PCK2 Antibody (C-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q16822 |
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Clone Names | 3033110 |
Gene ID | 5106 |
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Other Names | Phosphoenolpyruvate carboxykinase [GTP], mitochondrial, PEPCK-M, PCK2, PEPCK2 |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP8094b was selected from the C-term region of human PCK2 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | PCK2 (HGNC:8725) |
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Synonyms | PEPCK2 |
Function | Mitochondrial phosphoenolpyruvate carboxykinase that catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle (PubMed:28955899). Can play an active role in glyceroneogenesis and gluconeogenesis (PubMed:28955899). |
Cellular Location | Mitochondrion. |
Tissue Location | Widely expressed.. |
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Provided below are standard protocols that you may find useful for product applications.
Background
This gene encodes a member of the phosphoenolpyruvate carboxykinase (GTP) family. The protein is a mitochondrial enzyme that catalyzes the conversion of oxaloacetate to phosphoenolpyruvate in the presence of GTP. A cytosolic form encoded by a different gene has also been characterized and is the key enzyme of gluconeogenesis in the liver. The encoded protein may serve a similar function, although it is constitutively expressed and not modulated by hormones such as glucagon and insulin that regulate the cytosolic form. Alternatively spliced transcript variants have been described.
References
Strausberg, R.L., et al., Proc. Natl. Acad. Sci. U.S.A. 99(26):16899-16903 (2002).Modaressi, S., et al., Biochem. J. 333 (Pt 2), 359-366 (1998).Modaressi, S., et al., Biochem. J. 315 (Pt 3), 807-814 (1996).
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