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Rabbit Anti-CHGA Recombinant Antibody (CBWJC-2033) (CBMAB-C2657WJ)

This product is a Rabbit antibody that recognizes CHGA. This antibody CBWJC-2033 can be used for immunoassay techniques such as: WB, IHC-P, ICC, FC.
See all CHGA antibodies

Summary

Host Animal
Rabbit
Specificity
Human
Clone
CBWJC-2033
Antibody Isotype
IgG
Application
WB, IHC-P, ICC, FC

Basic Information

Specificity
Human
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Chromogranin A
Introduction
The protein encoded by this gene is a member of the chromogranin/secretogranin family of neuroendocrine secretory proteins. It is found in secretory vesicles of neurons and endocrine cells. This gene product is a precursor to three biologically active peptides; vasostatin, pancreastatin, and parastatin. These peptides act as autocrine or paracrine negative modulators of the neuroendocrine system. Two other peptides, catestatin and chromofungin, have antimicrobial activity and antifungal activity, respectively. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2014]
Entrez Gene ID
1113
UniProt ID
P10645
Alternative Names
Chromogranin A; Parathyroid Secretory Protein 1; Pituitary Secretory Protein I; SP-I; CGA; Betagranin (N-Terminal Fragment Of Chromogranin A); Chromogranin-A;
Function
Pancreastatin:
Strongly inhibits glucose induced insulin release from the pancreas.
Catestatin:
Inhibits catecholamine release from chromaffin cells and noradrenergic neurons by acting as a non-competitive nicotinic cholinergic antagonist (PubMed:15326220).
Displays antibacterial activity against Gram-positive bacteria S.aureus and M.luteus, and Gram-negative bacteria E.coli and P.aeruginosa (PubMed:15723172 and PubMed:24723458).
Can induce mast cell migration, degranulation and production of cytokines and chemokines (PubMed:21214543).
Acts as a potent scavenger of free radicals in vitro (PubMed:24723458).
May play a role in the regulation of cardiac function and blood pressure (PubMed:18541522).
Serpinin:
Regulates granule biogenesis in endocrine cells by up-regulating the transcription of protease nexin 1 (SERPINE2) via a cAMP-PKA-SP1 pathway. This leads to inhibition of granule protein degradation in the Golgi complex which in turn promotes granule formation.
Biological Process
Adenylate cyclase-activating adrenergic receptor signaling pathway involved in cardiac muscle relaxation Source: BHF-UCL
Antimicrobial humoral response Source: Reactome
Defense response to bacterium Source: GO_Central
Defense response to fungus Source: UniProtKB-KW
Defense response to Gram-negative bacterium Source: UniProtKB
Defense response to Gram-positive bacterium Source: UniProtKB
Innate immune response Source: UniProtKB
Killing of cells of other organism Source: UniProtKB-KW
Mast cell activation Source: UniProtKB
Mast cell chemotaxis Source: UniProtKB
Mast cell degranulation Source: UniProtKB
Negative regulation of catecholamine secretion Source: UniProtKB
Negative regulation of insulin secretion Source: GO_Central
Negative regulation of neuron death Source: BHF-UCL
Organelle organization Source: BHF-UCL
Positive regulation of cardiac muscle contraction Source: BHF-UCL
Positive regulation of dense core granule biogenesis Source: UniProtKB
Positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway Source: BHF-UCL
Positive regulation of relaxation of cardiac muscle Source: BHF-UCL
Protein localization to secretory granule Source: Ensembl
Regulation of blood pressure Source: ProtInc
Regulation of the force of heart contraction Source: BHF-UCL
Cellular Location
Serpinin: Secreted; secretory vesicle. Pyroglutaminated serpinin localizes to secretory vesicle.
Secreted; Secretory vesicle; Neuronal dense core vesicle. Associated with the secretory granule membrane through direct interaction to SCG3 that in turn binds to cholesterol-enriched lipid rafts in intragranular conditions. In pituitary gonadotropes, located in large secretory granules.
PTM
Sulfated on tyrosine residues and/or contains sulfated glycans.
O-glycosylated with core 1 or possibly core 8 glycans.
Proteolytic processing gives rise to an additional longer form of catestatin (residues 358-390) which displays a less potent catecholamine release-inhibitory activity (PubMed:10781584). Plasmin-mediated proteolytic processing can give rise to additional shorter and longer forms of catestatin peptides (PubMed:17991725).

Bralewska, M., Biesiada, L., Grzesiak, M., Rybak-Krzyszkowska, M., Huras, H., Gach, A., ... & Sakowicz, A. (2021). Chromogranin A demonstrates higher expression in preeclamptic placentas than in normal pregnancy. BMC Pregnancy and Childbirth, 21(1), 1-10.

Eissa, N., Hussein, H., Tshikudi, D. M., Hendy, G. N., Bernstein, C. N., & Ghia, J. E. (2020). Interdependence between Chromogranin-A, Alternatively Activated Macrophages, Tight Junction Proteins and the Epithelial Functions. A Human and In-Vivo/In-Vitro Descriptive Study. International Journal of Molecular Sciences, 21(21), 7976.

Mahata, S. K., & Corti, A. (2019). Chromogranin A and its fragments in cardiovascular, immunometabolic, and cancer regulation. Annals of the New York Academy of Sciences, 1455(1), 34.

Zhang, X., Zhang, H., Shen, B., & Sun, X. F. (2019). Chromogranin-A expression as a novel biomarker for early diagnosis of colon cancer patients. International journal of molecular sciences, 20(12), 2919.

Guo, Z., Wang, Y., Xiang, S., Wang, S., & Chan, F. L. (2019). Chromogranin A is a predictor of prognosis in patients with prostate cancer: a systematic review and meta-analysis. Cancer management and research, 11, 2747.

Eissa, N., Hussein, H., Kermarrec, L., Ali, A. Y., Marshall, A., Metz-Boutigue, M. H., ... & Ghia, J. E. (2018). Chromogranin-A regulates macrophage function and the apoptotic pathway in murine DSS colitis. Journal of Molecular Medicine, 96(2), 183-198.

Eissa, N., Hussein, H., Hendy, G. N., Bernstein, C. N., & Ghia, J. E. (2018). Chromogranin-A and its derived peptides and their pharmacological effects during intestinal inflammation. Biochemical pharmacology, 152, 315-326.

Wollam, J., Mahata, S., Riopel, M., Hernandez-Carretero, A., Biswas, A., Bandyopadhyay, G. K., ... & Mahata, S. K. (2017). Chromogranin A regulates vesicle storage and mitochondrial dynamics to influence insulin secretion. Cell and tissue research, 368(3), 487-501.

Bandyopadhyay, G. K., & Mahata, S. K. (2017). Chromogranin A regulation of obesity and peripheral insulin sensitivity. Frontiers in endocrinology, 8, 20.

Subramanian, L., Khan, A. A., Allu, P. K., Kiranmayi, M., Sahu, B. S., Sharma, S., ... & Mahapatra, N. R. (2017). A haplotype variant of the human chromogranin A gene (CHGA) promoter increases CHGA expression and the risk for cardiometabolic disorders. Journal of Biological Chemistry, 292(34), 13970-13985.

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For research use only. Not intended for any clinical use.

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