An efficient proteomics method to identify the cellular targets of protein kinase inhibitors.

Small molecule inhibitors of protein kinases are extensively utilized in sign transduction analysis and are rising as a significant class of medication. Though interpretation of organic outcomes obtained with these reagents critically is determined by their selectivity, environment friendly strategies for proteome-wide evaluation of kinase inhibitor selectivity haven’t but been reported.
Right here, we handle this vital problem and describe a way for figuring out targets of the extensively used p38 kinase inhibitor SB 203580. Immobilization of an acceptable SB 203580 analogue and totally optimized biochemical situations for affinity chromatography permitted the dramatic enrichment and identification of a number of beforehand unknown protein kinase targets of SB 203580.
In vitro kinase assays confirmed that cyclin G-associated kinase (GAK) and CK1 have been nearly as potently inhibited as p38alpha whereas RICK [Rip-like interacting caspase-like apoptosis-regulatory protein (CLARP) kinase/Rip2/CARDIAK] was much more delicate to inhibition by SB 203580. The mobile kinase exercise of RICK, a recognized sign transducer of inflammatory responses, was already inhibited by submicromolar concentrations of SB 203580 in intact cells.
Due to this fact, our outcomes warrant a reevaluation of the huge quantity of knowledge obtained with SB 203580 and may need important implications on the event of p38 inhibitors as antiinflammatory medicine. Primarily based on the procedures described right here, environment friendly affinity purification methods might be developed for different protein kinase inhibitors, offering essential details about their mobile modes of motion.
The immunological processes concerned within the collaborative defence of organisms are affected by dietary standing. Thus, a optimistic continual imbalance between power consumption and expenditure results in conditions of weight problems, which can affect unspecific and particular immune responses mediated by humoral and cell mediated mechanisms.
Moreover, a number of traces of proof have supported a hyperlink between adipose tissue and immunocompetent cells. This interplay is illustrated in weight problems, the place extra adiposity and impaired immune perform have been described in each people and genetically overweight rodents.
Nevertheless, restricted and sometimes controversial info exist evaluating immunity in overweight and non-obese topics in addition to concerning the mobile and molecular mechanisms implicated. Normally phrases, scientific and epidemiological knowledge assist the proof that the incidence and severity of particular forms of infectious diseases are increased in overweight individuals as in comparison with lean people along with the incidence of poor antibody responses to antigens in obese topics.
Leptin would possibly play a key function in linking dietary standing with T-cell perform. The complexities and heterogeneity of the host defences in regards to the immune response in several dietary circumstances affecting the power steadiness require an integral examine of the immunocompetent cells, their subsets and merchandise in addition to particular and unspecific inducer/regulator techniques. On this context, extra analysis is required to make clear the scientific implications of the alterations induced by weight problems on the immune perform.

Runx1 is required for zebrafish blood and vessel growth and expression of a human RUNX1-CBF2T1 transgene advances a mannequin for research of leukemogenesis.

RUNX1/AML1/CBFA2 is important for definitive hematopoiesis, and chromosomal translocations affecting RUNX1 are incessantly concerned in human leukemias. Consequently, the traditional perform of RUNX1 and its involvement in leukemogenesis stay topic to intensive analysis.
To additional elucidate the function of RUNX1 in hematopoiesis, we cloned the zebrafish ortholog (runx1) and analyzed its perform utilizing this mannequin system. Zebrafish runx1 is expressed in hematopoietic and neuronal cells throughout early embryogenesis. runx1 expression within the lateral plate mesoderm co-localizes with the hematopoietic transcription issue scl, and expression of runx1 is markedly diminished within the zebrafish mutants spadetail and cloche.
Transient expression of runx1 in cloche embryos resulted in partial rescue of the hematopoietic defect. Depletion of Runx1 with antisense morpholino oligonucleotides abrogated the event of each blood and vessels, as demonstrated by lack of circulation, incomplete growth of vasculature and the buildup of immature hematopoietic precursors.
The block in definitive hematopoiesis is just like that noticed in Runx1 knockout mice, implying that zebrafish Runx1 has a perform equal to that in mammals. Our knowledge counsel that zebrafish Runx1 capabilities in each blood and vessel growth on the hemangioblast degree, and contributes to each primitive and definitive hematopoiesis. Depletion of Runx1 additionally induced aberrant axonogenesis and irregular distribution of Rohon-Beard cells, offering the primary practical proof of a task for vertebrate Runx1 in neuropoiesis.
To offer a base for analyzing the function of Runx1 in leukemogenesis, we investigated the results of transient expression of a human RUNX1-CBF2T1 transgene [product of the t(8;21) translocation in acute myeloid leukemia] in zebrafish embryos.
Expression of RUNX1-CBF2T1 induced disruption of regular hematopoiesis, aberrant circulation, inside hemorrhages and mobile dysplasia. These defects reproduce these noticed in Runx1-depleted zebrafish embryos and RUNX1-CBF2T1 knock-in mice. The phenotype obtained with transient expression of RUNX1-CBF2T1 validates the zebrafish as a mannequin system to check t(8;21)-mediated leukemogenesis.

