Analytical Data
-
Gene name
PGA
- Application
-
Alternative Names
PGA；Cell wall Protein PGA59
-
Species
E.coli
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P00793
-
Expression Region
1-367aa
-
AA Sequence
SIHRVPLKKGKSLRKQLKDHGLLEDFLKKHPYNPASKYHPVLTATESYEPMTNYMDASYYGTISIGTPQQDFSVIFDTGSSNLWVPSIYCKSSACSNHKRFDPSKSSTYVSTNETVYIAYGTGSMSGILGYDTVAVSSIDVQNQIFGLSETEPGSFFYYCNFDGILGLAFPSISSSGATPVFDNMMSQHLVAQDLFSVYLSKDGETGSFVLFGGIDPNYTTKGIYWVPLSAETYWQITMDRVTVGNKYVACFFTCQAIVDTGTSLLVMPQGAYNRIIKDLGVSSDGEISCDDISKLPDVTFHINGHAFTLPASAYVLNEDGSCMLGFENMGTPTELGEQWILGDVFIREYYVIFDRANNKVGLSPLS
-
Molecular Weight
40.4 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
PGA (Poly-γ-glutamic acid) is a biopolymer composed of glutamic acid residues that has garnered significant attention in biomedical and biotechnological research due to its unique properties. Originating from various microbial sources, PGA exhibits excellent biocompatibility, biodegradability, and non-toxicity, making it an attractive candidate for a wide range of applications, including drug delivery, tissue engineering, and food preservation. The ability to manipulate its structure through genetic engineering has led to the production of recombinant PGA proteins, enabling researchers to enhance its functional properties, such as solubility, stability, and bioactivity. These engineered PGA proteins can be tailored for specific biomedical uses, such as promoting cell adhesion or modifying immune responses. Additionally, the growing interest in sustainable and environmentally friendly materials has intensified research into PGA as a biodegradable alternative to synthetic polymers. By harnessing genetic and metabolic engineering techniques, scientists aim to optimize the production and functionality of PGA, paving the way for innovative applications in medicine and industry. The ongoing exploration of PGA's potential continues to drive advancements in the field, highlighting its importance as a versatile and functional biomaterial.
