Recombinant Human ALG12, GST-tagged
Cat.No. : | ALG12-9572H |
Product Overview : | Recombinant Human ALG12 protein, fused to GST-tag, was expressed in E.coli and purified by GSH-sepharose. |
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Description : | This gene encodes a member of the glycosyltransferase 22 family. The encoded protein catalyzes the addition of the eighth mannose residue in an alpha-1,6 linkage onto the dolichol-PP-oligosaccharide precursor (dolichol-PP-Man(7)GlcNAc(2)) required for protein glycosylation. Mutations in this gene have been associated with congenital disorder of glycosylation type Ig (CDG-Ig)characterized by abnormal N-glycosylation. |
Source : | E.coli |
Species : | Human |
Tag : | GST |
Protein length : | 375-488a.a. |
Storage : | The protein is stored in PBS buffer at -20℃. Avoid repeated freezing and thawing cycles. |
Storage Buffer : | 1M PBS (58mM Na2HPO4,17mM NaH2PO4, 68mM NaCl, pH8. ) added with 100mM GSH and 1% Triton X-100,15%glycerol. |
Gene Name : | ALG12 asparagine-linked glycosylation 12, alpha-1,6-mannosyltransferase homolog (S. cerevisiae) [ Homo sapiens ] |
Official Symbol : | ALG12 |
Synonyms : | ALG12; asparagine-linked glycosylation 12, alpha-1,6-mannosyltransferase homolog (S. cerevisiae); asparagine linked glycosylation 12 homolog (yeast, alpha 1,6 mannosyltransferase); dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase; ECM39; membrane protein SB87; mannosyltransferase ALG12 homolog; asparagine-linked glycosylation protein 12 homolog; dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichyl-alpha-1,6-mannosyltransferase; dolichyl-P-mannose:Man-7-GlcNAc-2-PP-dolichyl-alpha-6-mannosyltransferase; asparagine-linked glycosylation 12 homolog (yeast, alpha-1,6-mannosyltransferase); asparagine-linked glycosylation 12 homolog (S. cerevisiae, alpha-1,6-mannosyltransferase); CDG1G; hALG12; PP14673; MGC3136; MGC111358; |
Gene ID : | 79087 |
mRNA Refseq : | NM_024105 |
Protein Refseq : | NP_077010 |
MIM : | 607144 |
UniProt ID : | Q9BV10 |
Chromosome Location : | 22q13.33 |
Pathway : | Asparagine N-linked glycosylation, organism-specific biosystem; Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein, organism-specific biosystem; Metabolic pathways, organism-specific biosystem; Metabolism of proteins, organism-specific biosystem; N-Glycan biosynthesis, organism-specific biosystem; N-Glycan biosynthesis, conserved biosystem; N-glycan precursor biosynthesis, organism-specific biosystem; |
Function : | alpha-1,6-mannosyltransferase activity; transferase activity, transferring glycosyl groups; |
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For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Q&As (18)
Ask a questionALG12 defects have not yet been fully explained by research on how they affect cell signaling mechanisms.
The relationship between ALG12 gene polymorphism and other genetic or environmental factors is still insufficient, and the existing results are not enough to make a full proof.
This protein mutations can lead to the failure of the synthesis of polysaccharides and glycoproteins, leading to diseases such as glycogen disease. Its clinical characteristics need to be evaluated through clinical studies.
ALG12's reading frame specifies an annotated sequence of organic molecules, branching point reactions in the process of breaking down sugars and lipids.
The protein encoded by ALG12 is involved in the reactants of the transfer chemical reaction, enabling the successful formation of polysaccharides and glycoproteins. Its functional characteristics are related to glycosyl synthesis in other glycogen organisms.
ALG12 is expressed in different tissues in different amounts, such as in fat, liver, gastrointestinal tract and muscle.
ALG12 is involved in the catalysis of glycosylation process, which may affect the interaction of fatty acid and glucose metabolism, but more studies are needed to clarify.
The mechanism and signaling pathway of ALG12 gene regulation are similar to other glycosylation genes, but the specific situation remains to be studied.
The mutations may cause a variety of neurological diseases and require further research using relevant animal models and nervous system cell lines.
The post-transcriptional modification and expression pattern of ALG12 gene have not been studied deeply enough, and further research is needed.
This can be used as a branch enzyme of NSDHL, if it produces an anthraquinone derivative with progesterone, and increases the amount of activated enzyme by reversing the reaction; It can also be treated with hyperliquefied P-body enzymes.
At present, a large number of studies have been carried out on the correlation between gene mutation and ALG12 gene and diseases, and many diseases have been confirmed to be associated with ALG12 gene mutation, but these scientific research results need more verification and analysis.
ALG12 mutations may affect lipid metabolism and enzyme activity, and there are some studies and confirmations, and further studies are needed to determine the specific mechanisms.
Although ALG12 has a regulatory role in lipid and glycogen processing, its detailed mechanism of action needs to be further investigated in cell and animal models.
The ALG12 genome structure is composed of multiple exons, which need to be processed into unique mRNA after transcription, and then function through regulation by various regulatory mechanisms.
Until now, there have been few studies on the effect of ALG12 mutation on hypoxia tolerance.
ALG12 encodes proteins that extend chains by transferring acid groups through molecules in glycosylation catalyzed by proteins such as lactase and glycoprotein processing enzymes.
ALG12 mutations may be associated with disorders of lipid metabolism and neurological disorders.
Customer Reviews (4)
Write a reviewAn important metabolic enzyme in the pathway of polysaccharide metabolism and pentose metabolism.
It can be used as a biomarker to prevent disease.
Strong operability in the experiment.
Activity is specific.
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