Recombinant Drosophila Melanogaster General Odorant-Binding Protein Lush (LUSH) Protein (His&Myc)

Name: Recombinant Drosophila Melanogaster General Odorant-Binding Protein Lush (LUSH) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-08946P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Drosophila melanogaster (Fruit fly) lush.

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Product Overview

Description	Recombinant Drosophila Melanogaster General Odorant-Binding Protein Lush (LUSH) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O02372
Target Symbol	LUSH
Synonyms	lush; Obp76a; Obp76c; CG8807; General odorant-binding protein lush
Species	Drosophila melanogaster (Fruit fly)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MTMEQFLTSLDMIRSGCAPKFKLKTEDLDRLRVGDFNFPPSQDLMCYTKCVSLMAGTVNKKGEFNAPKALAQLPHLVPPEMMEMSRKSVEACRDTHKQFKESCERVYQTAKCFSENADGQFMWP
Expression Range	30-153aa
Protein Length	Full Length of Mature Protein
Mol. Weight	19.2kDa
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	Odorant-binding protein required for olfactory behavior and for activity of pheromone-sensitive neurons. Binds to alcohols and mediates avoidance behavior to high concentrations of alcohols, the alcohol-binding possibly resulting in activation of receptors on T2B neurons, the activation of these receptors inhibiting these neurons. Acts in concert with Snmp and lush to capture cVA molecules on the surface of Or67d expressing olfactory dendrites and facilitate their transfer to the odorant-receptor Orco complex. Required for cVA response, probably by binding to VA. May act by serving as an adapter that bridges the presence of gaseous pheromone molecules, cVA, to activation of specific neuronal receptors expressed on T1 olfactory neurons, possibly via a specific conformational change induced by cVA that in turn activates T1 receptors. T1 neurons are excited by the pheromone VA, while T2 neurons are inhibited by alcohols. Also binds to phthalates.
Subcellular Location	Secreted.
Protein Families	PBP/GOBP family
Database References	KEGG: dme:Dmel_CG8807 STRING: 7227.FBpp0074737 UniGene: PMID: 23121132 the alcohol binding in the LUSH protein is the consequence of three important factors: H-bonding, solvation, and the other noncovalent interaction. PMID: 20550105 Structure of a specific alcohol-binding site defined by the odorant binding protein LUSH from Drosophila melanogaster PMID: 12881720 LUSH, a soluble odorant-binding protein, undergoes a major conformational change, triggered by ligands. PMID: 14759510 genetic interaction between lush and spontaneous activity in 11-cis vaccenyl acetate-sensitive neurons in the absence of pheromone PMID: 15664171 Detection of odorants by olfactory neurons is results from direct activation of odorant receptors by odor molecules; study shows that detection of the 11-cis vaccenyl acetate (cVA), is instead mediated by pheromone-induced conformational shifts in LUSH. PMID: 18585358

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.