Human TRIM72 Recombinant Protein (N-His) (HD364012)

Name: Human TRIM72 Recombinant Protein (N-His)
Brand: abinScience
SKU: HD364012
Price: 211 USD
Availability: InStock

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Overview

Catalog No.	HD364012
Description	Recombinant Human TRIM72 Protein, N-His (HD364012) expressed in E. coli, spanning Leu288-Ala477. Purity: >90% by SDS-PAGE. Highlights ●His-Tagged — N-terminal 6×His tag for IMAC purification. ●E. coli Expression — High-yield, cost-effective production. ●High Purity — >90% purity verified by SDS-PAGE.
Expression system	E. coli
Accession	Q6ZMU5
Protein length	Leu288-Ala477
Applications	ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
Species	Homo sapiens (Human)
Nature	Recombinant
Endotoxin level	Please contact with the lab for this information.
Purity	>90% as determined by SDS-PAGE.
Predicted molecular weight	23.27 kDa
Form	Lyophilized
Storage buffer	Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.
Reconstitution	Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details.
Shipping	In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
Stability and Storage	Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt.
Alternate Names	EC:2.3.2.27, MG53, Mg53, Mitsugumin-53, TRIM72, Tripartite motif-containing protein 72
Background	Tripartite motif-containing protein 72 is a ~52 kDa protein. Muscle-specific E3 ubiquitin-protein ligase that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Its ubiquitination activity is mediated by E2 ubiquitin-conjugating enzymes UBE2D1, UBE2D2 and UBE2D3. Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site. This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation. Probably acts upstream of the Ca(2+)-dependent membrane resealing process. 1. Ma, Y. et al. (2023) Nature communications 14, 1555. PMID: 36944613
Note	For research use only

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Human TRIM72 Recombinant Protein (N-His).pdf

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Human TRIM72 Recombinant Protein (N-His) (HD364012)

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