Recombinant Human GALM Protein (C-6His)

Beta LifeScience SKU/CAT #: BL-1311NP
BL-1311NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
BL-1311NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Recombinant Human GALM Protein (C-6His)

Beta LifeScience SKU/CAT #: BL-1311NP
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Product Overview

Description Recombinant Human Galactose Mutarotase is produced by our E.coli expression system and the target gene encoding Ala2-Ala342 is expressed with a 6His tag at the C-terminus.
Accession Q96C23
Synonym Aldose 1-Epimerase; Galactose Mutarotase; GALM
Gene Background Galactose Mutarotase (GALM) is a cytoplasmic enzyme that belongs to the Aldose Epimerase family. GALM is a Mutarotase that converts α-Aldose to the β-Anomer. GALM is active on D-Glucose, L-Arabinose, D-Xylose, D-Galactose, Maltose and Lactose. GALM may be required for normal Galactose metabolism by maintaining the equilibrium of α- and β- anomers of Galactose.
Molecular Mass 38.8 KDa
Apmol Mass 34 KDa, reducing conditions
Formulation Supplied as a 0.2 μm filtered solution of PBS, pH 7.4.
Endotoxin Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity Not tested
Reconstitution
Storage Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage For Research Use Only

Target Details

Target Function Mutarotase that catalyzes the interconversion of beta-D-galactose and alpha-D-galactose during galactose metabolism. Beta-D-galactose is metabolized in the liver into glucose 1-phosphate, the primary metabolic fuel, by the action of four enzymes that constitute the Leloir pathway: GALM, GALK1 (galactokinase), GALT (galactose-1-phosphate uridylyltransferase) and GALE (UDP-galactose-4'-epimerase). Involved in the maintenance of the equilibrium between the beta- and alpha-anomers of galactose, therefore ensuring a sufficient supply of the alpha-anomer for GALK1. Also active on D-glucose although shows a preference for galactose over glucose.
Subcellular Location Cytoplasm.
Protein Families Aldose epimerase family
Database References

HGNC: 24063

OMIM: 137030

KEGG: hsa:130589

STRING: 9606.ENSP00000272252

UniGene: PMID: 21339755

  • Identification and characterisation of human aldose 1-epimerase. PMID: 12753898
  • The enzyme is a monomer and has a similar structure to the Lactococcus lactis mutarotase. PMID: 15026423
  • Gene encodes a functional aldose 1-epimerase (mutarotase). The enzyme exhibits (approx. four-fold) preference for galactose over glucose. Mutation E307A results in no detactable activity. PMID: 12753898
  • 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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