Recombinant Acholeplasma Laidlawii Holo-[Acyl-Carrier-Protein] Synthase (ACPS) Protein (His&Myc)

Name: Recombinant Acholeplasma Laidlawii Holo-[Acyl-Carrier-Protein] Synthase (ACPS) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-04866P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins, Recombinant proteins fall special offers - full-length proteins

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Product Overview

Description	Recombinant Acholeplasma Laidlawii Holo-[Acyl-Carrier-Protein] Synthase (ACPS) 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	A9NHV3
Target Symbol	ACPS
Synonyms	acpS; ACL_1341Holo-[acyl-carrier-protein] synthase; Holo-ACP synthase; EC 2.7.8.7; 4'-phosphopantetheinyl transferase AcpS
Species	Acholeplasma laidlawii(strain PG-8A)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MIHAIGTDLVELERIKSIGIDRFKDKILNEDEKNEYAKINHENRKLTYLAGRFAVKESLFKCFKAGDKTANYKDFSVLNDSVGAPYVVSKHTSDFVVHITISHTNLYAIAFVVLETKV
Expression Range	1-118aa
Protein Length	Full Length
Mol. Weight	20.9 kDa
Research Area	Cancer
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.
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	Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Subcellular Location	Cytoplasm.
Protein Families	P-Pant transferase superfamily, AcpS family
Database References	KEGG: acl:ACL_1341 STRING: 441768.ACL_1341

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.