Recombinant Drosophila Melanogaster Stress-Activated Protein Kinase Jnk (BSK) Protein (His)

Name: Recombinant Drosophila Melanogaster Stress-Activated Protein Kinase Jnk (BSK) Protein (His)
Brand: Beta LifeScience
SKU: BLC-09058P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Drosophila Melanogaster Stress-Activated Protein Kinase Jnk (BSK) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P92208
Target Symbol	BSK
Synonyms	bsk; JNK; CG5680; Stress-activated protein kinase JNK; dJNK; EC 2.7.11.24; Protein basket
Species	Drosophila melanogaster (Fruit fly)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MTTAQHQHYTVEVGDTNFTIHSRYINLRPIGSGAQGIVCAAYDTITQQNVAIKKLSRPFQNVTHAKRAYREFKLMKLVNHKNIIGLLNAFTPQRNLEEFQDVYLVMELMDANLCQVIQMDLDHDRMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKADCTLKILDFGLARTAGTTFMMTPYVVTRYYRAPEVILGMGYTENVDIWSVGCIMGEMIRGGVLFPGTDHIDQWNKIIEQLGTPSPSFMQRLQPTVRNYVENRPRYTGYSFDRLFPDGLFPNDNNQNSRRKASDARNLLSKMLVIDPEQRISVDEALKHEYINVWYDAEEVDAPAPEPYDHSVDEREHTVEQWKELIYEEVMDYEAHNTNNRTR
Expression Range	1-372aa
Protein Length	Full Length
Mol. Weight	47.0kDa
Research Area	Others
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	Responds to activation by environmental stress by phosphorylating a number of transcription factors, primarily components of AP-1 such as Jra and also the transcriptional repressor aop, and thus regulates transcriptional activity. Component of the immune response activated by bacterial infection, and is involved in wound healing and in dorsal closure, a morphogenetic movement during embryogenesis. Functions in the systematic response to wounding acting downstream of the Hayan-phenoloxidase PPO1 cascade. Exhibits cytoprotective activity in neuronal cells in response to wounding to the integument. Controls the expression of a phosphatase, puckered, at the edges of wounded epidermal tissue and in the dorsal epithelium during dorsal closure. Regulates the activity of SREBP in neurons and thereby the accumulation of lipids in glia. Plays a role in postively regulating the expression of DIP2 independently of AP-1, thereby ensuring proper axon guidance in mushroom bodies.
Subcellular Location	Nucleus. Cytoplasm.
Protein Families	Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily
Database References	KEGG: dme:Dmel_CG5680 STRING: 7227.FBpp0079676 UniGene: PMID: 29133184 n addition to significantly increasing the number of JNK target genes identified so far, our results reveal that the LE is a highly heterogeneous morphogenetic organizer, sculpted through crosstalk between JNK, segmental and AP signalling. This fine-tuning regulatory mechanism is essential to coordinate morphogenesis and dynamics of tissue sealing PMID: 28231245 Diminished MTORC1-dependent JNK activation underlies the neurodevelopmental defects associated with lysosomal dysfunction. PMID: 26387958 This study demonstrated that the mechanism by which Bsk is required for pruning is through reducing the membrane levels of the adhesion molecule Fasciclin II (FasII) PMID: 26586184 Study solves the crystal structure of unphosphorylated DJNK in complex with adenylyl imidodiphosphate (AMP-PNP) and magnesium. PMID: 26377800 In a genetic screen, we identified signaling by the EGFR pathway as important for apoptosis-induced proliferation acting downstream of JNK signaling PMID: 24497843 We propose that JNK is a central stress response effector that is activated by nucleolar stress in Drosophila larvae PMID: 23412656 dUev1a modulates TNF-JNK mediated tumor progression and cell death in Drosophila. PMID: 23726905 Raw negatively regulates JNK signaling during gonad morphogenesis, and increased JNK signaling is sufficient to cause ensheathment defects. PMID: 22575490 ectopic Dpp led to DJNK-dependent cardial apoptosis through the non-canonical TGF-beta pathway during late embryogenesis of Drosophila. PMID: 22114909 stress-induced apoptosis in Drosophila is dependant on an amplification loop mediated by dp53 and JNK PMID: 21886179 Pan-neuronal knockdown of JNK mRNA expression by RNA interference resulted in a decrease in both sleep and longevity. PMID: 22197814 Data show that regeneration of genetically ablated tissue requires JNK activity, and that the JNK pathway is activated at the leading edges of healing tissue and not in apoptotic cells, and is required for regulation of healing and regenerative growth. PMID: 20215351 These findings demonstrate that Eiger can initiate cell death through an IAP-sensitive cell death pathway via JNK signaling. PMID: 12065414 Results introduce the Jun N-terminal kinase (JNK) signaling pathway as a genetic determinant of aging in Drosophila melanogaster. PMID: 14602080 Relish limits the duration of JNK activation in response to Gram-negative infections. Degradation of TAK1 leads to a rapid termination of JNK signaling, resulting in a transient JNK-dependent response that precedes sustained induction of immune loci. PMID: 15037551 The convergence of JNK signaling and IIS on Foxo provides a model to explain the effects of stress and nutrition on longevity. PMID: 15820683 JNK acts as the downstream mediator of the LKB1-dependent apoptosis. PMID: 16273080 Study found that the left-right asymmetric cell rearrangement in the circular visceral muscle was regulated by D-JNK signaling and required for the LR asymmetric looping of the anterior-midgut. PMID: 17915206 regulators of JNK were identified; using genetic & phosphoproteomics data, an integrative network algorithm to construct a JNK phosphorylation network was implemented PMID: 18927396 influences regeneration in the gut by directing proliferation of intestinal stem cells, contributes to the loss of tissue homeostasis in old and stressed intestines PMID: 18940735 JNK activity upregulates genes involved in intracellular transport in order to provide an increased level of trafficking activity in cells undergoing complex morphogenetic arrangements such as dorsal closure. PMID: 19427848

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.