Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) (C-Term) antibody

Antigen: Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH)

Synonyms: G3PD, GAPD, MGC88685, Gapd, MGC102544, MGC102546, MGC103190, MGC103191, MGC105239, GA3PDH, GADPH, GAP, GAPDH, GAPDH II, GAPDH2, Gapdh-2, Gapdh13F, DmelCG8893, CG8893, BEST:GH12586, GAPDH I, GAPDH-1, Gapdh43E, gh12586, DmelCG12055, CG12055, MGC127711, gapd, cb609, wu:fb33a10, KNC-NDS6, g3pd, MGC89215, G3PDH, DKFZp468E2417, MGC53986, GAPC-2, GAPC2, GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE C-2, glyceraldehyde-3-phosphate dehydrogenase C2, T6J4.17, T6J4_17

Binding Site: C-Term

Clonality: Polyclonal

Host: Rabbit

Reactivity: Please enquire

Conjugate: Un-conjugated

Application: Immunohistochemistry (IHC), Western Blotting (WB)

Catalog no.: ABIN350328

Additional Information

Alternative name: GAPDH (Glyceraldehyde 3 phosphate dehydrogenase)

UniProt: P04797

Immunogen: A synthetic peptide from c-terminal of rat GAPDH (Glyceraldehyde 3 phosphate dehydrogenase) conjugated to an immunogenic carrier protein was used as the immunogen. The antigen is homologous in mouse and shares 90% identity with human sequence.

Format: Lyophilized

Isotype: IgG

Description: FUNCTION: May bind tRNA. Has uracil-DNA-glycosylase activity. May activate transcription in neurons. Functions as a killing protein in apoptosis when over-expressed. CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH. PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. SUBUNIT: Homotetramer. SUBCELLULAR LOCATION: Cytoplasm. TISSUE SPECIFICITY: High levels in skeletal muscle and heart, low levels in liver, brain, and kidney. Also known as: 38 kDa BFA dependent ADP ribosylation substrate, BARS-38, Glyceraldehyde-3-phosphate dehydrogenase.

Specificity: Appears to be specific for GAPDH.

Synonyms: G3PD, GAPD, MGC88685, Gapd, MGC102544, MGC102546, MGC103190, MGC103191, MGC105239, GA3PDH, GADPH, GAP, GAPDH, GAPDH II, GAPDH2, Gapdh-2, Gapdh13F, DmelCG8893, CG8893, BEST:GH12586, GAPDH I, GAPDH-1, Gapdh43E, gh12586, DmelCG12055, CG12055, MGC127711, gapd, cb609, wu:fb33a10, KNC-NDS6, g3pd, MGC89215, G3PDH, DKFZp468E2417, MGC53986, GAPC-2, GAPC2, GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE C-2, glyceraldehyde-3-phosphate dehydrogenase C2, T6J4.17, T6J4_17

Application Details

Application Notes: IHC, WB. A concentration of 10-50 µg/ml is recommended. The optimal concentration should be determined by the end user. Not yet tested in other applications.

Purity: IgG

Storage: Maintain the lyophilised/reconstituted antibodies frozen at -20°C for long term storage and refrigerated at 2-8°C for a shorter term. When reconstituting, glycerol (1:1) may be added for an additional stability. Avoid freeze and thaw cycles.

Restrictions: For Research Use only

Images

WB on human neutrophil lysate using Rabbit antibody to c-terminal of GAPDH (Glyceraldehyde 3 phosphate dehydrogenase): IgG (ABIN350328) at a concentration of 30 µg/ml.

Publications

Fort, Marty, Piechaczyk et al.: "Various rat adult tissues express only one major mRNA species from the glyceraldehyde-3-phosphate-dehydrogenase multigenic family." in: Nucleic acids research, Vol. 13, Issue 5, pp. 1431-42, 1985 (PubMed).

Tso, Sun, Kao et al.: "Isolation and characterization of rat and human glyceraldehyde-3-phosphate dehydrogenase cDNAs: genomic complexity and molecular evolution of the gene." in: Nucleic acids research, Vol. 13, Issue 7, pp. 2485-502, 1985 (PubMed).

Mohr, Stamler, Bruene: "Posttranslational modification of glyceraldehyde-3-phosphate dehydrogenase by S-nitrosylation and subsequent NADH attachment." in: The Journal of biological chemistry, Vol. 271, Issue 8, pp. 4209-14, 1996 (PubMed).

Kullberg, Nilsson, Arnason et al.: "Housekeeping genes for phylogenetic analysis of eutherian relationships." in: Molecular biology and evolution, Vol. 23, Issue 8, pp. 1493-503, 2006 (PubMed).

Ballif, Carey, Sunyaev et al.: "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." in: Journal of proteome research, Vol. 7, Issue 1, pp. 311-8, 2008 (PubMed).