Recombinant E.Coli Lipopolysaccharide Export System Protein Lpta (LPTA) Protein (His-SUMO)

Name: Recombinant E.Coli Lipopolysaccharide Export System Protein Lpta (LPTA) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-04565P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description	Recombinant E.Coli Lipopolysaccharide Export System Protein Lpta (LPTA) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P0ADV1
Target Symbol	LPTA
Synonyms	lptA; yhbN; b3200; JW3167; Lipopolysaccharide export system protein LptA
Species	Escherichia coli (strain K12)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	VTGDTDQPIHIESDQQSLDMQGNVVTFTGNVIVTQGTIKINADKVVVTRPGGEQGKEVIDGYGKPATFYQMQDNGKPVEGHASQMHYELAKDFVVLTGNAYLQQVDSNIKGDKITYLVKEQKMQAFSDKGKRVTTVLVPSQLQDKNNKGQTPAQKKGN
Expression Range	28-185aa
Protein Length	Full Length of Mature Protein
Mol. Weight	33.3kDa
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	Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. May form a bridge between the inner membrane and the outer membrane, via interactions with LptC and LptD, thereby facilitating LPS transfer across the periplasm.
Subcellular Location	Periplasm. Note=Associates with both the inner membrane and the outer membrane.
Protein Families	LptA family
Database References	KEGG: ecj:JW3167 STRING: 316385.ECDH10B_3374

Gene Functions References

characterization of a viable quadruple lptA mutant impaired in the assembly of the Lpt machinery, although it retains the ability to bind LPS; although viable, the quadruple lptA mutant disrupts outer membrane (OM) asymmetry and severely impairs the OM permeability barrier; analysis of 2 independent suppressors revealed different strategies adopted by the cell to overcome defects in LPS biogenesis PMID: 29109183
LptA molecular structure is affected by lipopolysaccharides binding. PMID: 28419595
An induced folding process characterizes the partial-loss of function mutant LptAI36D in its interactions with lipopolysaccharide constituent ligands. PMID: 26123264
Studied the assembly and architecture of LptA oligomers. PMID: 23897621
results suggest that LptA operate in the LPS assembly pathway and, together with other as-yet-unidentified components, could be part of a complex devoted to the transport of LPS from the periplasmic surface of the IM to the OM. PMID: 18424520
LptA binds structurally diverse lipopolysaccharide (LPS) substrates in vitro and demonstrate that it interacts specifically with the lipid A domain of LPS PMID: 18480051

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.