signaling. It is a cytoplasmic protein expressed in most tissues and consists of five LIM domains, a nuclear localization signal and a nuclear export signal. The PINCH-1/ILK complex is regulated by another member of the Pinch family, PINCH-2, which also forms a complex with ILK.
Supplier:  Bioss
Description:   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 p65-c-Rel complexes are transcriptional activators. The NF-kappa-B p65-p65 complex appears to be involved in invasin-mediated activation of IL-8 expression. The inhibitory effect of I-kappa-B upon NF-kappa-B the cytoplasm is exerted primarily through the interaction with p65. p65 shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappa-B complex. Associates with chromatin at the NF-kappa-B promoter region via association with DDX1. Essential for cytokine gene expression in T-cells (PubMed:15790681).
Supplier:  Bioss
Description:   PDHX is component X of the pyruvate dehydrogenase (PDH) complex.It is required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex. PDHX is expressed in the mithochondrion.
Catalog Number: (10106-490)

Supplier:  Prosci
Description:   MCM7 encodes a protein that is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein complex formed by the MCM proteins is a key component of the pre-replication complex (pre_RC) and may be involved in the formation of replication forks and in the recruitment of other DNA replication related proteins. The MCM complex consisting of this protein and MCM2, 4 and 6 proteins possesses DNA helicase activity, and may act as a DNA unwinding enzyme.The protein encoded by this gene is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein complex formed by the MCM proteins is a key component of the pre-replication complex (pre_RC) and may be involved in the formation of replication forks and in the recruitment of other DNA replication related proteins. The MCM complex consisting of this protein and MCM2, 4 and 6 proteins possesses DNA helicase activity, and may act as a DNA unwinding enzyme. Cyclin D1-dependent kinase, CDK4, is found to associate with this protein, and may regulate the binding of this protein with the tumorsuppressor protein RB1/RB. Alternatively spliced transcript variants encoding distinct isoforms have been reported.

Supplier:  Bioss
Description:   Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex. The BCR(KLHL7) complex acts by mediating ubiquitination and subsequent degradation of substrate proteins. Probably mediates 'Lys-48'-linked ubiquitination.
Supplier:  Bioss
Description:   Stabilizes the cyclin H-CDK7 complex to form a functional CDK-activating kinase (CAK) enzymatic complex. CAK activates the cyclin-associated kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C-terminal domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter and elongation of the transcripts. Involved in cell cycle control and in RNA transcription by RNA polymerase II.
Catalog Number: (10471-806)

Supplier:  Bioss
Description:   Involved in intracellular signal transduction mediated by cytokines and growth factors. Upon IL-2 and GM-CSL stimulation, it plays a role in signaling leading to DNA synthesis and MYC induction. May also play a role in T-cell development. Involved in down-regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with HGS (ESCRT-0 complex). The ESCRT-0 complex binds ubiquitin and acts as sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential lysosomal sorting/trafficking processes.

Supplier:  Bioss
Description:   Stabilizes the cyclin H-CDK7 complex to form a functional CDK-activating kinase (CAK) enzymatic complex. CAK activates the cyclin-associated kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C-terminal domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter and elongation of the transcripts. Involved in cell cycle control and in RNA transcription by RNA polymerase II.
Supplier:  New England Biolabs (NEB)
Description:   Peptide-N-Glycosidase F, also known as PNGase F, is a recombinant amidase which cleaves between the innermost GlcNAc and asparagine residues of high mannose, hybrid, and complex oligosaccharides from N-linked glycoproteins.
Small Business Enterprise
Inquire for Price
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.
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.
This product is marked as restricted and can only be purchased by approved Shipping Accounts. If you need further assistance, email VWR Regulatory Department at Regulatory_Affairs@vwr.com
-Additional Documentation May be needed to purchase this item. A VWR representative will contact you if needed.
This product has been blocked by your organization. Please contact your purchasing department for more information.
The original product is no longer available. The replacement shown is available.
This product is no longer available. Alternatives may be available by searching with the VWR Catalog Number listed above. If you need further assistance, please call VWR Customer Service at 1-800-932-5000.
2,401 - 2,416  of 27,384