|Place of Origin:||China|
|Certification:||ISO 9001, USP,GMP|
|Minimum Order Quantity:||10 Vials|
|Packaging Details:||Disguised pacakge|
|Delivery Time:||3~5 work days|
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|Supply Ability:||Mass in stock|
|Melting Point:||192-194°C||Storage Temp.:||2-8°C|
|Form:||Lyophilized Powder||Grade:||Pharmaceutical Grade|
muscle growth peptides,
human growth hormone powder
Human Growth Hormone Peptide Oxytocin For Facilitate Birth
Appearance: White Lyophilized Powder
Export Markets: Global
Storage: Lyophilized peptides although stable at room temperature for 3 months, should be stored desiccated below -18° C. Upon reconstitution of the peptide it should be stored at 4° C between 2-21 days and for future use below -18° C.
Oxytocin is a mammalian hormone that acts primarily as a neuromodulator in the brain. Oxytocin is best known for its roles in sexual reproduction, in particular during and after childbirth. It is released in large amounts after distension of the cervix and uterus during labor, facilitating birth, and after stimulation of the nipples, facilitating breastfeeding. The word oxytocin was derived from the Greek word", meaning quick birth. The oxytocin peptide is synthesized as an inactive precursor protein from the OXT gene.
Oxytocin is a peptide of nine amino acids (a nonapeptide). Its systematic name is cysteine-tyrosine-isoleucine-glutamine-asparagine-cysteine-proline-leucine-glycine-amine (cys, tyr, ile,gln,asn,cys, pro, leu, gly - NH2, or CYIQNCPLG-NH2). The cysteine residues form a disulfide bond. Oxytocin has a molecular mass of 1007 daltons. One international unit (IU) of oxytocin is the equivalent of about 2 micrograms of pure peptide. The trust-inducing property of oxytocin might help those who suffer from social anxieties and mood disorders, but with the potential for abuse with confidence tricks and military applications.
The structure of oxytocin is very similar to that of vasopressin (cys,tyr,phe, gln,asn,cys, pro,arg,gly - NH2), also a nonapeptide with a sulfur bridge, whose sequence differs from oxytocin by two amino acids. A table showing the sequences of members of the vasopressin/oxytocin super family and the species expressing them is present in the vasopressin article. Oxytocin and vasopressin were isolated and synthesized by Vincent du Vigneaud in 1953, work for which he received the Nobel Prize in Chemistry in 1955. Oxytocin and vasopressin are the only known hormones released by the human posterior pituitary gland to act at a distance. However, oxytocin neurons make other peptides, including corticotropin-releasing hormone and dynorphin, for example, that act locally. Oxytocin has peripheral (hormonal) actions, and also has actions in the brain. Its actions are mediated by specific, high-affinity oxytocin receptors. The oxytocin receptor is a G-protein-coupled receptor that requires Mg2+ and cholesterol.
Oxytocin is a powerful hormone. When we hug or kiss a loved one, oxytocin levels drive up. It also acts as a neurotransmitter in the brain. In fact, the hormone plays a huge role in pair bonding. Prairie voles, one of nature's most monogamous species, produce oxytocin in spades. This hormone is also greatly stimulated during sex, birth, breast feeding
Oxytocin secreted from the pituitary gland cannot re-enter the brain because of the blood-brain barrier. Instead, the behavioral effects of oxytocin are thought to reflect release from centrally projecting oxytocin neurons, different from those that project to the pituitary gland. Oxytocin receptors are expressed by neurons in many parts of the brain and spinal cord, including the amygdala, ventromedial hypothalamus, septum and brainstem.
The oxytocin peptide is synthesized as an inactive precursor protein from the OXT gene. This precursor protein also includes the oxytocin carrier protein neurophysin.
The inactive precursor protein is progressively hydrolyzed into smaller fragments (one of which is neurophysin I) via a series of enzymes. The last hydrolysis that releases the active oxytocin nonapeptide is catalyzed by peptidylglycine alpha-amidating monooxygenase (PAM).
The activity of the PAM enzyme system is dependent upon vitamin C (ascorbate), which is a necessary vitamin cofactor. By chance, sodium ascorbate by itself was found to stimulate the production of oxytocin from ovarian tissue over a range of concentrations in a dose-dependent manner. Many of the same tissues (e.g. ovaries, testes, eyes, adrenals, placenta, thymus, pancreas) where PAM (and oxytocin by default) is found are also known to store higher concentrations of vitamin C.
Oxytocin is known to be metabolized by the oxytocinase, leucyl/cystinyl aminopeptidase. Other oxytocinases are also known to exist. Amastatin, bestatin (ubenimex), leupeptin, and puromycin have been found to inhibit the enzymatic degradation of oxytocin, though they also inhibit the degradation of various other peptides, such as vasopressin, met-enkephalin, and dynorphin A.
