Human CASP9 blocking peptide (CDBP0693)

Synthetic Human CASP9 blocking peptide for BL

Product Overview
Caspase 9 ( N - term ) peptide ( human )
Target
Caspase 9
Nature
Synthetic
Species Reactivity
Human
Tag/Conjugate
Unconjugated
Procedure
None
Concentration
0.2 mg/ml
Size
50 μg
Buffer
PBS with 0.1% BSA 0.02% sodium azide pH7.2
Preservative
0.02% Sodium Azide
Storage
Upon receipt - Keep as concentrated solution. Aliquot and store at -20℃ or below. Avoid freeze-thaw cycles.
UniProt ID
Antigen Description
This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein can undergo autoproteolytic processing and activation by the apoptosome, a protein complex of cytochrome c and the apoptotic peptidase activating factor 1; this step is thought to be one of the earliest in the caspase activation cascade. This protein is thought to play a central role in apoptosis and to be a tumor suppressor. Alternative splicing results in multiple transcript variants. [provided by RefSeq, May 2013]
Function
SH3 domain binding; cysteine-type endopeptidase activity; enzyme activator activity; peptidase activity; protein binding; protein kinase binding;
Synonyms
CASP9; caspase 9, apoptosis-related cysteine peptidase; MCH6; APAF3; APAF-3; PPP1R56; ICE-LAP6; caspase-9; apoptotic protease MCH-6; ICE-like apoptotic protease 6; apoptotic protease activating factor 3; protein phosphatase 1, regulatory subunit 56;

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References


Ecotoxicological assessment of solar cell leachates: Copper indium gallium selenide (CIGS) cells show higher activity than organic photovoltaic (OPV) cells

SCIENCE OF THE TOTAL ENVIRONMENT

Authors: Brun, Nadia Rebecca; Wehrli, Bernhard; Fent, Karl

Despite the increasing use of photovoltaics their potential environmental risks are poorly understood. Here, we compared ecotoxicological effects of two thin-film photovoltaics: established copper indium gallium selenide (CIGS) and organic photovoltaic (OPV) cells. Leachates were produced by exposing photovoltaics to UV light, physical damage, and exposure to environmentally relevant model waters, representing mesotrophic lake water, acidic rain, and seawater. CIGS cell leachates contained 583 mu g L-1 molybdenum at lake water, whereas at acidic rain and seawater conditions, iron, copper, zinc, molybdenum, cadmium, silver, and tin were present up to 7219 mu g L-1. From OPV, copper (14 mu g L-1), zinc (87 mu g L-1) and silver (78 mu g L-1) leached. Zebrafish embryos were exposed until 120 h post-fertilization to these extracts. CIGS leachates produced under acidic rain, as well as CIGS and OPV leachates produced under seawater conditions resulted in a marked hatching delay and increase in heart edema. Depending on model water and solar cell, transcriptional alterations occurred in genes involved in oxidative stress (cat), hormonal activity (vtg1, ar), metallothionein (mt2), ER stress (bip, chop), and apoptosis (casp9). The effects were dependent on the concentrations of cationic metals in leachates. Addition of ethylenediaminetetraacetic acid protected zebrafish embryos from morphological and molecular effects. Our study suggests that metals leaching from damaged CIGS cells, may pose a potential environmental risk. (C) 2015 Elsevier B.V. All rights reserved.

Effects of sex steroids on indices of protein turnover in rainbow trout (Oncorhynchus mykiss) white muscle

GENERAL AND COMPARATIVE ENDOCRINOLOGY

Authors: Cleveland, Beth M.; Weber, Gregory M.

Effects of 17 beta-estradiol (E2), testosterone, and 5 alpha-dihydrotestosterone (DHT) on protein turnover and proteolytic gene expression were determined in rainbow trout (Oncorhynchus mykiss) primary myocytes and white muscle tissue. E2 reduced rates of protein synthesis and increased rates of protein degradation in primary myocytes by 45% and 27%, respectively. DHT reduced rates of protein synthesis by 27%. Testosterone did not affect protein synthesis and neither testosterone nor DHT affected rates of protein degradation. Single injections of E2 increased expression of ubiquitin ligase genes fbxo32, fbxo25, and murf1, and the proteasome subunit psmd6 by 24 h after injection. Within the cathepsin-lysosome pathway, E2 increased expression of cathepsins ctsd and ctsl, as well as autophagy-related genes atg4b and lc3b. Additionally, E2 injection up-regulated the expression of casp3 and casp9 caspase genes. Incubation of primary myocytes with E2 also increased expression of ubiquitin ligase genes. Therefore, catabolic effects of E2 on protein turnover result in part from E2-induced increases in proteolytic gene expression directly in muscle. Injection of testosterone increased milli-calpain (capn2) and casp3 expression, and DHT increased ctsd expression in vivo, whereas both androgens up-regulated fbxo32 expression in primary myocytes. These results suggest that effects of androgens on protein turnover in muscle are not driven primarily by direct effects of these hormones in this tissue. Published by Elsevier Inc.

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