Analytical Data
-
Gene name
ALG1L
- Application
-
Alternative Names
ALG1L; Putative glycosyltransferase ALG1-like; EC 2.4.1.
-
Species
Human
-
Source
E. coli
-
Tag
GST-tag at N-terminal
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q6GMV1
-
Expression Region
1-187aa
-
AA Sequence
MERSAFMELD AGSRLVMHLR EWPALLVSST GWTEFEQLTL DGHNLPSLVC VITGSVDLGV CLHMSSSGLD LPMKVVDMFG CCLPVCAVNF KCLHELVKHE ENGLVFEDSE ELAALQMLFS NFPDPAGKLN QFWKNLRESQ QLRWDESWVQ TVLPLVMDIQ LLGQRLKPRD PCCPSRSFFS ESQGKPF
-
Molecular Weight
20.6 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
ALG1L (ALG1-like) is a protein crucial for the proper folding and assembly of glycoproteins, playing a vital role in the endoplasmic reticulum's glycosylation pathway. Researchers are increasingly focusing on ALG1L due to its potential implications in various biological processes and diseases, including cancer and congenital disorders caused by glycosylation defects. Abnormalities in glycosylation can lead to impaired protein function, resulting in significant clinical consequences. ALG1L shares structural and functional similarities with the ALG1 enzyme, which is essential for the synthesis of lipid-linked oligosaccharides, a precursor for glycoprotein synthesis. Understanding the mechanisms by which ALG1L operates may provide valuable insights into cell signaling and protein interactions, as well as offer new therapeutic targets for treating glycosylation-related diseases. Recent advances in recombinant protein technology have facilitated the production and characterization of ALG1L, making it possible to study its biochemical properties and interactions in detail. This research could pave the way for innovative treatments and a better understanding of the molecular underpinnings of glycosylation disorders. As the scientific community continues to uncover the roles of ALG1L in cellular processes, it remains a promising candidate for further exploration in both basic and applied research, potentially leading to breakthroughs in medical science and biotechnology.