In the hypothalamus, oxytocin is made in magnocellular neurosecretory cells of the supraoptic and paraventricular nuclei, and is stored in Herring bodies at the axon terminals in the posterior pituitary. It is then released into the blood from the posterior lobe (neurohypophysis) of the pituitary gland. These axons (likely, but dendrites have not been ruled out) have collaterals that innervate neurons in the nucleus accumbens, a brain structure where oxytocin receptors are expressed. The endocrine effects of hormonal oxytocin and the cognitive or behavioral effects of oxytocin neuropeptides are thought to be coordinated through its common release through these collaterals. Oxytocin is also produced by some neurons in the paraventricular nucleus that project to other parts of the brain and to the spinal cord. Depending on the species, oxytocin receptor-expressing cells are located in other areas, including the amygdala and bed nucleus of the stria terminalis.
In the pituitary gland, oxytocin is packaged in large, dense-core vesicles, where it is bound to neurophysin I as shown in the inset of the figure; neurophysin is a large peptide fragment of the larger precursor protein molecule from which oxytocin is derived by enzymatic cleavage.
Secretion of oxytocin from the neurosecretory nerve endings is regulated by the electrical activity of the oxytocin cells in the hypothalamus. These cells generate action potentials that propagate down axons to the nerve endings in the pituitary; the endings contain large numbers of oxytocin-containing vesicles, which are released by exocytosis when the nerve terminals are depolarised.
Endogenous oxytocin concentrations in the brain have been found to be as much as 1000-fold higher than peripheral levels.
Outside the brain, oxytocin-containing cells have been identified in several diverse tissues, including in females in the corpus luteum and the placenta, in males in the testicles' interstitial cells of Leydig, the retina, the adrenal medulla, the thymus and the pancreas. The finding of significant amounts of this classically "neurohypophysial" hormone outside the central nervous system raises many questions regarding its possible importance in these different tissues.
The Leydig cells in some species have been shown to possess the biosynthetic machinery to manufacture testicular oxytocin de novo, to be specific, in rats (which can synthesize vitamin C endogenously), and in guinea pigs, which, like humans, require an exogenous source of vitamin C (ascorbate) in their diets.
Oxytocin is synthesized by corpora lutea of several species, including ruminants and primates. Along with estrogen, it is involved in inducing the endometrial synthesis of prostaglandin F2α to cause regression of the corpus luteum.
Virtually all vertebrates have an oxytocin-like nonapeptide hormone that supports reproductive functions and a vasopressin-like nonapeptide hormone involved in water regulation. The two genes are usually located close to each other (less than 15,000 bases apart) on the same chromosome, and are transcribed in opposite directions (however, in fugu, the homologs are further apart and transcribed in the same direction).
The two genes are believed to result from a gene duplication event; the ancestral gene is estimated to be about 500 million years old and is found in cyclostomata (modern members of the Agnatha).
Oxytocin has peripheral (hormonal) actions, and also has actions in the brain. Its actions are mediated by specific, oxytocin receptors. The oxytocin receptor is a G-protein-coupled receptor that requires magnesium and cholesterol. It belongs to the rhodopsin-type (class I) group of G-protein-coupled receptors.
Studies have looked at oxytocin's role in various behaviors, including orgasm, social recognition, pair bonding, anxiety, and maternal behaviors.
Usage and dosage
1. Odinopoeia or oxytocin intravenous drip, once the 2.5 - 5 units, with Sodium Chloride Injection diluted to each 1ml contains 0.01 units. Intravenous drip of the beginning of every minute of not more than 0.001 to 0.002 units, each 15 - 30 minutes increased 0.001 to 0.002 units, to achieve the contractions and normal childbirth is similar, the fastest per minute of not more than 0.02 units, usually 0.002 to 0.005 units per minute.
2. Control postpartum hemorrhage per minute intravenous drip of 0.02 - 0.04 units, expulsion of the placenta after intramuscular injection of 5 to 10 units.
3. Lactogenic just before a 2 - 3 minutes, with nasal drops a 3 drop, drop into one side or both sides of the nostril.
Preparation and specification : oxytocin injection (1) 0.5ml:2.5 units (2) 1ml:5 (3) 1ml units 10 units;
4. Oxytocin nasal drops 1ml:40 units.
The induction of labor or prenatal uterine atony: in 2.5-5 units in 500ml 5% glucose for intravenous drip slowly (10-30 drops / minute), maximum time 20 units. (2). Prevention of postpartum hemorrhage: intramuscular injection of 5-10 on each unit, or 5% glucose solution for intravenous drip.
5. The main contraindication heart disease, a Caesarean history and more than three fetal maternal disable.
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