Recombinant Drosophila Melanogaster Bursicon (BURS) Protein (GST)

Name: Recombinant Drosophila Melanogaster Bursicon (BURS) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-04504P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Drosophila Melanogaster Bursicon (BURS) 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	Q9VD83
Target Symbol	BURS
Synonyms	Burs; burs-alpha; CG13419Bursicon; Bursicon subunit alpha; Cuticle-tanning hormone
Species	Drosophila melanogaster (Fruit fly)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	QPDSSVAATDNDITHLGDDCQVTPVIHVLQYPGCVPKPIPSFACVGRCASYIQVSGSKIWQMERSCMCCQESGEREAAVSLFCPKVKPGERKFKKVLTKAPLECMCRPCTSIEESGIIPQEIAGYSDEGPLNNHFRRIALQ
Expression Range	33-173aa
Protein Length	Full Length of Mature Protein
Mol. Weight	42.5kDa
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	Final heterodimeric neurohormone released at the end of the molting cycle, involved in the sclerotization (tanning) of the insect cuticle, melanization and wing spreading. Heterodimer specifically activates the G protein-coupled receptor rk.
Subcellular Location	Secreted.
Database References	KEGG: dme:Dmel_CG13419 STRING: 7227.FBpp0083529 UniGene: Dm.25481
Tissue Specificity	Expressed in one to two pairs of neurons in each of the thoracic and abdominal neuromeres of the larval CNS. Coexpressed with CCAP in most CCAP-specific neurons. Coexpressed with Pburs in four bilateral neurons in thoracic and abdominal neuromeres of the

Gene Functions References

Bursicon-alpha subunit modulates LGR2 activity in the adult Drosophila melanogaster midgut independently to Bursicon-beta. PMID: 27191973
acts in cuticle synthesis and degradation by regulating the expression of cuticular protein and chitin metabolizing related genes PMID: 25821138
results show that the functions thought to be subserved by CCAP are partially effected by bursicon, and that bursicon plays an important and heretofore undescribed role in ecdysis behavior itself. PMID: 22593051
Study provides evidence that bursicon release can precede the initiation of larval ecdysis, and that bursicon tans the puparium; results establish bursicon signaling as essential to insect growth and development. PMID: 20807433
identify here Drosophila bioactive bursicon as a heterodimer made of two cystine knot polypeptides PMID: 15811337
the Bursicon/Rickets signaling pathway is necessary for both wing expansion and initiation of the EMT that leads to removal of the epithelial cells from the wing. PMID: 18780731
the results of this study reveal novel neuromodulatory functions for bursicon and support the hypothesis that the BSEG are essential for orchestrating both the behavioral and somatic processes underlying wing expansion. PMID: 19118171

FAQs

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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.