Recombinant E.Coli Inositol-1-Monophosphatase (SUHB) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-08378P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant E.Coli Inositol-1-Monophosphatase (SUHB) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-08378P
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Product Overview

Description Recombinant E.Coli Inositol-1-Monophosphatase (SUHB) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P0ADG4
Target Symbol SUHB
Synonyms suhB; ssyA; b2533; JW2517; Inositol-1-monophosphatase; I-1-Pase; IMPase; Inositol-1-phosphatase; EC 3.1.3.25
Species Escherichia coli (strain K12)
Expression System E.coli
Tag N-GST
Target Protein Sequence MHPMLNIAVRAARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGTDQDVQWVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFKAKQYATTYINIVGKLFNECADFRRTGSAALDLAYVAAGRVDGFFEIGLRPWDFAAGELLVREAGGIVSDFTGGHNYMLTGNIVAGNPRVVKAMLANMRDELSDALKR
Expression Range 1-267aa
Protein Length Full Length
Mol. Weight 56.2kDa
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 Part of the processive rRNA transcription and antitermination complex (rrnTAC). The complex forms an RNA-chaperone ring around the RNA exit tunnel of RNA polymerase (RNAP). It supports rapid transcription and antitermination of rRNA operons, cotranscriptional rRNA folding, and annealing of distal rRNA regions to allow correct ribosome biogenesis. This subunit may play a central role in organizing the structure. Involved in 30S ribosomal subunit biogenesis; thought to be required for loop formation between NusB/NusE (rpsJ, ribosomal protein S10) bound to boxA upstream of the rRNA operons and the elongating RNAP complex. This would promote correct co-transcriptional folding of rRNA. Plays a role in transcription antitermination in a plasmid context in vivo. Required for rrn transcription antitermination; required for integration of NusB/NusE into the antitermination complex. The Nus factor complex (NusA, NusB, NusE (rpsJ), NusG and SuhB) represses expression of suhB and possibly other genes via boxA; the Nus complex prevents or promotes Rho-mediated transcription termination depending on gene context. Involved in post-transcriptional control of gene expression (Probable). Enzymatic activity is not required for complementation of the cold-sensitive phenotype of the dnaB121 mutation (Probable).; Has D,L-inositol-1-monophosphatase and beta-glycerophosphatase activity, has less to no activity against a number of other substrates. 2.5-fold more active on 1D-inositol-1-monophosphate than L-inositol-1-monophosphate (1D-myo-inositol 3-phosphate). Specific activity increases significantly upon heating. Only beta-glycerophosphate and adenosine 2'-monophosphate are alternative substrates.; Required for growth at low temperatures. Identified as a suppressor (ssyA3) of a temperature-sensitive, protein export missense mutation of secY (secY24), allows growth at 42 but not 30 degrees Celsius. Identified as a suppressor (suhB2) of an rpoH missense mutation (rpoH15), allowing growth at 37 and 40 but not 25, 30 or 34 degrees Celsius, increases expression of RpoH. Identified as a suppressor of a dnaB helicase missense mutation (dnaB121), restores growth at 42 but not 30 degrees Celsius. In both suhB2 and ssyA3 there is an insertion in the 5' region of the gene which prevents SuhB protein expression. Missense mutant suhB10 is suppressed by mutations in RNase III (rnc), showing genetic interaction between them. Deletion of suhB is suppressed by mutations in RNase III, by a mutation in nusA or deletion of nusB, indicating that in the absence of SuhB the Nus complex inhibits growth.
Subcellular Location Cytoplasm.
Protein Families Inositol monophosphatase superfamily
Database References

Gene Functions References

  1. The authors demonstrate that the main function of this SuhB-containing complex is not to prevent premature transcription termination within the rRNA operon, as had been long claimed, but to enable rRNA maturation and a functional ribosome fully competent for translation. PMID: 26980831

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.

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