From in vivo to in silico biology and again.

The large acquisition of knowledge in molecular and mobile biology has led to the renaissance of an outdated matter: simulations of organic techniques. Simulations, more and more paired with experiments, are being efficiently and routinely utilized by computational biologists to know and predict the quantitative behaviour of complicated techniques, and to drive new experiments.
However, many experimentalists nonetheless think about simulations an esoteric self-discipline just for initiates. Suspicion in the direction of simulations ought to dissipate as the restrictions and benefits of their utility are higher appreciated, opening the door to their everlasting adoption in on a regular basis analysis.

Proteome-wide evaluation of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.

Submit-translational modification of proteins by lysine acetylation performs vital regulatory roles in residing cells. The budding yeast Saccharomyces cerevisiae is a extensively used unimobile eukaryotic mannequin organism in biomedical analysis.
S. cerevisiae accommodates a number of evolutionary conserved lysine acetyltransferases and deacetylases. Nevertheless, just a few dozen acetylation websites in S. cerevisiae are recognized, presenting a significant impediment for additional understanding the regulatory roles of acetylation on this organism.
An efficient proteomics method to identify the cellular targets of protein kinase inhibitors.
Right here we use excessive decision mass spectrometry to determine about 4000 lysine acetylation websites in S. cerevisiae. Acetylated proteins are implicated within the regulation of numerous cytoplasmic and nuclear processes together with chromatin group, mitochondrial metabolism, and protein synthesis.
Bioinformatic evaluation of yeast acetylation websites reveals that acetylated lysines are considerably extra conserved in contrast with nonacetylated lysines. A big fraction of the conserved acetylation websites are current on proteins concerned in mobile metabolism, protein synthesis, and protein folding. Moreover, quantification of the Rpd3-regulated acetylation websites recognized a number of beforehand recognized, in addition to new putative substrates of this deacetylase.

SOD1 (Superoxide Dismutase 1 (SOD1, Superoxide Dismutase, Cystolic, Superoxide Dismutase 1 Soluble, SOD Soluble, Cu/Zn Superoxide Dismutase) (FITC)

MBS6394765-01mL 0.1mL
EUR 920

SOD1 (Superoxide Dismutase 1 (SOD1, Superoxide Dismutase, Cystolic, Superoxide Dismutase 1 Soluble, SOD Soluble, Cu/Zn Superoxide Dismutase) (FITC)

MBS6394765-5x01mL 5x0.1mL
EUR 3990

SOD1 (Superoxide Dismutase 1 (SOD1, Superoxide Dismutase, Cystolic, Superoxide Dismutase 1 Soluble, SOD Soluble, Cu/Zn Superoxide Dismutase) (HRP)

MBS6394766-01mL 0.1mL
EUR 920

SOD1 (Superoxide Dismutase 1 (SOD1, Superoxide Dismutase, Cystolic, Superoxide Dismutase 1 Soluble, SOD Soluble, Cu/Zn Superoxide Dismutase) (HRP)

MBS6394766-5x01mL 5x0.1mL
EUR 3990

SOD1 (Superoxide Dismutase 1 (SOD1, Superoxide Dismutase, Cystolic, Superoxide Dismutase 1 Soluble, SOD Soluble, Cu/Zn Superoxide Dismutase) (PE)

MBS6394772-01mL 0.1mL
EUR 920

SOD1 (Superoxide Dismutase 1 (SOD1, Superoxide Dismutase, Cystolic, Superoxide Dismutase 1 Soluble, SOD Soluble, Cu/Zn Superoxide Dismutase) (PE)

MBS6394772-5x01mL 5x0.1mL
EUR 3990

SOD1 (Superoxide Dismutase 1 (SOD1, Superoxide Dismutase, Cystolic, Superoxide Dismutase 1 Soluble, SOD Soluble, Cu/Zn Superoxide Dismutase) (Biotin)

