Recombinant Zebrafish ALG9
Cat.No. : | ALG9-10898Z |
Product Overview : | Recombinant Zebrafish ALG9 full length or partial length protein was expressed. |
- Specification
- Gene Information
- Related Products
Source : | Mammalian Cells |
Species : | Zebrafish |
Tag : | His |
Form : | Liquid or lyophilized powder |
Endotoxin : | < 1.0 eu per μg of the protein as determined by the LAL method. |
Purity : | >80% |
Notes : | This item requires custom production and lead time is between 5-9 weeks. We can custom produce according to your specifications. |
Storage : | Store it at +4 oC for short term. For long term storage, store it at -20 oC~-80 oC. |
Storage Buffer : | PBS buffer |
Gene Name : | alg9 ALG9, alpha-1,2-mannosyltransferase [ Danio rerio (zebrafish) ] |
Official Symbol : | ALG9 |
Gene ID : | 393598 |
mRNA Refseq : | NM_200625 |
Protein Refseq : | NP_956919 |
UniProt ID : | Q6PGT9 |
Products Types
◆ Recombinant Protein | ||
ALG9-471M | Recombinant Mouse ALG9 Protein, His (Fc)-Avi-tagged | +Inquiry |
ALG9-468H | Recombinant Human ALG9 Protein, GST-tagged | +Inquiry |
ALG9-1551M | Recombinant Mouse ALG9 Protein | +Inquiry |
ALG9-3812H | Recombinant Human ALG9 protein, His-tagged | +Inquiry |
◆ Lysates | ||
ALG9-8904HCL | Recombinant Human ALG9 293 Cell Lysate | +Inquiry |
Related Gene
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.
Inquiry
- 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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