Hemorphin-7 6x5mg


Hemorphin-7 is a hemorphin peptide, an endogenous opioid peptide derived from the β-chain of hemoglobin. Hemorphin peptides exhibit antinociceptive and antihypertensive activities, activating opioid receptors and inhibiting angiotensin-converting enzyme (ACE).

• Increase the blood plasma levels of immunoreactive hemorphin-7
• Anti-inflammatory response in acute and chronic injuries
• Reduces Blood Pressure
• Supports oxygen transport from lung to various peripheral tissues
• Reduce stiffness and aids in flexibilty

Brochure Fact Sheet



Purity: > 95%
Molecular Formula: C49H64N12O11
Molecular Weight: 997.110
Sequence (three-letter code): {TYR}{PRO}{TRP}{THR}{GLN}{ARG}{PHE}

Hemorphins are opioid peptides derived by proteolysis from hemoglobin. Their sequences are identical in several mammalian species including horses and camels. LVV‐hemorphin 7 (LVVYPWTQRF) binds strongly to the Angiotensin IV (AT4) receptors in the brain. The AT4 receptor is an integral membrane aminopeptidase also known as IRAP (insulin‐ regulated membrane aminopeptidase). LVV‐hemorphin 7 and AT4 are not substrates but rather inhibitors of the AT4 (IRAP) receptor. Both promote learning and memory and reverse amnesia in animal models. Elevated serum levels of LVV Hemorphin 7 have also been documented in patients with some forms of breast cancers that are associated with an increased expression of Cathespins B and D.

Dosing Protocol
Use 1 vial mixed with 2.5ml sterile water, sub-contaneus (under the skin). For best results use 1x 5mg vial every 5 days for 6 treatments.

6x5mg HEMORPHIN 7 (99%).

Keep Refrigerated when possible and out of direct sunlight.

Clinical Research
In the current study, a series of alanine-substituted and N- or C-terminally modified analogs of LVV-hemorphin-7 were evaluated for their abilities to compete for 125I-Ang IV binding in horse adrenal and cerebellar membranes.

Selected analogs were also analyzed for binding to recombinant human IRAP and inhibition of IRAP aminopeptidase activity. C-Terminal deletions of LVV-hemorphin-7 resulted in modest changes in affinity for IRAP, whereas deletion of the first three N-terminal residues abolished binding. Monosubstitutions of Tyr4 and Trp6 with alanine resulted in a 10-fold reduction in affinity. Competition binding studies using recombinant horse IRAP demonstrated the same rank order of affinity as obtained for the ovine tissues. All LVV-hemorphin-7 analogs tested, except for Leu-Val-Val-Tyr, inhibit the cleavage of the synthetic substrate, leucine -naphthylamide, by IRAP,with Ki values between 56 and 620 nM. We find that the Val3 residue is crucial for LVV-hemorphin-7 binding to IRAP, whereas the C-terminal domain seems to play a minor role. The current study highlights the minimal residues necessary for binding and inhibition of IRAP and provides a basis to design peptidomimetic analogs for experimental and potentially clinical use

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