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Recombinant Human Sirtuin 2/SIRT2 Protein is a Human Full Length protein, in the 2 to 389 aa range, expressed in HEK 293, with >=95% purity, <= 0.005 EU/µg endotoxin level and suitable for SDS-PAGE, MS, HPLC.

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Purity

>=95% HPLC

Endotoxin level

<= 0.005 EU/µg

Expression system

HEK 293 cells

Tags

Tag free

Applications

SDS-PAGE, MS, HPLC

Biologically active

No

Actual molecular weight

43.1 kDa

Sequence

A E P D P S H P L E T Q A G K V Q E A Q D S D S D S E G G A A G G E A D M D F L R N L F S Q T L S L G S Q K E R L L D E L T L E G V A R Y M Q S E R C R R V I C L V G A G I S T S A G I P D F R S P S T G L Y D N L E K Y H L P Y P E A I F E I S Y F K K H P E P F F A L A K E L Y P G Q F K P T I C H Y F M R L L K D K G L L L R C Y T Q N I D T L E R I A G L E Q E D L V E A H G T F Y T S H C V S A S C R H E Y P L S W M K E K I F S E V T P K C E D C Q S L V K P D I V F F G E S L P A R F F S C M Q S D F L K V D L L L V M G T S L Q V Q P F A S L I S K A P L S T P R L L I N K E K A G Q S D P F L G M I M G L G G G M D F D S K K A Y R D V A W L G E C D Q G C L A L A E L L G W K K E L E D L V R R E H A S I D A Q S G A G V P N P S T S A S P K K S P P P A K D E A R T T E R E K P Q

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Reactivity data

Application
SDS-PAGE
Reactivity
Reacts
Dilution info
-
Notes

-

Application
MS
Reactivity
Reacts
Dilution info
-
Notes

-

Application
HPLC
Reactivity
Reacts
Dilution info
-
Notes

-

Images

Target data

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Recombinant Human Sirtuin 2/SIRT2 Protein is a Human Full Length protein, in the 2 to 389 aa range, expressed in HEK 293, with >=95% purity, <= 0.005 EU/µg endotoxin level and suitable for SDS-PAGE, MS, HPLC.

Key facts

Purity

>=95% HPLC

Endotoxin level

<= 0.005 EU/µg

Expression system

HEK 293 cells

Applications

SDS-PAGE, MS, HPLC

Predicted molecular weight

43.1 kDa

Amino acids

2 to 389

Sequence

A E P D P S H P L E T Q A G K V Q E A Q D S D S D S E G G A A G G E A D M D F L R N L F S Q T L S L G S Q K E R L L D E L T L E G V A R Y M Q S E R C R R V I C L V G A G I S T S A G I P D F R S P S T G L Y D N L E K Y H L P Y P E A I F E I S Y F K K H P E P F F A L A K E L Y P G Q F K P T I C H Y F M R L L K D K G L L L R C Y T Q N I D T L E R I A G L E Q E D L V E A H G T F Y T S H C V S A S C R H E Y P L S W M K E K I F S E V T P K C E D C Q S L V K P D I V F F G E S L P A R F F S C M Q S D F L K V D L L L V M G T S L Q V Q P F A S L I S K A P L S T P R L L I N K E K A G Q S D P F L G M I M G L G G G M D F D S K K A Y R D V A W L G E C D Q G C L A L A E L L G W K K E L E D L V R R E H A S I D A Q S G A G V P N P S T S A S P K K S P P P A K D E A R T T E R E K P Q

Accession
Q8IXJ6-1
Protein length

Full Length

Animal free

Yes

Carrier free

Yes

Nature

Recombinant

Species

Human

Reconstitution

Store lyophilized form at room temperature. Reconstitute in PBS, aliquot and store at -80°C for 12 months or +4°C for 1 week. Avoid repeated freeze-thaw. Lyophilized contents may appear as either a translucent film or a white powder. This variance does not affect the quality of the product.

Concentration
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Storage buffer

pH: 7.4
Constituents: 10.26% Trehalose, 0.727% Dibasic monohydrogen potassium phosphate, 0.248% Potassium phosphate monobasic

