Recombinant Human Cytochrome C (CYCS) Protein (GST)

Name: Recombinant Human Cytochrome C (CYCS) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-04408P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) CYCS.

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Product Overview

Description	Recombinant Human Cytochrome C (CYCS) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P99999
Target Symbol	CYCS
Synonyms	CYC; CYC_HUMAN; CYCS; Cytochrome c; Cytochrome c somatic; HCS; THC4
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	GDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGYSYTAANKNKGIIWGEDTLMEYLENPKKYIPGTKMIFVGIKKKEERADLIAYLKKATNE
Expression Range	2-105aa
Protein Length	Full Length of Mature Protein
Mol. Weight	38.6kDa
Research Area	Apoptosis
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.; Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases.
Subcellular Location	Mitochondrion intermembrane space. Note=Loosely associated with the inner membrane.
Protein Families	Cytochrome c family
Database References	HGNC: 19986 OMIM: 123970 KEGG: hsa:54205 STRING: 9606.ENSP00000307786 UniGene: PMID: 29257225 The caspase-8/Bid/cytochrome c axis links signals from death receptors to mitochondrial reactive oxygen species production. PMID: 28888620 This work reveals a direct conformational link between the 40-57 Omega-loop of cytochrome c in which residue 41 resides and the dynamical properties of the axial ligand to the heme iron. PMID: 27461282 The naturally occurring Y48H variant of cytochrome c in its oxidized heme state is more peroxidatic than either the Wild Type protein or the G41S variant that is also implicated in thrombocytopenia. PMID: 29083920 ROCK activation phosphorylated Rac1b at Ser71 and increased reactive oxygen species (ROS) levels by facilitating the interaction between Rac1b and cytochrome c. Conversely, ROCK inactivation abolished their interaction, concomitant with ROS reduction. PMID: 28317242 Data suggest that although HCCS mediates heme attachment to N-terminal cysteine in heme-attachment site (CXXXH) of cytochrome C variants, up to 50% of cytochrome C produced is modified in an oxygen-dependent manner, resulting in a mixed population of cytochrome c. [HCCS = holocytochrome c synthase] PMID: 28617588 Data suggest that the stronger effect of K72A mutation on the peroxidase activity of human versus yeast cytochrome c results from relief of steric interactions between side chains at positions 72 and 81 (Ile in human vs Ala in yeast), which suppresses the dynamics of omega-loop D necessary for the intrinsic peroxidase activity of cytochrome c. PMID: 28598148 These findings establish a framework for understanding the molecular basis of cytochrome c-mediated blocking of SET/TAF-Ibeta. PMID: 26216969 Monitoring of serum cytochrome c might also serve as a sensitive apoptotic marker in vivo reflecting chemotherapy-induced cell death burden in patients with non-small cell lung cancer. PMID: 25578497 G-Rh2 causes rapid and dramatic translocation of both Bak and Bax, which subsequently triggers mitochondrial cytochrome c release and consequent caspase activation. PMID: 23443079 The mitochondrial metalloprotease OMA1 was activated in a Bax- and Bak-dependent fashion. PMID: 25275009 In vitro ultrastructural changes of MCF-7 for metastasise bone cancer and induction of apoptosis via mitochondrial cytochrome C released by CaCO3/Dox nanocrystals PMID: 25028650 a mechanism of multiple radical formations in the cytochrome c-phospholipid complexes under H2O2 treatment, consistent with the stabilization of the radical in the G41S mutant, which elicits a greater peroxidase activity from cytochrome c PMID: 24099549 proposed that mutation of residue 41, and interaction with cardiolipin, increase peroxidase activity by altering the 40-57 Omega loop and its hydrogen bond network with the propionate of haem ring A; these changes enhance access of hydrogen peroxide and substrate to the haem PMID: 24329121 Data indicate a novel missense mutation (Y48H) of the cytochrome c (CYCS) gene responsible for thrombocytopenia. PMID: 24326104 results suggest the impact of residue 41 on the conformation of cytochrome c influences its ability to act in both of its physiological roles, electron transport and caspase activation PMID: 23334161 structural characterization of cytochrome c in micelle PMID: 23070294 Data indicate that the formation of cytochrome c-Apaf-1 apoptosome and the presence of Smac are absolutely required for PSAP-induced