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AB197107

Anti-PNGase antibody

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(1 Publication)

Rabbit Polyclonal PNGase antibody. Suitable for WB, IHC-P and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Recombinant Fragment Protein within Human NGLY1 aa 300-550.

View Alternative Names

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

2 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-PNGase antibody (AB197107)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-PNGase antibody (AB197107)

Immunohistochemical analysis of formalin-fixed, paraffin-embedded human fetal stomach tissue labeling PNGase with ab197107 at 1/100 dilution.

Western blot - Anti-PNGase antibody (AB197107)
  • WB

Supplier Data

Western blot - Anti-PNGase antibody (AB197107)

All lanes:

Western blot - Anti-PNGase antibody (ab197107) at 1/500 dilution

All lanes:

HeLa cell lysate

Predicted band size: 74 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

IHC-P, WB

applications

Immunogen

Recombinant Fragment Protein within Human NGLY1 aa 300-550. The exact immunogen used to generate this antibody is proprietary information.

Q96IV0

Reactivity data

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Properties and storage information

Form
Lyophilized
Reconstitution
reconstitute with water at 200µL
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7.2 Preservative: 0.02% Sodium azide Constituents: PBS, 1% 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.

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

Journal of immunology research 2023:3397940 PubMed36999136

2023

SERPINB4 Promotes Keratinocyte Inflammation via p38MAPK Signaling Pathway.

Applications

Unspecified application

Species

Unspecified reactive species

Yanan Zhang,Luling Wang,Xiaoying Sun,Fulun Li
View all publications

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