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AB73984

Anti-PNGase antibody

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(1 Publication)

Rabbit Polyclonal PNGase antibody. Suitable for ICC, WB and reacts with Human samples. Cited in 1 publication.

View Alternative Names

PNG1, NGLY1, Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase, PNGase, hPNGase, N-glycanase 1, Peptide:N-glycanase

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB, ICC

applications

Immunogen

Synthetic Peptide within Human NGLY1 aa 100-200. The exact immunogen used to generate this antibody is proprietary information.

Q96IV0

Reactivity data

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Properties and storage information

Form
Liquid
Purity
Whole antiserum
Storage buffer
Constituents: Whole serum
Shipped at conditions
Blue Ice
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.

PNGase also known as Peptide:N-Glycosidase F is an enzyme that mechanically removes N-linked glycans from glycoproteins a process known as deglycosylation. PNGase primarily acts by cleaving the bond between the asparagine residue of the peptide and the N-linked oligosaccharides. The enzyme is extensively utilized in laboratories where it has become important in the study of glycoprotein characterization and analysis. PNGase F with a molecular mass of approximately 36 kDa is expressed in the bacterium Flavobacterium meningosepticum and sometimes can be recombinantly expressed in hosts like E. coli for research purposes.
Biological function summary

PNGase F plays a significant role in the modification of proteins and affects their stability solubility and function. It operates as a part of the broader glycan-processing machinery but is not typically within the complex protein structures. By removing glycan groups PNGase F influences protein folding and degradation processes making it key in the study of protein lifespan and function after glycosylation. Understanding its activity assists in elucidating the complex roles of glycoproteins in cellular function and signaling.

Pathways

PNGase F is involved in glycoconjugate pathway modulation by facilitating the turnover of glycoproteins. It interfaces with the ERAD (Endoplasmic Reticulum-Associated Degradation) pathway by preparing misfolded glycoproteins for further degradation. Through these interactions PNGase F indirectly influences proteins like EDEM (ER degradation-enhancing alpha-mannosidase-like protein) which aid in the recognition and targeting of proteins for disposal within the cell ensuring the cellular protein quality control.

PNGase F activity relates predominantly to neurodegenerative diseases like Alzheimer's where abnormal glycoprotein accumulation occurs. Abnormal glycans or improperly folded glycoproteins contribute to disease pathology and PNGase F's functional relationship with ERAD affects proteins involved in misfolding such as amyloid precursor protein (APP). This connection suggests that PNGase F could play a potential role in both understanding and developing therapeutic strategies for diseases where glycoprotein metabolism is disrupted.

Product protocols

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

Target data

Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins.
See full target information NGLY1

Publications (1)

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

Nature communications 7:13150 PubMed27748395

2016

Human genome-wide RNAi screen reveals host factors required for enterovirus 71 replication.

Applications

Unspecified application

Species

Unspecified reactive species

Kan Xing Wu,Patchara Phuektes,Pankaj Kumar,Germaine Yen Lin Goh,Dimitri Moreau,Vincent Tak Kwong Chow,Frederic Bard,Justin Jang Hann Chu
View all publications

Product promise

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