Home > Product > APIs > Calcitonin (salmon)

APIs

Calcitonin (salmon)

Price Inquiry
CAT#
10-101-08
Synonyms/Alias
Salcatonin; Salmon Calcitonin; Thyrocalcitonin (salmon); Ciba 47175-BA; Ciba47175-BA; Calcitrin; Calcitonin(1-32); Calcitonin (1-32); Calcitonin1-32; Calcitonin 1-32; Cibacalcin; UNII-I0IO929019; EINECS 244-276-2
CAS No.
47931-85-1 (net)
Sequence
H-Cys-Ser-Asn-Leu-Ser-Thr-Cys-Val-Leu-Gly-Lys-Leu-Ser-Gln-Glu-Leu-His-Lys-Leu-Gln-Thr-Tyr-Pro-Arg-Thr-Asn-Thr-Gly-Ser-Gly-Thr-Pro-NH2 acetate salt (Disulfide bond)
M.W/Mr.
3431.9
Molecular Formula
C145H240N44O48S2
Source
Synthetic
Long-term Storage Conditions
−20°C
Application
Calcitonin (salmon) stimulates the bone formation and inhibits the bone resorption in postmenopausal osteoporotic women.
Description
Calcitonin (salmon) is a 32-amino acid polypeptide hormone that is produced in humans primarily by the parafollicular cells (also known as C-cells) of the thyroid, and in many other animals in the ultimobranchial body. It acts to reduce blood calcium (Ca2+), opposing the effects of parathyroid hormone (PTH). The calcitonin receptor has been cloned and shown to be a member of the seven-transmembrane, G protein-coupled receptor family.
Areas of Interest
Diseases
  • Background
  • Related Products
  • References

Calcitonin, also called thyrocalcitonin, a protein hormone synthesized and secreted in humans and other mammals primarily by parafollicular cells (C cell) in the thyroid gland. At first it was believed that this hypocalcemic agent was produced by the parathyroid glands. Shortly thereafter, however, it was demonstrated that calcitonin was produced specifically within the parafollicular cells (C cells) of the thyroid gland giving rise to the name 'thyrocalcitonin'. More recent studies have shown calcitonin is also produced by the brain, breast, placenta and other neuroendocrine cells.  >> Read More

CAS: 37025-55-1
Sequence: Butyryl-Tyr(Me)-Ile-Gln-Asn-Cys-Pro-Leu-Gly-NH2(Disulfide bond)
M.W: 988.2
Molecular Formula: C45H69N11O12S
CAS: 38821-49-7
Sequence: ---
M.W: 244.24
Molecular Formula: C10H16N2O5
CAS: 638-23-3
Sequence: H-Cys(carboxymethyl)-OH
M.W: 179.19
Molecular Formula: C5H9NO4S
CAS: 35144-91-3
Sequence: H-Trp-Met-Asp-Phe-NH2 acetate
M.W: 596.71
Molecular Formula: C29H36N6O6S
CAS: 133099-04-4 (net), 133099-07-7 (hydrobromide)
Sequence: ---
M.W: 505.44606
Molecular Formula: C28H29BrN2O2

Calcitonin was originally discovered as a hypocalcemic factor synthesized by thyroid parafollicular C cells. Early experiments demonstrated that calcitonin inhibited bone resorption and decreased calcium efflux from isolated cat tibiae and subsequent histologic and culture studies confirmed the osteoclast as its major site of action. Its potent antiresorptive effect and analgesic action have led to its clinical use in treatment of Paget's bone disease, osteoporosis, and hypercalcemia of malignancy. This review surveys the cellular and molecular basis of these physiologic and clinical actions.

Inzerillo A M, Zaidi M, Huang C L H. Calcitonin: the other thyroid hormone[J]. Thyroid, 2002, 12(9): 791-798.

Calcitonin (CT), a 32 amino acid peptide hormone produced primarily by the thyroid, and its receptor (CTR) are well known for their ability to regulate osteoclast mediated bone resorption and enhance Ca2+ excretion by the kidney. However, recent studies now suggest that CT and CTRs may play an important role in a variety of processes as wide ranging as embryonic/foetal development and sperm function/physiology. In this review article, CT and CTR gene transcription, signal transduction and function are addressed. The effects of CT on the physiology of a variety of organ systems are discussed and the relationship between polymorphisms in the CTR gene and bone mineral density (BMD)/osteoporosis is examined. Recent studies demonstrating the ability of receptor activity modifying proteins (RAMPs) to post-translationally modify the calcitonin receptor-like receptor (CRLR) are detailed and studies employing transgenic mouse technology to determine the temporal and tissue specific transcriptional activity of the CTR gene in vivo are discussed.

Pondel M. Calcitonin and calcitonin receptors: bone and beyond[J]. International journal of experimental pathology, 2000, 81(6): 405-422.

Online Inquiry

First Name:
Last Name:
Phone:
Email: *
Service & Products of Interest: *
Services Required and Project Description:
Verification code: *Please enter the code "peptides"
Home | Site Map | Contact Us | Resources
Copyright © 2008 - Creative Peptides. All rights reserved.