ALG9
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Official Full Name
asparagine-linked glycosylation 9, alpha-1,2-mannosyltransferase homolog
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Overview
This gene encodes an alpha-1,2-mannosyltransferase enzyme that functions in lipid-linked oligosaccharide assembly. Mutations in this gene result in congenital disorder of glycosylation type Il. Multiple transcript variants encoding different isoforms have been found for this gene. -
Synonyms
ALG9; asparagine-linked glycosylation 9, alpha-1,2-mannosyltransferase homolog (S. cerevisiae); asparagine linked glycosylation 9 homolog (yeast, alpha 1,2 mannosyltransferase) , asparagine linked glycosylation 9, alpha 1,2 mannosyltransferase homolog (;
- Recombinant Proteins
- Cell & Tissue Lysates
- Protein Pre-coupled Magnetic Beads
- Human
- Mouse
- Zebrafish
- E.coli
- HEK293
- In Vitro Cell Free System
- Mammalian Cell
- Wheat Germ
- GST
- His
- His (Fc)
- Avi
- N/A
| Species | Cat.# | Product name | Source (Host) | Tag | Protein Length | Price |
|---|---|---|---|---|---|---|
| Human | ALG9-468H | Recombinant Human ALG9 Protein, GST-tagged | Wheat Germ | GST |
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| Human | ALG9-8904HCL | Recombinant Human ALG9 293 Cell Lysate | HEK293 | N/A |
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| Human | ALG9-3812H | Recombinant Human ALG9 protein, His-tagged | E.coli | His | 440-618 aa | |
| Human | ALG9-1440HF | Recombinant Full Length Human ALG9 Protein, GST-tagged | In Vitro Cell Free System | GST | 618 amino acids |
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| Mouse | ALG9-1551M | Recombinant Mouse ALG9 Protein | Mammalian Cell | His |
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| Mouse | ALG9-471M | Recombinant Mouse ALG9 Protein, His (Fc)-Avi-tagged | HEK293 | His (Fc)-Avi |
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| Mouse | ALG9-471M-B | Recombinant Mouse ALG9 Protein Pre-coupled Magnetic Beads | HEK293 |
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| Zebrafish | ALG9-10898Z | Recombinant Zebrafish ALG9 | Mammalian Cell | His |
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- Involved Pathway
- Protein Function
- Interacting Protein
- ALG9 Related Articles
ALG9 involved in several pathways and played different roles in them. We selected most pathways ALG9 participated on our site, such as N-Glycan biosynthesis, Metabolic pathways, which may be useful for your reference. Also, other proteins which involved in the same pathway with ALG9 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
|---|---|
| N-Glycan biosynthesis | ALG6;ALG8;DOLPP1;ALG10B;ST6GAL2;MGAT4C;MGAT1A;ALG10;GANAB |
| Metabolic pathways | CDIPT;HSD3B5;SDHDB;BCMO1;CYP3A25;MTMR1;NDUFA2;ADH1C;ASPA |
ALG9 has several biochemical functions, for example, dol-P-Man:Man(6)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase activity, dol-P-Man:Man(8)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase activity, mannosyltransferase activity. Some of the functions are cooperated with other proteins, some of the functions could acted by ALG9 itself. We selected most functions ALG9 had, and list some proteins which have the same functions with ALG9. You can find most of the proteins on our site.
| Function | Related Protein |
|---|---|
| dol-P-Man:Man(6)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase activity | ZNF408;ALG9 |
| dol-P-Man:Man(8)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase activity | ZNF408;ALG9 |
| mannosyltransferase activity | PIGB;ALG12;DPY19L4;POC1BL;ZNF408;DPY19L3;B3GNT9-PS;GALNT18A;GLT8D1 |
ALG9 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with ALG9 here. Most of them are supplied by our site. Hope this information will be useful for your research of ALG9.
flhA; BHMT
- Q&As
- Reviews
Q&As (17)
Ask a questionALG9 participates in the glycosylation of polypeptide chains through n-glycosylation transfer, and regulates the selectivity of n-glycosylation.
ALG9 is involved in the glycosylation of pectin synthetase and plays an important role in pectin biosynthesis.
ALG9 is involved in the modification of glycosylase of insulin precursor protein, and has a certain influence on the assembly and secretion of glycosylated insulin precursor protein.
Transcription and regulation of ALG9 are regulated by nucleic acid and protein interactions.
The glycosylation position of ALG9 is mainly involved in N-biglycosylation transfer.
ALG9 may be involved in many signaling pathways, such as glucose metabolism and endogenous antioxidant pathways.
ALG9 is related to other ALG family transferases, such as ALG3 and ALG12, which are involved in the control of protein n-glycosylation.
This is not only present in cell wall and cell membrane, but also widely expressed in underground organs and young leaves.
The high expression of ALG9 is associated with the occurrence of hypertension, obesity and other diseases.
It is mainly located in the endoplasmic reticulum and is involved in N-glycosylation.
Absence of ALG9 may be associated with congenital N-glycosylation disorder.
This is a membrane protein that contains a mini-domain on the cell membrane, a peptide expression regulation region and an N-terminal extension region.
The protein is involved in protein glycosylation and is related to the occurrence and development of some malignant tumors.
This protein is expressed in a variety of tissues and organs, such as the liver, the nervous system can be found in ALG9
The expression pattern of ALG9 protein is affected by many factors, including the regulation of transcription factors and external stimuli.
The structure and function of ALG9 are directly related, including the active site of the enzyme, the binding of the transfer substrate, etc., which are related to the glycosylation reaction of the polypeptide chain.
ALG9 is involved in many physiological processes, such as protein glycosylation, cell recognition, etc., and then affect the growth and development of the body and immune response.
Customer Reviews (4)
Write a reviewIt has made significant research progress in the application of related fields.
Low immunogenicity and does not cause abnormal immune responses.
ALG9 has good DNA binding ability and performs well in related experiments.
The structural integrity of ALG9 was verified, and the folding state and secondary structure were consistent with the native protein.
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