Recombinant Streptomyces Actuosus Nosiheptide Precursor (NOSM) Protein (GST)

Name: Recombinant Streptomyces Actuosus Nosiheptide Precursor (NOSM) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-10501P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Streptomyces Actuosus Nosiheptide Precursor (NOSM) 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	C6FX52
Target Symbol	NOSM
Synonyms	nosM; Nosiheptide precursor [Cleaved into: Nosiheptide; NOS; Antibiotic 9671-RP; Multhiomycin)]
Species	Streptomyces actuosus
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MDAAHLSDLDIDALEISEFLDESRLEDSEVVAKVMSASCTTCECCCSCSS
Expression Range	1-50aa
Protein Length	Full Length
Mol. Weight	32.4kDa
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

Inhibits bacterial protein biosynthesis by binding to ribosomes. Specifically, binds to the complex of 23S rRNA and ribosomal protein L11 (RPLK) in the 50S ribosomal subunit. While allowing a weak binding of elongation factor G (EF-G) to the ribosome and subsequent GTP-hydrolysis, probably impairs conformational changes in both the ribosome and EF-G which are necessary for translocation. In vitro, inhibits Gram-positive bacteria S.aureus strain 209P (MIC=0.0009 ug/ml), S.aureus strain 133 (MIC=0.0019 ug/ml), S.aureus strain B3 (MIC=0.003 ug/ml), S.aureus strain Hb (MIC=0.003 ug/ml), M.citreus strain ATCC 8411 (MIC=0.0038 ug/ml), M.lysodeikticus strain ATCC 4698 (MIC=0.003 ug/ml), S.lutea strain ATCC 9341 (MIC=0.0011 ug/ml), S.faecalis strain ATCC 9790 (MIC=0.0007 ug/ml), S.viridans (MIC=0.0065 ug/ml), S.pyogenes hemolyticus strain Dig7 (MIC=0.00028 ug/ml), D.pneumoniae strain Til (MIC=0.00015 ug/ml), N.catrrhalis (MIC=0.0017 ug/ml), L.casei strain ATCC 6633 (MIC=0.003 ug/ml), B.cereus strain ATCC 6630 (MIC=0.0071 ug/ml) and various isolates of L.monocytogenes. In vitro, inhibits Gram-negative bacterium P.multocida strain A125 (MIC=0.0024 ug/ml) but not M.smegmatis strain ATCC 6630, S.typhimurium, A.aerogenes strain ATCC 8308, P.vulgaris, K.pneumoniae strain ATCC 10031, S.marcescens strain A476, P.aeruginosa strain Bass or B.bronchiseptica strain CN387. Does not inhibit Gram-negative bacterium E.coli strain ATCC 9637 but does inhibit purified ribosomes from E.coli. In vivo, has no systemic effect in mice infected with staphylococci or streptococci when applied orally or subcutaneously. Has a local effect in mice infected subcutaneously or intraperitoneally with staphylococci when applied immediately afterwards. Is not toxic to mice.

Protein Families

Thiocillin family

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.