MBS6394764-01mL 0.1mL
EUR 920

SOD1 (Superoxide Dismutase 1 (SOD1, Superoxide Dismutase, Cystolic, Superoxide Dismutase 1 Soluble, SOD Soluble, Cu/Zn Superoxide Dismutase) (Biotin)

MBS6394764-5x01mL 5x0.1mL
EUR 3990

Superoxide Dismutase 3

SOD-003 100ug
EUR 1038.4
Description: Greater than 95%

SOD1 (Superoxide Dismutase 1 (SOD1, Superoxide Dismutase, Cystolic, Superoxide Dismutase 1 Soluble, SOD Soluble, Cu/Zn Superoxide Dismutase) (MaxLight 405)

MBS6394767-01mL 0.1mL
EUR 920

SOD1 (Superoxide Dismutase 1 (SOD1, Superoxide Dismutase, Cystolic, Superoxide Dismutase 1 Soluble, SOD Soluble, Cu/Zn Superoxide Dismutase) (MaxLight 405)

MBS6394767-5x01mL 5x0.1mL
EUR 3990

SOD1 (Superoxide Dismutase 1 (SOD1, Superoxide Dismutase, Cystolic, Superoxide Dismutase 1 Soluble, SOD Soluble, Cu/Zn Superoxide Dismutase) (MaxLight 490)

MBS6394768-01mL 0.1mL
EUR 920

SOD1 (Superoxide Dismutase 1 (SOD1, Superoxide Dismutase, Cystolic, Superoxide Dismutase 1 Soluble, SOD Soluble, Cu/Zn Superoxide Dismutase) (MaxLight 490)

MBS6394768-5x01mL 5x0.1mL
EUR 3990

SOD1 (Superoxide Dismutase 1 (SOD1, Superoxide Dismutase, Cystolic, Superoxide Dismutase 1 Soluble, SOD Soluble, Cu/Zn Superoxide Dismutase) (MaxLight 550)

MBS6394769-01mL 0.1mL
EUR 920

SOD1 (Superoxide Dismutase 1 (SOD1, Superoxide Dismutase, Cystolic, Superoxide Dismutase 1 Soluble, SOD Soluble, Cu/Zn Superoxide Dismutase) (MaxLight 550)

MBS6394769-5x01mL 5x0.1mL
EUR 3990

SOD1 (Superoxide Dismutase 1 (SOD1, Superoxide Dismutase, Cystolic, Superoxide Dismutase 1 Soluble, SOD Soluble, Cu/Zn Superoxide Dismutase) (MaxLight 650)

MBS6394770-01mL 0.1mL
EUR 920

SOD1 (Superoxide Dismutase 1 (SOD1, Superoxide Dismutase, Cystolic, Superoxide Dismutase 1 Soluble, SOD Soluble, Cu/Zn Superoxide Dismutase) (MaxLight 650)

MBS6394770-5x01mL 5x0.1mL
EUR 3990

SOD1 (Superoxide Dismutase 1 (SOD1, Superoxide Dismutase, Cystolic, Superoxide Dismutase 1 Soluble, SOD Soluble, Cu/Zn Superoxide Dismutase) (MaxLight 750)

MBS6394771-01mL 0.1mL
EUR 920

SOD1 (Superoxide Dismutase 1 (SOD1, Superoxide Dismutase, Cystolic, Superoxide Dismutase 1 Soluble, SOD Soluble, Cu/Zn Superoxide Dismutase) (MaxLight 750)

MBS6394771-5x01mL 5x0.1mL
EUR 3990

Superoxide Dismutase 3 antibody

10R-7477 100 ul
EUR 471.6
Description: Mouse monoclonal Superoxide Dismutase 3 antibody

Superoxide dismutase

44R-1105 1 MU Ask for price
Description: Superoxide dismutase enzyme

Superoxide Dismutase 3, mouse

LF-P0418 0.5mg
EUR 363.6
Description: Superoxide Dismutase 3, mouse protein

Superoxide Dismutase 3 [Cys0] (33-54) (Superoxide Dismutase 3 Extracellular, SOD 3, SOD3, Extracellular Superoxide Dismutase [Cu Zn], EC SOD, EC-SOD, MGC20077)

MBS6001542-02mg 0.2(mg
EUR 1105

Superoxide Dismutase 3 [Cys0] (33-54) (Superoxide Dismutase 3 Extracellular, SOD 3, SOD3, Extracellular Superoxide Dismutase [Cu Zn], EC SOD, EC-SOD, MGC20077)

