Recombinant E.Coli Lactose Operon Repressor (LACI) Protein (His)

Name: Recombinant E.Coli Lactose Operon Repressor (LACI) Protein (His)
Brand: Beta LifeScience
SKU: BLC-01591P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant E.Coli Lactose Operon Repressor (LACI) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P03023
Target Symbol	LACI
Species	Escherichia coli (strain K12)
Expression System	E.coli
Tag	N-10His
Target Protein Sequence	MKPVTLYDVAEYAGVSYQTVSRVVNQASHVSAKTREKVEAAMAELNYIPNRVAQQLAGKQSLLIGVATSSLALHAPSQIVAAIKSRADQLGASVVVSMVERSGVEACKAAVHNLLAQRVSGLIINYPLDDQDAIAVEAACTNVPALFLDVSDQTPINSIIFSHEDGTRLGVEHLVALGHQQIALLAGPLSSVSARLRLAGWHKYLTRNQIQPIAEREGDWSAMSGFQQTMQMLNEGIVPTAMLVANDQMALGAMRAITESGLRVGADISVVGYDDTEDSSCYIPPLTTIKQDFRLLGQTSVDRLLQLSQGQAVKGNQLLPVSLVKRKTTLAPNTQTASPRALADSLMQLARQVSRLESGQC
Expression Range	1-360aa(Q360QC)
Protein Length	Full Length
Mol. Weight	44.7 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	Repressor of the lactose operon. Binds allolactose as an inducer.
Database References	KEGG: ecj:JW0336 STRING: 316385.ECDH10B_1357

Gene Functions References

Effect of helix length on the stability of the Lac repressor antiparallel coiled coil. PMID: 25969365
LacI autoregulation balances two opposing states, one that allows quicker response to smaller pulses of external lactose, and the other that minimizes production costs in the absence of lactose. PMID: 23658223
Data indicate that in the absence of its inducer, LacI binds to primary operator lac O1 near the transcription start site of the lac operon, and represses its transcription. PMID: 22594825
findings show the lac repressor slides 45 +/- 10 base pairs on chromosomal DNA and that sliding can be obstructed by other DNA-bound proteins near the operator; the repressor frequently slides over its natural lacO(1) operator several times before binding PMID: 22723426
The role of lactose repressor residues asparagine-125 and aspartate-149 illustrate how readily the ligand binding and allosteric response function of a regulatory bacterial protein can be altered, generating diminished operator binding. PMID: 21928765
Using the extensive LacI family of transcriptional factors, identified a set of specificity correlations--determined by two AAs of the TFs and two NTs in the binding sites- and that act as a relatively consistent recognition code. PMID: 21085639
solution structure and dynamics of the complex of a dimeric lac repressor DNA binding domain with nonspecific DNA PMID: 15256668
The Lac repressor artificially attached to the Escherichia coli cytoplasmic membrane is able to perfectly represses transcription initiated at the tac operator-promoter present on a plasmid and even in the chromosome. PMID: 15867195
Linear DNA segments of short-to-medium chain length (50-180 bp) give rise to loops with the extended form of LacR and loops formed within negatively supercoiled plasmids induce the V-shaped structure. PMID: 16785444
The mutational spectrum of the genomic lacI gene induced by low-energy nitrogen ion irradiation in wild type Escherichia coli strain W3110 were compared with the spontaneous and the vacuum controls. PMID: 17049362
In single molecule experiments, both specific bending and non-specific compaction by integration host factor alter LacI-mediated looping of DNA PMID: 17543441
The altered hydrogen bonding can account in part for the different structural conformations of the repressor, and is vital for the allosteric transition PMID: 17543986
The structure of lactose repressor (LacI) protein confirms previously reported structures on the monomer level, however, the tetramer is much more densely packed. PMID: 19004002
irradiation induces the change of the oligomerization state of LacI from tetramer to dimer. PMID: 19520056

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.