Recombinant Proteins

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CHGA Human

Chromogranin-A Human Recombinant

Recombinant Human CHGA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 114 amino acids (19-131 a.a) and having a molecular mass of 12.8 kDa.
Chromgranin-A is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8413
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

CHGA Human, HEK

Chromogranin A Human Recombinant, HEK

CHGA Human Recombinant is a single, glycosylated polypeptide chain containing 445 amino acids (19-457a.a) and having a molecular mass of 49.7kDa (calculated). CHGA is fused to a 6 a.a His tag at C-terminal.

Shipped with Ice Packs
Cat. No.
BT8496
Source

HEK293 cells.

Appearance
Filtered White lyophilized (freeze-dried) powder.

CHGA Human, His

Chromogranin-A Human Recombinant, His Tag

Recombinant Human CHGA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 460 amino acids (19-457 a.a) and having a molecular mass of 51.2kDa (Molecular weight on SDS-PAGE will appear higher).
Chromgranin-A is fused to 21 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8544
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

CHGA Human, Sf9

Chromogranin A Human Recombinant, Sf9

CHGA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (19-457 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 448 amino acids and having a molecular mass of 50kDa.CHGA shows multiple bands between 50-70kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT8672
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered colorless solution.

CHGB Human

Chromogranin B Human Recombinant

CHGB Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 677 amino acids (21-677 a.a.) and having a molecular mass of 78.4kDa. CHGB protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.
Shipped with Ice Packs
Cat. No.
BT8732
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.
Definition and Classification

Chromogranins are a family of acidic, soluble secretory proteins found in the secretory granules of neuroendocrine cells. The most well-known members of this family are Chromogranin A, Chromogranin B, and Chromogranin C . Chromogranin A (CgA) is the most abundant and widely studied member, encoded by the CHGA gene in humans . These proteins are involved in the formation of secretory granules and the regulated secretion of hormones and neurotransmitters .

Biological Properties

Key Biological Properties: Chromogranin A is an intrinsically disordered protein that can be cleaved into various bioactive peptides, such as vasostatin-1, pancreastatin, and catestatin . These peptides have diverse functions, including modulation of neuroendocrine activities and immune responses .

Expression Patterns and Tissue Distribution: Chromogranin A is widely expressed in neuroendocrine tissues, including the adrenal medulla, pituitary gland, pancreas, and gastrointestinal tract . It is also found in the central and peripheral nervous systems .

Biological Functions

Primary Biological Functions: Chromogranin A serves as a prohormone, giving rise to several bioactive peptides that regulate various physiological processes . These peptides are involved in the modulation of hormone secretion, calcium homeostasis, and glucose metabolism .

Role in Immune Responses and Pathogen Recognition: Chromogranin A-derived peptides, such as catestatin, have antimicrobial properties and play a role in innate immunity . They can modulate immune cell functions and contribute to the body’s defense against pathogens .

Modes of Action

Mechanisms with Other Molecules and Cells: Chromogranin A interacts with various molecules, including catecholamines, serotonin, and histamine, within the secretory granules . These interactions are crucial for the formation and function of neurosecretory granules .

Binding Partners and Downstream Signaling Cascades: Chromogranin A-derived peptides bind to specific receptors on target cells, triggering downstream signaling cascades that regulate cellular functions . For example, catestatin inhibits catecholamine release by binding to nicotinic acetylcholine receptors .

Regulatory Mechanisms

Regulatory Mechanisms Controlling Expression and Activity: The expression of Chromogranin A is regulated at the transcriptional level by various transcription factors . Post-translational modifications, such as phosphorylation and glycosylation, also play a role in modulating its activity and stability .

Transcriptional Regulation and Post-Translational Modifications: Specific transcription factors, such as Sp1 and CREB, bind to the promoter region of the CHGA gene, regulating its transcription . Post-translational modifications, including proteolytic cleavage, generate bioactive peptides from Chromogranin A .

Applications

Biomedical Research: Chromogranin A is used as a biomarker in the diagnosis and monitoring of neuroendocrine tumors, such as pheochromocytomas and carcinoid tumors . Its levels in blood and urine can indicate disease progression and response to treatment .

Diagnostic Tools and Therapeutic Strategies: Chromogranin A-derived peptides have potential therapeutic applications due to their diverse biological activities . For example, catestatin has been studied for its antihypertensive and cardioprotective effects .

Role in the Life Cycle

Role Throughout the Life Cycle: Chromogranin A plays a crucial role in various stages of life, from development to aging . During development, it is involved in the formation of neuroendocrine tissues and the regulation of hormone secretion . In aging and disease, altered levels of Chromogranin A and its peptides are associated with various pathological conditions, including cardiovascular diseases and neurodegenerative disorders .

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