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AB178697

Anti-ALG2 antibody [EPR12006(2)(B)]

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(1 Publication)

Rabbit Recombinant Monoclonal ALG2 antibody. Suitable for WB and reacts with Human samples. Cited in 1 publication.

View Alternative Names

UNQ666/PRO1298, ALG2, Asparagine-linked glycosylation protein 2 homolog, GDP-Man:Man(1)GlcNAc(2)-PP-dolichol mannosyltransferase

1 Images
Western blot - Anti-ALG2 antibody [EPR12006(2)(B)] (AB178697)
  • WB

Supplier Data

Western blot - Anti-ALG2 antibody [EPR12006(2)(B)] (AB178697)

All lanes:

Western blot - Anti-ALG2 antibody [EPR12006(2)(B)] (ab178697) at 1/10000 dilution

Lane 1:

HepG2 lysate at 10 µg

Lane 2:

HeLa lysate at 10 µg

Lane 3:

A431 lysate at 10 µg

Lane 4:

Human fetal kidney lysate at 10 µg

Predicted band size: 47 kDa

false

  • Carrier free

    Anti-ALG2 antibody [EPR12006(2)(B)] - BSA and Azide free

Key facts

Host species

Rabbit

Clonality

Monoclonal

Clone number

EPR12006(2)(B)

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB

applications

Immunogen

The exact immunogen used to generate this antibody is proprietary information.

Reactivity data

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Product details

Species reactivity
Mouse, Rat: We have preliminary internal testing data to indicate this antibody may not react with these species.
Please contact us for more information.

Patented technology
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.

What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:

  • - High batch-to-batch consistency and reproducibility
  • - Improved sensitivity and specificity
  • - Long-term security of supply
  • - Animal-free batch production

For more information, read more on recombinant antibodies.

Properties and storage information

Form
Liquid
Purity
Tissue culture supernatant
Storage buffer
pH: 7.2 - 7.4 Preservative: 0.01% Sodium azide Constituents: PBS, 50% Tissue culture supernatant, 40% Glycerol (glycerin, glycerine), 0.05% BSA
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The ALG2 protein also known as asparagine-linked glycosylation 2 plays a role in the early steps of N-glycan precursor biosynthesis. ALG2 has a molecular mass of approximately 51 kDa and shows expression in multiple tissues including the liver and brain. The protein acts mechanically to facilitate the addition of the first mannose residue to the lipid-linked oligosaccharide (LLO) precursor in the endoplasmic reticulum a fundamental step in protein glycosylation processes.
Biological function summary

Certain processes depend on the actions of ALG2. This protein becomes part of the larger oligosaccharyltransferase complex where it ensures proper glycosylation of nascent proteins—a modification important for protein folding and stability. ALG2 modulates the efficiency of protein maturation by its role in glycan formation affecting how proteins interact within cellular processes. Defects in ALG2 lead to improper protein folding and cellular distribution.

Pathways

ALG2 functions as an important component in the protein glycosylation pathway and more specifically in the N-glycan assembly pathway. This protein interacts closely with other glycosylation enzymes like ALG12 which further add branches to the glycans once ALG2 completes its function. The interactions within this pathway ensure proper biological functionalization of glycoproteins facilitating diverse roles from cell signaling to immune recognition.

ALG2 mutations have known associations with congenital disorders of glycosylation (CDG) a group of diseases caused by defects in glycosylation. Such mutations can cause a spectrum of developmental and metabolic issues. ALG2 dysfunction linked to proteins like ALG9 in co-regulatory roles reveals the impact of glycosylation on cellular homeostasis. These insights into ALG2 give promise for potential therapeutic targets in managing CDG symptoms and advancing understanding of glycosylation-related pathology.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Mannosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. Catalyzes, on the cytoplasmic face of the endoplasmic reticulum, the addition of the second and third mannose residues to the dolichol-linked oligosaccharide chain, to produce Man3GlcNAc(2)-PP-dolichol core oligosaccharide. Man3GlcNAc(2)-PP-dolichol is a substrate for ALG11, the following enzyme in the biosynthetic pathway (PubMed : 12684507, PubMed : 35136180). While both alpha 1,3 and alpha 1,6 linkages are possible, the sequential addition of alpha 1,3 followed by alpha 1,6 is probably the preferred route (PubMed : 35136180).
See full target information ALG2

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Genetics 224: PubMed36943791

2023

An unknown essential function of tRNA splicing endonuclease is linked to the integrated stress response and intron debranching.

Applications

Unspecified application

Species

Unspecified reactive species

Jennifer E Hurtig,Ambro van Hoof
View all publications

Product promise

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