Recombinant Autographa Californica Nuclear Polyhedrosis Virus Major Capsid Protein (P39) Protein (His&Myc)

Name: Recombinant Autographa Californica Nuclear Polyhedrosis Virus Major Capsid Protein (P39) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-01026P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Autographa Californica Nuclear Polyhedrosis Virus Major Capsid Protein (P39) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P17499
Target Symbol	P39
Species	Autographa californica nuclear polyhedrosis virus (AcMNPV)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MALVPVGMAPRQMRVNRCIFASIVSFDACITYKSPCSPDAYHDDGWFICNNHLIKRFKMSKMVLPIFDEDDNQFKMTIARHLVGNKERGIKRILIPSATNYQDVFNLNSMMQAEQLIFHLIYNNENAVNTICDNLKYTEGFTSNTQRVIHSVYATTKSILDTTNPNTFCSRVSRDELRFFDVTNARALRGGAGDQLFNNYSGFLQNLIRRAVAPEYLQIDTEELRFRNCATCIIDETGLVASVPDGPELYNPIRSSDIMRSQPNRLQIRNVLKFEGDTRELDRTLSGYEEYPTYVPLFLGYQIINSENNFLRNDFIPRANPNATLGGGAVAGPAPGVAGEAGGGIAV
Expression Range	1-347aa
Protein Length	Full Length
Mol. Weight	46.4 kDa
Research Area	Microbiology
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	Most abundant structural protein of the nucleocapsid produced during the infection cycle. The monomers are arranged in stacked rings around the nucleoprotein core.
Subcellular Location	Virion.
Protein Families	Baculoviridae major capsid protein family
Database References	KEGG: vg:1403922

Gene Functions References

Capsid proteins VP39 and EXON0 interact with kinesin-1 in insect cells. PMID: 22072745
At late times ME53 formed distinct foci at the cell periphery and colocalized with the major envelope fusion protein GP64 and frequently with VP39 capsid protein, suggesting that these cell membrane regions may represent viral budding sites. PMID: 21775466

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.