MBS6001542-5x02mg 5x0.2mg
EUR 4830

Superoxide Dismutase 3 [Cys0] (33-54) (Superoxide Dismutase 3 Extracellular, SOD 3, SOD3, Extracellular Superoxide Dismutase [Cu Zn], EC SOD, EC-SOD, MGC20077) (Biotin)

MBS644956-01mL 0.1mL
EUR 1220

Superoxide Dismutase 3 [Cys0] (33-54) (Superoxide Dismutase 3 Extracellular, SOD 3, SOD3, Extracellular Superoxide Dismutase [Cu Zn], EC SOD, EC-SOD, MGC20077) (Biotin)

MBS644956-5x01mL 5x0.1mL
EUR 5345

Superoxide Dismutase, Cu,Zn (Superoxide Dismutase [Cu-Zn], SOD Cu,Zn, SOD1)

MBS6010735-01mg 0.1(mg
EUR 615

Superoxide Dismutase, Cu,Zn (Superoxide Dismutase [Cu-Zn], SOD Cu,Zn, SOD1)

MBS6010735-5x01mg 5x0.1mg
EUR 2605

Superoxide Dismutase 3 Antibody (SOD3)

F49928-0.08ML 0.08 ml
EUR 140.25
Description: SOD3 is a member of the superoxide dismutase(SOD) protein family. SODs are antioxidant enzymes that catalyze the dismutation of two superoxide radicals into hydrogen peroxide and oxygen. This protein is thought to protect the brain, lungs, and other tissues from oxidative stress. The protein is secreted into the extracellular space and forms a glycosylated homotetramer that is anchored to the extracellular matrix (ECM) and cell surfaces through an interaction with heparan sulfate proteoglycan and collagen. A fraction of the protein is cleaved near the C-terminus before secretion to generate circulating tetramers that do not interact with the ECM.

Superoxide Dismutase 3 Antibody (SOD3)

F52953-0.08ML 0.08 ml
EUR 140.25
Description: SOD3 protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen.

SOD3 Antibody / Superoxide Dismutase 3

R30999 100 ug
EUR 356.15
Description: Superoxide Dismutase 3 is an enzyme that in humans is encoded by the SOD3 gene. This gene encodes a member of the superoxide dismutase (SOD) protein family. SODs are antioxidant enzymes that catalyze the dismutation of two superoxide radicals into hydrogen peroxide and oxygen. Hendrickson et al.(1990) mapped the SOD3 gene to 4pter-q21 by a study of somatic cell hybrids. Stern et al.(2003) narrowed the assignment to 4p15.3-p15.1 by somatic cell and radiation hybrid analysis, linkage mapping, and FISH. The product of this gene is though to protect the brain, lungs, and other tissues from oxidative stress. The protein is secreted into the extracellular space and forms a glycosylated homotetramer that is anchored to the extracellular matrix(ECM) and cell surfaces through an interaction with heparan sulfate proteoglycan and collagen. A fraction of the protein is cleaved near the C-terminus before secretion to generate circulating tetramers that do not interact with the ECM.

Superoxide Dismutase 3 Antibody / SOD3

R31796 100 ug
EUR 356.15
Description: SOD3 (SUPEROXIDE DISMUTASE 3), also called SUPEROXIDE DISMUTASE, EXTRACELLULAR, EC-SOD, and Cu-Zn, is an enzyme that in humans is encoded by the SOD3 gene. This gene encodes a member of the superoxide dismutase (SOD) protein family. SODs are antioxidant enzymes that catalyze the dismutation of two superoxide radicals into hydrogen peroxide and oxygen. Hendrickson et al. (1990) mapped the SOD3 gene to 4pter-q21 by a study of somatic cell hybrids. Stern et al. (2003) narrowed the assignment to 4p15.3-p15.1 by somatic cell and radiation hybrid analysis, linkage mapping, and FISH. The product of this gene is thought to protect the brain, lungs, and other tissues from oxidative stress. The protein is secreted into the extracellular space and forms a glycosylated homotetramer that is anchored to the extracellular matrix (ECM) and cell surfaces through an interaction with heparan sulfate proteoglycan and collagen. A fraction of the protein is cleaved near the C-terminus before secretion to generate circulating tetramers that do not interact with the ECM.

