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:

Boc-Cys(SEt)-OH\\\\\\\\u00B7DCHA


39,102  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:"39102"
  List View Searching Easy View BETA(new)
Sort by:
 
 
 
 

Supplier:  Bioss
Description:   May catalyze the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. Specific for amino acid residues with aromatic side chains in the P1 position. Cleaves insulin A chain at '14-Tyr-|-Gln-15' and insulin B chain at '6-Leu-|-Cys-7', '16-Tyr-|-Leu-17', '25-Phe-|-Tyr-26' and '26-Tyr-|-Thr-27'. Could play a role in the activation of precursors to inflammatory cytokines.
Catalog Number: (10459-162)

Supplier:  Bioss
Description:   RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.Sequence similarities: Belongs to the RuBisCO large chain family. Type I subfamily.Post-translational modifications: The disulfide bond which can form between Cys-247 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover (By similarity). The disulfide bonds reported in 1RBO may be the result of oxidation during crystallization.

Supplier:  Genetex
Description:   Mouse Monoclonal antibody to Actin [AC-40]
Catalog Number: (75790-534)

Supplier:  Prosci
Description:   It is a single-pass type I membrane protein and contains 4 TNFR-Cys repeats. The protein is a member of the tumor necrosis factor (TNF) family of receptors. It is expressed on the surface of most cell types, including cells of epithelial and myeloid lineages, but not on T and B lymphocytes. The protein is the receptor for the heterotrimeric lymphotoxin containing LTA and LTB, and for TNFS14/LIGHT. It promotes apoptosis via TRAF3 and TRAF5 and may play a role in the development of lymphoid organs. The encoded protein and its ligand play a role in the development and organization of lymphoid tissue and transformed cells. Activation of the encoded protein can trigger apoptosis. Not only does the TNFRSF3 help trigger apoptosis, it can lead to the release of the cytokine interleukin 8. Overexpression of TNFRSF3 in Human Cells cells increases IL-8 promoter activity and leads to IL-8 release. TNFRSF3 is also essential for development and organization of the secondary lymphoid organs and chemokine release.
Supplier:  Bioss
Description:   EphA3 is a member of the Ephrin (Eph) family. The Ephrins and Eph-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and have been implicated in mediating developmental events, especially in the nervous system and in erythropoiesis. Based on their structures and sequence relationships, ephrins are divided into the Ephrin A (EphA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the Ephrin B (EphB) class, which are transmembrane proteins. Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats.
Supplier:  PeproTech, Inc.
Description:   Persephin is a disulfide-linked, homodimeric, neurotrophic factor structurally related to GDNF, artemin, and neurturin. These proteins belong to the cysteine knot family of growth factors that assume stable dimeric structures. Persephin signals through a multicomponent receptor system, composed of RET and one of four GFR α (α1-α4) receptors. The GFRα4 was first identified in chicken, and was later shown to be the preferential binding subunit for persephin. Persephin promotes the survival of ventral midbrain dopaminergic neurons and motor neurons after sciatic nerve oxotomy, and, like GDNF, promotes ureteric bud branching. However, in contrast to GDNF and neurturin, persephin does not support the survival of peripheral neurons. Recombinant Murine Persephin is a disulfide-linked homodimer, composed of two 10.3 kDa polypeptide chains (192 total amino acid residues). Each chain contains seven conserved cysteine residues, one of which (Cys 63) is used for inter-chain disulfide bridging, and the others are involved in the intramolecular ring formation known as the cysteine knot configuration.
Supplier:  Anaspec Inc
Description:   Oxytocin (OT) is a 9-amino acid peptide that is synthesized primarily in the hypothalamic neurons, specifically the magnocellular oxytocin neurons in the supraoptic and paraventricular nuclei and is secreted by the posterior pituitary gland. It is also secreted from other tissues, such as the ovaries and testes. Circulating OT is important during parturition and lactation. In the pregnant uterus, oxytocin and the oxytocin receptor play a major part for uterine contractility and the induction of labor. OT is also involved in complex social behaviors such as affiliation, sexual behavior, social recognition, stress buffering, aggression, and trust.
Sequence: CYIQNCPLG-NH2 (Disulfide bridge: 1-6)
MW: 1007.2 Da
% Peak area by HPLC: 95
Storage condition: -20° C
Supplier:  Bioss
Description:   May catalyze the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. Specific for amino acid residues with aromatic side chains in the P1 position. Cleaves insulin A chain at '14-Tyr-|-Gln-15' and insulin B chain at '6-Leu-|-Cys-7', '16-Tyr-|-Leu-17', '25-Phe-|-Tyr-26' and '26-Tyr-|-Thr-27'. Could play a role in the activation of precursors to inflammatory cytokines.
Supplier:  Bioss
Description:   Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide, cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Isoform 3 seems to be inactive.

Supplier:  Bioss
Description:   Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide, cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Isoform 3 seems to be inactive.
Supplier:  AMBEED, INC
Description:   L(+)-Cysteine hydrochloride 95%
Supplier:  Bioss
Description:   EphA3 is a member of the Ephrin (Eph) family. The Ephrins and Eph-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and have been implicated in mediating developmental events, especially in the nervous system and in erythropoiesis. Based on their structures and sequence relationships, ephrins are divided into the Ephrin A (EphA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the Ephrin B (EphB) class, which are transmembrane proteins. Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats.
Supplier:  AMBEED, INC
Description:   tert-Butyl ((1R,4S)-4-(hydroxymethyl)cyclopent-2-en-1-yl)carbamate 97%
Supplier:  Bioss
Description:   Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide, cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Isoform 3 seems to be inactive.

Supplier:  Bioss
Description:   Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide, cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Isoform 3 seems to be inactive.
Supplier:  ANTIBODIES.COM LLC
Description:   Mouse monoclonal [EH12.2H7] antibody to CD279 (PerCP-Cyanine 5.5) for Flow Cytometry with samples derived from Human and Non-Human Primates.
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.
1,969 - 1,984  of 39,102