| Catalogue No. |
M-879-100 |
| Description |
Autophagy is a process of bulk protein degradation in which cytoplasmic components, including organelles, are enclosed in double-membrane structures called autophagosomes and delivered to lysosomes or vacuoles for degradation. ATG12 is the human homolog of a yeast protein involved in autophagy. ATG12 is conjugated to ATG5. The ATG12-ATG5 conjugate has an apparent molecular mass of 65 kDa. The C-terminal glycine of ATG12 is conjugated to a central lysine (lys130) of ATG5. Studies showed that over expression of ATG3 facilitated formation of the ATG12-ATG5 conjugate, suggesting that ATG3 cross-talks with the ATG12 conjugation system. ATG12 is ubiquitously expressed.
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| Batch No. |
See product label |
| Unit size |
100 ug |
| Antigen |
Full recombinant human ATG12, isoform 2, (1-74) with a GST tag. |
| Clone |
2H8 |
| Other Names |
Autophagy-related protein 12; ATG12; APG12; APG12L; APG12-like; |
| Accession |
ATG12_HUMAN |
| Produced in |
Mouse |
| Purity |
Protein G purified immunoglobulin |
| Applications |
This antibody is recommended for WB, and sandwich ELISA. Biosensis recommends optimal dilutions/concentrations should be determined by the end user. |
| Specificity |
Specificity has been confirmed by WB and direct ELISA against the antigen. |
| Cross-reactivity |
Human. Other species have not been tested. |
| Blast it |
To see the shared identity between different species or other proteins, follow the link in the Accession field, select the sequence that you are interested in and copy and paste it HERE and blast/format it. |
| Form |
Lyophilised from PBS pH 7.2 |
| Reconstitution |
Reconstitute in 100 uL of sterile water. Centrifuge to remove any insoluble material. |
| Storage |
After reconstitution keep aliquots at -20C for higher stability or at 2-8C with an appropriate antibacterial agent. Glycerol (1:1) may be added for additional stability. Avoid repetitive freeze/thaw cycles. |
| Expiry Date |
12 months after purchase |
| Specific References |
De la Mata M. et al (2015) Pharmacological Chaperones and Coenzyme Q10 Treatment Improves Mutant β-Glucocerebrosidase Activity and Mitochondrial Function in Neuronopathic Forms of Gaucher Disease.
Sci Rep. 2015 Jun 5;5:10903.
Garrido-Maraver J. et al (2015) Critical role of AMP-activated protein kinase in the balance between mitophagy and mitochondrial biogenesis in MELAS disease.
Biochim Biophys Acta. 2015 Nov;1852(11):2535-53.
Garrido-Maraver J. et al (2012) Screening of effective pharmacological treatments for MELAS syndrome using yeasts, fibroblasts and cybrids models of the disease.
Br J Pharmacol. 2012 Jul 2.
De la Mata M. et al (2012) Recovery of MERRF fibroblasts and cybrids pathophysiology by Coenzyme Q₁₀.
Neurotherapeutics. 2012 Apr;9(2):446-63.
Bullon P et al (2012) Autophagy in periodontitis patients and gingival fibroblasts: unraveling the link between chronic diseases and inflammation.
BMC Med. 2012 Oct 17;10:122.
Cotán D et al (2011) Secondary coenzyme Q10 deficiency triggers mitochondria degradation by mitophagy in MELAS fibroblasts.
FASEB J. 2011 Aug;25(8):2669-87.
Rodriguez-Hernandez A et al (2009) Coenzyme Q deficiency triggers mitochondria degradation by mitophagy.
Autophagy. 2009 Jan;5(1):19-32.
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