apoptosis. PMID: 23207240 Spectroscopic analyses of HCCS alone and complexes of HCCS with site-directed variants of cytochrome c revealed the fundamental steps of heme attachment and maturation. PMID: 23150584 The levels of cellular apoptosis-associated proteins such as Smac/DIABLO, Cyto C, and the activated fragment of caspase-3 increased in pancreatic cancer cells, but the expression of XIAP was significantly decreased after 24 h treatment with the combination of TRAIL and gemcitabine. PMID: 22320973 CCN1 promotes the activation of p53 and p38 MAPK, which mediate enhanced cytochrome c release to amplify the cytotoxicity of TNFalpha. PMID: 22363611 Translocation of ARTS initiates a first wave of caspase activation leading to the subsequent release of additional mitochondrial factors, including cytochrome C and SMAC/Diablo. PMID: 21869827 Tyrosine phosphorylation turns alkaline transition into a biologically relevant process and makes human cytochrome c behave as an anti-apoptotic switch. PMID: 21706253 mitochondrial import and direct electron transfer from cytochrome c to Rac1 modulates mitochondrial H(2)O(2) production in alveolar macrophages pulmonary fibrosis. PMID: 22157762 Dynamic changes in cytochrome c distribution at the Raman band of 750 cm(-1) were observed after adding an apoptosis inducer to the cells. PMID: 22184220 Specific nitration of tyrosines 46 and 48 makes cytochrome c assemble a non-functional apoptosome. PMID: 22192356 Studies indicate that the CYCS mutation in TP Cargeegis a glycine 41 replacement by serine, which yields a cytochrome C variant with enhanced apoptotic pathway activity in vitro. PMID: 22102269 Data show that G-Rh2 and Bet A cooperated to induce Bax traslocation to mitochondria and cytochrome c release, and enhanced cleavage of caspase-8 and Bid. PMID: 21751259 Cerebrospinal fluid Bcl-2 and cytochrome C levels are elevated in adults after severe traumatic brain injury. PMID: 21448217 Resveratrol induces p53-independent, X-linked inhibitor of apoptosis protein (XIAP)-mediated Bax protein oligomerization on mitochondria to initiate cytochrome c release and caspase activation. PMID: 21712378 heme electronic structure change may ultimately be responsible for the enhanced proapoptotic activity of G41S mutated human cyt c PMID: 21192676 it is the specific nitration of solvent-exposed Tyr74 which enhances the peroxidase activity and blocks the ability of cytochrome c to activate caspase-9, thereby preventing the apoptosis signaling pathway PMID: 20227384 Data show that sorafenib initiated lethal apoptotic process through the release of cytochrome c and caspase 3/7 activation. PMID: 19770576 Serum LRG when bound to extracellular Cyt c that is released from apoptotic cells acts as a survival factor for lymphocytes and possibly other cells that are susceptible to the toxic effect of extracellular Cyt c. PMID: 19851871 NOA36/ZNF330 is translocated from the mitochondria to the cytoplasm when apoptosis is induced and that it contributes to cytochrome c release. PMID: 19895853 Membrane-associated XIAP induces mitochondrial outer membrane permeabilization leading to cytochrome c and Smac release, which is dependent on Bax and Bak. PMID: 19875445 galectin-3 is enriched in the mitochondria and prevents mitochondrial damage and cytochrome c release PMID: 11839755 non-rare allelic variants of the Cyt c protein are absent in the populations analyzed in this study PMID: 16934433 Mutation of human cytochrome c enhances the intrinsic apoptotic pathway and causes thrombocytopenia PMID: 18345000 MICS1 individually functions in mitochondrial morphology and cytochrome c release. PMID: 18417609 Serum cyto-c is a potent tumor marker as a predictor for malignant potential in several different types of cancer. PMID: 18825408 Both neurons and cancer cells strictly inhibit cytochrome c-mediated apoptosis by a mechanism dependent on glucose metabolism. PMID: 19029908 In 77 Italian patients with inherited thrombocytopenia and clinical and laboratory features similar to those of patients with the CYCS missense (Gly41Ser) mutation, no alterations of the open reading frame were identified. PMID: 19172527 there was no evidence of somatic mutations of CYTOCHROME C in the cancers PMID: 19404857 No difference in the serum level of cytochrome c was seen among the the groups of patients with type 2 diabetes, controls or in subjects with IGT. PMID: 19640329

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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