Recombinant Human Serine/threonine-protein kinase BRSK2 (BRSK2)

Code CSB-YP815566HU
MSDS
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Source Yeast
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Code CSB-EP815566HU
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Source E.coli
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Code CSB-EP815566HU-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP815566HU
MSDS
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Source Baculovirus
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Code CSB-MP815566HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
BRSK2
Uniprot No.
Alternative Names
BRSK2; C11orf7; PEN11B; SADA; STK29; HUSSY-12; Serine/threonine-protein kinase BRSK2; EC 2.7.11.1; Brain-selective kinase 2; EC 2.7.11.26; Brain-specific serine/threonine-protein kinase 2; BR serine/threonine-protein kinase 2; Serine/threonine-protein kinase 29; Serine/threonine-protein kinase SAD-A
Species
Homo sapiens (Human)
Expression Region
1-736
Target Protein Sequence
MTSTGKDGGA QHAQYVGPYR LEKTLGKGQT GLVKLGVHCV TCQKVAIKIV NREKLSESVL MKVEREIAIL KLIEHPHVLK LHDVYENKKY LYLVLEHVSG GELFDYLVKK GRLTPKEARK FFRQIISALD FCHSHSICHR DLKPENLLLD EKNNIRIADF GMASLQVGDS LLETSCGSPH YACPEVIRGE KYDGRKADVW SCGVILFALL VGALPFDDDN LRQLLEKVKR GVFHMPHFIP PDCQSLLRGM IEVDAARRLT LEHIQKHIWY IGGKNEPEPE QPIPRKVQIR SLPSLEDIDP DVLDSMHSLG CFRDRNKLLQ DLLSEEENQE KMIYFLLLDR KERYPSQEDE DLPPRNEIDP PRKRVDSPML NRHGKRRPER KSMEVLSVTD GGSPVPARRA IEMAQHGQRS RSISGASSGL STSPLSSPRV TPHPSPRGSP LPTPKGTPVH TPKESPAGTP NPTPPSSPSV GGVPWRARLN SIKNSFLGSP RFHRRKLQVP TPEEMSNLTP ESSPELAKKS WFGNFISLEK EEQIFVVIKD KPLSSIKADI VHAFLSIPSL SHSVISQTSF RAEYKATGGP AVFQKPVKFQ VDITYTEGGE AQKENGIYSV TFTLLSGPSR RFKRVVETIQ AQLLSTHDPP AAQHLSDTTN CMEMMTGRLS KCGSPLSNFF DVIKQLFSDE KNGQAAQAPS TPAKRSAHGP LGDSAAAGPG PGGDAEYPTG KDTAKMGPPT ARREQP
Protein Length
full length protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Serine/threonine-protein kinase that plays a key role in polarization of neurons and axonogenesis, cell cycle progress and insulin secretion. Phosphorylates CDK16, CDC25C, MAPT/TAU, PAK1 and WEE1. Following phosphorylation and activation by STK11/LKB1, acts as a key regulator of polarization of cortical neurons, probably by mediating phosphorylation of microtubule-associated proteins such as MAPT/TAU at 'Thr-529' and 'Ser-579'. Also regulates neuron polarization by mediating phosphorylation of WEE1 at 'Ser-642' in postmitotic neurons, leading to down-regulate WEE1 activity in polarized neurons. Plays a role in the regulation of the mitotic cell cycle progress and the onset of mitosis. Plays a role in the regulation of insulin secretion in response to elevated glucose levels, probably via phosphorylation of CDK16 and PAK1. While BRSK2 phosphorylated at Thr-174 can inhibit insulin secretion, BRSK2 phosphorylated at Thr-260 can promote insulin secretion. Regulates reorganization of the actin cytoskeleton. May play a role in the apoptotic response triggered by endoplasmic reticulum (ER) stress.
Gene References into Functions
  1. the intrinsic molecular merit that BRSK2 provides is a survival advantage to PDAC cells and strengthens the invasiveness of these neoplastic cells in energy-deprived environments. PMID: 28591720
  2. SAD-A and AMPK kinases are regulators of mTORC1 signaling in the pancreatic beta-cells. PMID: 24047693
  3. BRSK2 interacted with VCP/p97 via three of the four functional domains of VCP/p97. Immunofluorescence demonstrated that BRSK2 and VCP/p97 were co-localized and also that knockdown of endogenous BRSK2 induced increased levels of CD3delta. PMID: 23907667
  4. Anaphase-promoting complex/cyclosome-Cdh1, rather than Cdc20, promotes the degradation of BRSK2 in vivo. PMID: 23029325
  5. a novel function of BRSK2 in the regulation of GSIS in beta-cells via a PCTAIRE1-dependent mechanism and suggest that BRSK2 is an attractive target for developing novel diabetic drugs. PMID: 22798068
  6. these findings demonstrate ER stress may reduce BRSK2 protein and change BRSK2 subcellular localization, which in turn alleviate ER stress-induced apoptosis. PMID: 22713462
  7. these findings provide a novel regulatory mechanism of BRSK2 through direct interaction with Jab1. PMID: 22609399
  8. BRSK2 is up-regulated in pancreatic ductal adenocarcinoma. PMID: 20646422
  9. BRSK2 may be an autoantigen involved in the pathogenesis of small-cell lung cancer-associated limbic encephalitis. PMID: 16165222
  10. we identified cAMP-dependent protein kinase A (PKA) as another upstream kinase of BRSK2, which can phosphorylate BRSK2 at Thr260. Kinase activity of BRSK2 can be increased through phosphorylation by PKA. PMID: 16870137
  11. protein phosphatase 2C is a likely candidate for catalyzing the dephosphorylation and inactivation of BRSK1/2. PMID: 18339622
  12. level of SAD within neurons is modulated by TORC1 PMID: 18794342
  13. STRADalpha.MO25alpha complexes containing LKB1 variants were equally effective at phosphorylating and activating AMPK, BRSK1, and BRSK2 PMID: 18854318

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Subcellular Location
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, perinuclear region. Endoplasmic reticulum. Note=Detected at centrosomes during mitosis. Localizes to the endoplasmic reticulum in response to stress caused by tunicamycin.
Protein Families
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, SNF1 subfamily
Tissue Specificity
Detected in pancreas islets (at protein level).
Database Links

HGNC: 11405

OMIM: 609236

KEGG: hsa:9024

STRING: 9606.ENSP00000310697

UniGene: Hs.170819

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