Specifications

Form

Lyophilized

General info

Function

NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and alpha-tubulin as well as many other proteins such as key transcription factors (PubMed:24177535, PubMed:12620231, PubMed:16648462, PubMed:18249187, PubMed:18332217, PubMed:18995842, PubMed:20587414, PubMed:21081649, PubMed:20543840, PubMed:22014574, PubMed:21726808, PubMed:21949390, PubMed:22771473, PubMed:23468428, PubMed:23908241, PubMed:24940000, PubMed:24769394, PubMed:24681946). Participates in the modulation of multiple and diverse biological processes such as cell cycle control, genomic integrity, microtubule dynamics, cell differentiation, metabolic networks, and autophagy. Plays a major role in the control of cell cycle progression and genomic stability. Functions in the antephase checkpoint preventing precocious mitotic entry in response to microtubule stress agents, and hence allowing proper inheritance of chromosomes. Positively regulates the anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase complex activity by deacetylating CDC20 and FZR1, then allowing progression through mitosis. Associates both with chromatin at transcriptional start sites (TSSs) and enhancers of active genes. Plays a role in cell cycle and chromatin compaction through epigenetic modulation of the regulation of histone H4 'Lys-20' methylation (H4K20me1) during early mitosis. Specifically deacetylates histone H4 at 'Lys-16' (H4K16ac) between the G2/M transition and metaphase enabling H4K20me1 deposition by KMT5A leading to ulterior levels of H4K20me2 and H4K20me3 deposition throughout cell cycle, and mitotic S-phase progression (PubMed:23468428). Deacetylates KMT5A modulating KMT5A chromatin localization during the mitotic stress response (PubMed:23468428). Deacetylates also histone H3 at 'Lys-57' (H3K56ac) during the mitotic G2/M transition. Upon bacterium Listeria monocytogenes infection, deacetylates 'Lys-18' of histone H3 in a receptor tyrosine kinase MET- and PI3K/Akt-dependent manner, thereby inhibiting transcriptional activity and promoting late stages of listeria infection (PubMed:23908241). During oocyte meiosis progression, may deacetylate histone H4 at 'Lys-16' (H4K16ac) and alpha-tubulin, regulating spindle assembly and chromosome alignment by influencing microtubule dynamics and kinetochore function. Deacetylates histone H4 at 'Lys-16' (H4K16ac) at the VEGFA promoter and thereby contributes to regulate expression of VEGFA, a key regulator of angiogenesis (PubMed:24940000). Deacetylates alpha-tubulin at 'Lys-40' and hence controls neuronal motility, oligodendroglial cell arbor projection processes and proliferation of non-neuronal cells. Phosphorylation at Ser-368 by a G1/S-specific cyclin E-CDK2 complex inactivates SIRT2-mediated alpha-tubulin deacetylation, negatively regulating cell adhesion, cell migration and neurite outgrowth during neuronal differentiation. Deacetylates PARD3 and participates in the regulation of Schwann cell peripheral myelination formation during early postnatal development and during postinjury remyelination. Involved in several cellular metabolic pathways. Plays a role in the regulation of blood glucose homeostasis by deacetylating and stabilizing phosphoenolpyruvate carboxykinase PCK1 activity in response to low nutrient availability. Acts as a key regulator in the pentose phosphate pathway (PPP) by deacetylating and activating the glucose-6-phosphate G6PD enzyme, and therefore, stimulates the production of cytosolic NADPH to counteract oxidative damage. Maintains energy homeostasis in response to nutrient deprivation as well as energy expenditure by inhibiting adipogenesis and promoting lipolysis. Attenuates adipocyte differentiation by deacetylating and promoting FOXO1 interaction to PPARG and subsequent repression of PPARG-dependent transcriptional activity. Plays a role in the regulation of lysosome-mediated degradation of protein aggregates by autophagy in neuronal cells. Deacetylates FOXO1 in response to oxidative stress or serum deprivation, thereby negatively regulating FOXO1-mediated autophagy (PubMed:20543840). Deacetylates a broad range of transcription factors and co-regulators regulating target gene expression. Deacetylates transcriptional factor FOXO3 stimulating the ubiquitin ligase SCF(SKP2)-mediated FOXO3 ubiquitination and degradation (By similarity). Deacetylates HIF1A and therefore promotes HIF1A degradation and inhibition of HIF1A transcriptional activity in tumor cells in response to hypoxia (PubMed:24681946). Deacetylates RELA in the cytoplasm inhibiting NF-kappaB-dependent transcription activation upon TNF-alpha stimulation. Inhibits transcriptional activation by deacetylating p53/TP53 and EP300 (PubMed:18249187). Deacetylates also EIF5A (PubMed:22771473). Functions as a negative regulator on oxidative stress-tolerance in response to anoxia-reoxygenation conditions. Plays a role as tumor suppressor (PubMed:22014574).

Sequence similarities

Belongs to the sirtuin family. Class I subfamily.

Post-translational modifications

Phosphorylated at phosphoserine and phosphothreonine. Phosphorylated at Ser-368 by a mitotic kinase CDK1/cyclin B at the G2/M transition; phosphorylation regulates the delay in cell-cycle progression. Phosphorylated at Ser-368 by a mitotic kinase G1/S-specific cyclin E/Cdk2 complex; phosphorylation inactivates SIRT2-mediated alpha-tubulin deacetylation and thereby negatively regulates cell adhesion, cell migration and neurite outgrowth during neuronal differentiation. Phosphorylated by cyclin A/Cdk2 and p35-Cdk5 complexes and to a lesser extent by the cyclin D3/Cdk4 and cyclin B/Cdk1, in vitro. Dephosphorylated at Ser-368 by CDC14A and CDC14B around early anaphase.

Subcellular localisation

Nucleus, Cytoskeleton, Microtubule organizing center, Centrosome, Centriole, Spindle

Storage

Shipped at conditions

Ambient - Can Ship with Ice

Appropriate long-term storage conditions

Ambient

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Product protocols

For this product, it's our understanding that no specific protocols are required. You can:

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