Superoxide dismutase 3 Antibody / Sod3

RQ6518 100ug
EUR 356.15
Description: SOD3 (SUPEROXIDE DISMUTASE 3), also called SUPEROXIDE DISMUTASE, EXTRACELLULAR, EC-SOD, and Cu-Zn, is an enzyme that in humans is encoded by the SOD3 gene. This gene encodes a member of the superoxide dismutase (SOD) protein family. SODs are antioxidant enzymes that catalyze the dismutation of two superoxide radicals into hydrogen peroxide and oxygen. Hendrickson et al. (1990) mapped the SOD3 gene to 4pter-q21 by a study of somatic cell hybrids. Stern et al. (2003) narrowed the assignment to 4p15.3-p15.1 by somatic cell and radiation hybrid analysis, linkage mapping, and FISH. The product of this gene is thought to protect the brain, lungs, and other tissues from oxidative stress. The protein is secreted into the extracellular space and forms a glycosylated homotetramer that is anchored to the extracellular matrix (ECM) and cell surfaces through an interaction with heparan sulfate proteoglycan and collagen. A fraction of the protein is cleaved near the C-terminus before secretion to generate circulating tetramers that do not interact with the ECM.

Superoxide Dismutase 3 Antibody / SOD3

RQ4091 100 ug
EUR 356.15
Description: SOD3 (Superoxide Dismutase 3), also called Superoxide Dismutase extracellular, EC-SOD, and Cu-Zn, is an enzyme that in humans is encoded by the SOD3 gene. This gene encodes a member of the superoxide dismutase (SOD) protein family. SODs are antioxidant enzymes that catalyze the dismutation of two superoxide radicals into hydrogen peroxide and oxygen. Hendrickson et al. (1990) mapped the SOD3 gene to 4pter-q21 by a study of somatic cell hybrids. Stern et al. (2003) narrowed the assignment to 4p15.3-p15.1 by somatic cell and radiation hybrid analysis, linkage mapping, and FISH. The product of this gene is thought to protect the brain, lungs, and other tissues from oxidative stress. The protein is secreted into the extracellular space and forms a glycosylated homotetramer that is anchored to the extracellular matrix (ECM) and cell surfaces through an interaction with heparan sulfate proteoglycan and collagen. A fraction of the protein is cleaved near the C-terminus before secretion to generate circulating tetramers that do not interact with the ECM.

