Fragment 176-191

Fragment 176-191

Fragment 176-191 (also recognized in metabolic literature as hGH Fragment 176-191 or its stabilized tyrosine-modified variant, AOD9604) is a synthetic polypeptide fragment replicating the terminal C-terminus region of human growth hormone (somatotropin). Composed of a distinct 16-amino acid sequence, this molecule is highly utilized in endocrinology and lipolysis research models.

Because it represents an isolated region of the parent hormone, it completely lacks the growth-promoting, IGF-1-mediated, and insulin-sensitizing binding domains found on the full somatotropin structure. This structural restriction allows investigators to safely study the independent, localized lipid-regulatory behaviors of the growth hormone molecule in isolated in vitro configurations.

Technical Specifications

Research Applications & Mechanism of Interest

The primary value of Fragment 176-191 in laboratory settings is its highly localized action on cellular fat matrices without triggering generalized systemic growth cascades.

Primary fields of in vitro and cell culture laboratory investigation include:

• Lipid Pathway Mapping: Observing how the C-terminal sequence interacts with lipid-dense matrices in cultured adipocyte lines. Researchers utilize this compound to track beta-3 adrenergic receptor cross-talk and subsequent changes in cyclic adenosine monophosphate (cAMP) levels.

• Disulfide Stability Studies: Evaluating the chemical stability and cleavage rate of the internal disulfide loop formed between the Cys7 and Cys14 residues. This loop creates a specific rigid cyclic conformation that is heavily scrutinized under shifting electrochemical, pH, and enzymatic conditions.

• Enzymatic Degradation Analysis: Tracking the susceptibility of the linear peptide bonds to ambient serum peptidases, allowing researchers to evaluate structural modifications that might extend the compound’s analytical lifespan.

• Secondary Messenger Translocation: Monitoring the movement of intracellular molecules across cell membranes following compound introduction to map the precise cascade of non-growth hormone receptor (GHR) signaling loops.

Storage & Handling Guidelines

To secure complete peptide chain uniformity, shield the terminal amino acids from enzymatic breakdown, and ensure high cross-batch reproducibility:

• Lyophilized Powder Management: The dry, solid reference powder is stable at room temperature (15–25°C) for short intervals if kept out of direct light. For long-term chemical archiving, the material must be stored continuously in a frozen state at -20°C or below.

• Reconstituted Assay Solutions: Once dissolved in ultra-pure molecular water or sterile laboratory saline lines, store liquid stocks inside a regulated refrigeration environment at 2–8°C. Use solutions within 10–14 days to prevent gradual hydrolytic degradation.

• Atmospheric Protection: Keep all container caps tightly and hermetically sealed within a desiccated environment to isolate the lyophilized cake from atmospheric moisture ingress.

• Aseptic Manipulation: Always deploy sterile laboratory equipment, clean working surfaces, and calibrated pipettes during reconstitution to ensure the product remains free of bacterial or chemical contaminants.

• Analytical Auditing Validation: Kimera Chems subjects every batch to a strict dual-method verification protocol combining High-Performance Liquid Chromatography (HPLC) and Mass Spectrometry (MS) to independently audit structural identity, precise mass distribution, and an absolute purity baseline of ≥98.0%.

Research Use Only Disclaimer: This product is developed, synthesized, and distributed strictly as a Research Use Only (RUO) laboratory reference material designed exclusively for non-clinical analytical and scientific investigation. It is not an FDA-approved drug formulation, active pharmaceutical ingredient, or dietary supplement, and is strictly prohibited for direct human or veterinary consumption. Kimera Chems supplies these high-purity peptide batches solely to accredited institutional laboratories, academic departments, and certified investigators.