Superoxide Dismutase 3 (SOD3) Antibody

abx115903-100g 100 µg Ask for price

Superoxide Dismutase 3 (SOD3) Antibody

abx115903-10g 10 µg
EUR 612.5

Superoxide Dismutase 3 (SOD3) Antibody

abx115903-200g 200 µg Ask for price

Superoxide Dismutase 3 (SOD3) Antibody

abx129985-100l 100 µl
EUR 262.5

Superoxide Dismutase 3 (SOD3) Antibody

abx129985-1ml 1 ml
EUR 725

Superoxide Dismutase 3 (SOD3) Antibody

abx129985-200l 200 µl
EUR 337.5

Superoxide Dismutase 3 (SOD3) Antibody

abx174663-1ml 1 ml
EUR 262.5

Superoxide Dismutase 3 (SOD3) Antibody

abx174664-100l 100 µl
EUR 775

Superoxide Dismutase 3 (SOD3) Antibody

abx174664-1ml 1 ml Ask for price

Superoxide Dismutase 3 (SOD3) Antibody

abx174664-200l 200 µl Ask for price

Superoxide Dismutase 3 (SOD3) Antibody

abx174665-100l 100 µl
EUR 775

Superoxide Dismutase 3 (SOD3) Antibody

abx174665-1ml 1 ml Ask for price

Superoxide Dismutase 3 (SOD3) Antibody

abx174665-200l 200 µl Ask for price

Superoxide Dismutase 3 (SOD3) Antibody

abx305397-100g 100 µg
EUR 362.5

Superoxide Dismutase 3 (SOD3) Antibody

abx305397-20g 20 µg
EUR 162.5

Superoxide Dismutase 3 (SOD3) Antibody

abx305397-50g 50 µg
EUR 250

Superoxide Dismutase 3 (SOD3) Antibody

abx033034-400l 400 µl
EUR 518.75

Superoxide Dismutase 3 (SOD3) Antibody

abx320304-100l 100 µl
EUR 350

Superoxide Dismutase 3 (SOD3) Antibody

abx320304-50l 50 µl
EUR 237.5

Superoxide Dismutase 3 (SOD3) Antibody

abx448432-1096tests 10 × 96 tests Ask for price

Superoxide Dismutase 3 (SOD3) Antibody

abx448432-596tests 5 × 96 tests Ask for price

Superoxide Dismutase 3 (SOD3) Antibody

abx448432-96tests 96 tests
EUR 537.5

Superoxide Dismutase 3 (SOD3) Antibody

abx005295-100l 100 µl
EUR 400

Superoxide Dismutase 3 (SOD3) Antibody

abx005295-20l 20 µl
EUR 175

Superoxide Dismutase 3 (SOD3) Antibody

abx005295-50l 50 µl
EUR 275

Superoxide Dismutase 3 (SOD3) Antibody

abx103950-100g 100 µg
EUR 675

Superoxide Dismutase 3 (SOD3) Antibody

abx103950-20g 20 µg
EUR 250

Superoxide Dismutase 3 (SOD3) Antibody

abx103950-50g 50 µg
EUR 312.5

Superoxide Dismutase 3 (SOD3) Antibody

abx103951-100g 100 µg
EUR 687.5

Superoxide Dismutase 3 (SOD3) Antibody

abx103951-20g 20 µg
EUR 262.5

Superoxide Dismutase 3 (SOD3) Antibody

abx103951-50g 50 µg
EUR 325

Superoxide Dismutase 3 (SOD3) Antibody

abx103952-100g 100 µg
EUR 725

Superoxide Dismutase 3 (SOD3) Antibody

abx103952-20g 20 µg
EUR 262.5

Superoxide Dismutase 3 (SOD3) Antibody

abx103952-50g 50 µg
EUR 337.5

Rabbit anti Bovine Superoxide dismutase

MBS573153-1mg 1mg
EUR 715

Rabbit anti Bovine Superoxide dismutase

MBS573153-5x1mg 5x1mg
EUR 3080

Rabbit anti Bovine Superoxide dismutase

MBS573613-10mg 10mg
EUR 325

Rabbit anti Bovine Superoxide dismutase

MBS573613-5x10mg 5x10mg
EUR 1320

Superoxide Dismutase Antibody

abx021109-1mg 1 mg
EUR 1111.2

Superoxide Dismutase Antibody

abx022850-1ml 1 ml
EUR 1053.6

Superoxide Dismutase Antibody

GWB-F8DC97 1 ml Ask for price

Superoxide Dismutase 1

E8ET1702-36 100ul
EUR 275
Description: Available in various conjugation types.

Superoxide Dismutase 1

MBS8534344-01mL 0.1mL
EUR 345

Superoxide Dismutase 1

MBS8534344-01mLAF405L 0.1mL(AF405L)
EUR 565

Superoxide Dismutase 1

MBS8534344-01mLAF405S 0.1mL(AF405S)
EUR 565

Superoxide Dismutase 1

MBS8534344-01mLAF610 0.1mL(AF610)
EUR 565

Superoxide Dismutase 1

MBS8534344-01mLAF635 0.1mL(AF635)
EUR 565

Superoxide Dismutase 1

SOD-002 100ug
EUR 1038.4
Description: Greater than 95%

Mouse Anti Human Superoxide Dismutase-1

MBS146663-0005mg 0.005mg
EUR 240

Mouse Anti Human Superoxide Dismutase-1

MBS146663-002mg 0.02mg
EUR 310

Mouse Anti Human Superoxide Dismutase-1

MBS146663-01mg 0.1mg
EUR 610

Mouse Anti Human Superoxide Dismutase-1

MBS146663-5x01mg 5x0.1mg
EUR 2405

MOUSE ANTI SUPEROXIDE DISMUTASE (Cu-Zn)

MBS212905-01mg 0.1mg
EUR 515

MOUSE ANTI SUPEROXIDE DISMUTASE (Cu-Zn)

MBS212905-5x01mg 5x0.1mg
EUR 2145

Superoxide Dismutase 3 [Cys0] (33-54) (Superoxide Dismutase 3 Extracellular, SOD 3, SOD3, Extracellular Superoxide Dismutase [Cu Zn], EC SOD, EC-SOD, MGC20077) (Carboxyfluorescein)

MBS643479-01mL 0.1mL
EUR 1220

Superoxide Dismutase 3 [Cys0] (33-54) (Superoxide Dismutase 3 Extracellular, SOD 3, SOD3, Extracellular Superoxide Dismutase [Cu Zn], EC SOD, EC-SOD, MGC20077) (Carboxyfluorescein)

MBS643479-5x01mL 5x0.1mL
EUR 5345

Superoxide Dismutase 3 Rabbit pAb

E2382024 100ul
EUR 225
Description: Available in various conjugation types.

Superoxide Dismutase 3 Rabbit mAb

56236 100ul
EUR 339

Superoxide Dismutase 3 Rabbit mAb

E2R382024 100ul
EUR 275
Description: Biotin-Conjugated, FITC-Conjugated , AF350 Conjugated , AF405M-Conjugated ,AF488-Conjugated, AF514-Conjugated ,AF532-Conjugated, AF555-Conjugated ,AF568-Conjugated , HRP-Conjugated, AF405S-Conjugated, AF405L-Conjugated , AF546-Conjugated, AF594-Conjugated , AF610-Conjugated, AF635-Conjugated , AF647-Conjugated , AF680-Conjugated , AF700-Conjugated , AF750-Conjugated , AF790-Conjugated , APC-Conjugated , PE-Conjugated , Cy3-Conjugated , Cy5-Conjugated , Cy5.5-Conjugated , Cy7-Conjugated Antibody

Superoxide Dismutase 3 Rabbit pAb

MBS8543488-01mL 0.1mL
EUR 305

Superoxide Dismutase 3 Rabbit pAb

MBS8543488-01mLAF405L 0.1mL(AF405L)
EUR 565

Superoxide Dismutase 3 Rabbit pAb

MBS8543488-01mLAF405S 0.1mL(AF405S)
EUR 565

Superoxide Dismutase 3 Rabbit pAb

MBS8543488-01mLAF610 0.1mL(AF610)
EUR 565

Superoxide Dismutase 3 Rabbit pAb

MBS8543488-01mLAF635 0.1mL(AF635)
EUR 565

Superoxide Dismutase, Mn (Manganese Superoxide Dismutase, Manganese SOD, Mn SOD, MnSOD, IPO-B, Superoxide Dismutase [Mn] Mitochondrial Precursor, Superoxide Dismutase 2 Mitochondrial, SOD 2, SOD2, SOD-2)

MBS623319-01mL 0.1mL
EUR 665

Superoxide Dismutase, Mn (Manganese Superoxide Dismutase, Manganese SOD, Mn SOD, MnSOD, IPO-B, Superoxide Dismutase [Mn] Mitochondrial Precursor, Superoxide Dismutase 2 Mitochondrial, SOD 2, SOD2, SOD-2)

MBS623319-5x01mL 5x0.1mL
EUR 2850

Superoxide Dismutase, Cu,Zn (Superoxide Dismutase Cu/Zn, SOD Cu,Zn, Cu/Zn SOD, Amyotrophic Lateral Sclerosis 1, ALS1, ALS, Homodimer, Indophenoloxidase A, IPOA, Superoxide Dismutase 1, Superoxide Dismutase 1 Soluble, SOD1, SOD-1, Superoxide Dismutase Cyst

MBS619705-01mL 0.1mL
EUR 650

Superoxide Dismutase, Cu,Zn (Superoxide Dismutase Cu/Zn, SOD Cu,Zn, Cu/Zn SOD, Amyotrophic Lateral Sclerosis 1, ALS1, ALS, Homodimer, Indophenoloxidase A, IPOA, Superoxide Dismutase 1, Superoxide Dismutase 1 Soluble, SOD1, SOD-1, Superoxide Dismutase Cyst

MBS619705-5x01mL 5x0.1mL
EUR 2780

Superoxide Dismutase, Cu,Zn (Superoxide Dismutase Cu/Zn, SOD Cu,Zn, Cu/Zn SOD, Amyotrophic Lateral Sclerosis 1, ALS1, ALS, Homodimer, Indophenoloxidase A, IPOA, Superoxide Dismutase 1, Superoxide Dismutase 1 Soluble, SOD1, SOD-1, Superoxide Dismutase Cyst

MBS620361-01mL 0.1mL
EUR 650

Superoxide Dismutase, Cu,Zn (Superoxide Dismutase Cu/Zn, SOD Cu,Zn, Cu/Zn SOD, Amyotrophic Lateral Sclerosis 1, ALS1, ALS, Homodimer, Indophenoloxidase A, IPOA, Superoxide Dismutase 1, Superoxide Dismutase 1 Soluble, SOD1, SOD-1, Superoxide Dismutase Cyst

MBS620361-5x01mL 5x0.1mL
EUR 2780

Superoxide Dismutase, Cu,Zn (Superoxide Dismutase Cu/Zn, SOD Cu,Zn, Cu/Zn SOD, Amyotrophic Lateral Sclerosis 1, ALS1, ALS, Homodimer, Indophenoloxidase A, IPOA, Superoxide Dismutase 1, Superoxide Dismutase 1 Soluble, SOD1, SOD-1, Superoxide Dismutase Cyst

MBS623222-01mL 0.1mL
EUR 650

Superoxide Dismutase, Cu,Zn (Superoxide Dismutase Cu/Zn, SOD Cu,Zn, Cu/Zn SOD, Amyotrophic Lateral Sclerosis 1, ALS1, ALS, Homodimer, Indophenoloxidase A, IPOA, Superoxide Dismutase 1, Superoxide Dismutase 1 Soluble, SOD1, SOD-1, Superoxide Dismutase Cyst

MBS623222-5x01mL 5x0.1mL
EUR 2780

Human Superoxide Dismutase

90240-A 20 µg
EUR 130
Description: SOD is a disulfide-linked homodimeric protein consisting of two 154 amino acid residues, and migrates as an approximately 31 kDa protein under non-reducing and as 16 kDa under reducing conditions in SDS-PAGE. Optimized DNA sequence encoding Human Superoxide Dismutase mature chain was expressed in E. coli.

Human Superoxide Dismutase

90240-B 100 µg
EUR 205
Description: SOD is a disulfide-linked homodimeric protein consisting of two 154 amino acid residues, and migrates as an approximately 31 kDa protein under non-reducing and as 16 kDa under reducing conditions in SDS-PAGE. Optimized DNA sequence encoding Human Superoxide Dismutase mature chain was expressed in E. coli.

Human Superoxide Dismutase

MBS430265-01mg 0.1mg
EUR 255

Human Superoxide Dismutase

MBS430265-5x01mg 5x0.1mg
EUR 990

Bovine Superoxide Dismutase

IBOSODLY10MG each
EUR 274
Description: Bovine Superoxide Dismutase

Bovine Superoxide Dismutase

IBOSODLY2MG each
EUR 96
Description: Bovine Superoxide Dismutase

Superoxide Dismutase 3 (SOD3) Antibody (PE)

abx444263-100g 100 µg
EUR 600

Superoxide Dismutase 3 (SOD3) Antibody (PE)

abx446278-100g 100 µg
EUR 637.5

Superoxide Dismutase protein

30R-2714 100 ug
EUR 434
Description: Purified recombinant Human Superoxide Dismutase protein

Superoxide Dismutase 3 (SOD3) Antibody (HRP)

abx305398-100g 100 µg
EUR 362.5

Superoxide Dismutase 3 (SOD3) Antibody (HRP)

abx305398-20g 20 µg
EUR 162.5

Superoxide Dismutase 3 (SOD3) Antibody (HRP)

abx305398-50g 50 µg
EUR 250

Superoxide Dismutase 3 (SOD3) Antibody (APC)

abx442579-100g 100 µg
EUR 600

Superoxide Dismutase 3 (SOD3) Antibody (HRP)

abx443420-100l 100 µl
EUR 587.5

Superoxide Dismutase 3 (SOD3) Antibody (APC)

abx446272-100g 100 µg
EUR 650

Superoxide Dismutase 3 (SOD3) Antibody (HRP)

abx446275-100g 100 µg
EUR 625

CCS (Copper Chaperone for Superoxide Dismutase, Superoxide Dismutase Copper Chaperone) APC

MBS6135716-01mL 0.1(mL
EUR 875

CCS (Copper Chaperone for Superoxide Dismutase, Superoxide Dismutase Copper Chaperone) APC

MBS6135716-5x01mL 5x0.1mL
EUR 3800

CCS (Copper Chaperone for Superoxide Dismutase, Superoxide Dismutase Copper Chaperone) (AP)

MBS6130413-01mL 0.1(mL
EUR 875

CCS (Copper Chaperone for Superoxide Dismutase, Superoxide Dismutase Copper Chaperone) (AP)

MBS6130413-5x01mL 5x0.1mL
EUR 3800
Rpd3 deficiency elevated acetylation of the SAGA (Spt-Ada-Gcn5-Acetyltransferase) complicated subunit Sgf73 on Okay33. This acetylation website is situated inside a crucial regulatory area in Sgf73 that interacts with Ubp8 and is concerned within the activation of the Ubp8-containing histone H2B deubiquitylase complicated. Our knowledge supplies the primary world survey of acetylation in budding yeast, and suggests a wide-ranging regulatory scope of this modification. The offered knowledgeset might function an vital useful resource for the practical evaluation of lysine acetylation in eukaryotes.

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