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Hyaluronidase Sale

(Synonyms: 透明质酸酶; Hyaluronate 4-glycanohydrolase; Hyaluronoglucosaminidase) 目录号 : GC36265

Hyaluronidase (Hyaluronate 4-glycanohydrolase, Hyaluronoglucosaminidase, Amphadase, Hydase, Vitrase) 是一种天然酶,该酶可降解透明质酸。

Hyaluronidase Chemical Structure

Cas No.:37326-33-3

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10mg (10mg/mL in Water)
¥385.00
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10mg
¥350.00
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50mg
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500mg
¥1,680.00
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产品描述

Hyaluronidase degrades hyaluronic acid through the cleavage of glycosidic bonds. Initially discovered in bacteria, this enzyme is known to be widely distributed in nature and has been found in various species, including insects, snakes, fish, and mammals. In humans, six different hyaluronidases have been identified, namely HYAL 1-4, HYAL-P1, and PH-20. PH-20 exhibits the strongest biological activity, with high concentrations found in the testes and localization on the head and acrosome of human sperm. Currently, hyaluronidases sourced from animal testes, such as bovine or ovine, as well as synthetic hyaluronidases, are applied clinically as adjuncts for increasing drug bioavailability, treating extravasation, or managing complications associated with cosmetic injections using hyaluronic acid-based fillers[1].

References:
[1] Buhren B A , Schrumpf H , Hoff N P ,et al. Hyaluronidase: from clinical applications to molecular and cellular mechanisms[J].European Journal of Medical Research, 2016, 21(1).DOI:10.1186/s40001-016-0201-5.

透明质酸酶(Hyaluronidase)通过糖苷键的裂解来解聚透明质酸。透明质酸酶最初在细菌中发现,已知其广泛分布于自然界中,并且已在许多种类中发现,包括昆虫、蛇、鱼和哺乳动物。在人类中,已经鉴定了六种不同的透明质酸酶,HYAL 1-4、HYAL-P1和PH-20。PH-20具有最强的生物活性,在睾丸中发现高浓度,并可定位于人类精子的头部和顶体。如今,动物来源的牛或绵羊睾丸透明质酸酶以及合成透明质酸酶在临床上被应用为用于增加药物生物利用度、用于治疗外渗或用于管理与基于透明质酸的填充剂的美容注射相关的并发症的辅助剂[1]

Chemical Properties

Cas No. 37326-33-3 SDF
别名 透明质酸酶; Hyaluronate 4-glycanohydrolase; Hyaluronoglucosaminidase
Canonical SMILES [Hyaluronoglucosaminidase]
分子式 分子量
溶解度 Water : 100 mg/mL 储存条件 Store at -20°C, protect from light
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Research Update

Clinical Applications of Hyaluronidase

Adv Exp Med Biol 2019;1148:255-277.PMID:31482503DOI:10.1007/978-981-13-7709-9_12.

Hyaluronidases are enzymes that degrade hyaluronic acid, which constitutes an essential part of the extracellular matrix. Initially discovered in bacteria, hyaluronidases are known to be widely distributed in nature and have been found in many classes including insects, snakes, fish and mammals. In the human, six different hyaluronidases, HYAL1-4, HYAL-P1 and PH-20, have been identified. PH-20 exerts the strongest biologic activity, is found in high concentrations in the testicles and can be localized on the head and the acrosome of human spermatozoa. Today, animal-derived bovine or ovine testicular hyaluronidases as well as synthetic hyaluronidases are clinically applied as adjuncts to increase the bioavailability of drugs, for the therapy of extravasations, or for the management of complications associated with the aesthetic injection of hyaluronic acid-based fillers. Further applications in the fields of surgery, aesthetic medicine, immunology, oncology, and many others can be expected for years to come. Here, we give an overview over the molecular and cellular mode of action of Hyaluronidase and the hyaluronic acid metabolism, as well as over current and potential future clinical applications of Hyaluronidase.

The role of Hyaluronidase in the treatment of complications from hyaluronic acid dermal fillers

Aesthet Surg J 2013 Nov 1;33(8):1167-74.PMID:24197934DOI:10.1177/1090820X13511970.

Hyaluronidases, a family of enzymes that are able to degrade hyaluronic acid (HA), are employed in medicine to increase drug diffusion and reverse the effects of HA filler injections. Hyaluronidases are able to dissolve subcutaneous nodules or to correct excessive quantities of injected filler. Knowledge of the use, methods of application, and adverse effects of hyaluronidases is essential for the aesthetic practitioner. Therefore, we performed an extensive review of the available literature from 1928 to 2011 and compared the different enzymes available, recording each author's indications regarding usage and side effects.

Hyaluronidase Caveats in Treating Filler Complications

Dermatol Surg 2015 Dec;41 Suppl 1:S347-53.PMID:26618463DOI:10.1097/DSS.0000000000000555.

Background: Most of the complications associated with hyaluronic acid (HA) fillers can be addressed by Hyaluronidase. Extensive experience with this enzyme was accumulated in ophthalmology and anesthesia. In dermatologic use multiple aspects still remain controversial. Objective: To elucidate questions with regard to Hyaluronidase use in HA-induced complications, including appropriate dosage, timing, and technique of delivery, differences in the activity of hyaluronidases of different origins, interaction between the enzymes and different HA gels, and safety issues. Materials and methods: Extensive review of the relevant literature was conducted. The conclusions are based on this review and personal author's experience. Results: FDA-approved hyaluronidases provide predictable results and can be used interchangeably. A physician has to be closely familiar with specific characteristics of other hyaluronidases. Different brands of HA fillers have different sensitivity to degradation by Hyaluronidase. For filler overcorrection or misplacement, low dose of the enzyme has to be injected directly into the palpable HA mass. In case of vascular accident, flushing of the ischemic area with high doses of Hyaluronidase is required. Hypersensitivity reactions to Hyaluronidase are so far not reported in dermatologic literature. Conclusion: With increased popularity of HA fillers, Hyaluronidase had become an indispensable tool in dermatology office. It is safe and reliable for treatment of HA-induced complications.

Hyaluronidase and its substrate hyaluronan: biochemistry, biological activities and therapeutic uses

Cancer Lett 1998 Sep 11;131(1):3-11.PMID:9839614DOI:10.1016/s0304-3835(98)00195-5.

This is an overview of the biochemistry, biological function and therapeutic uses of Hyaluronidase and its substrate, hyaluronate. We focus on the role of hyaluronate and its receptor CD44 in cell-cell and cell-matrix adhesion and cell activation as well as on the putative role of hyaluronate and Hyaluronidase in morphogenesis. Variants of CD44 and their putative role in tumor metastasis are also included. Other topics that are discussed are the chemical and enzymatic nature of Hyaluronidase, i.e. the mode of substrate degradation, pharmacodynamical and pharmacokinetic aspects of this enzyme and its role as spreading factor. Purification methods, possible contaminations and techniques of activity determinations are mentioned as well as the physiological role of Hyaluronidase and tumor-associated alterations in serum and tissue enzyme levels. As far as therapeutic applications are concerned, we discuss uses of Hyaluronidase in ophthalmology and regional anesthesia as well as pain management in osteoarthritis using hyaluronate.

Hyaluronidase inhibitors: a biological and therapeutic perspective

Curr Med Chem 2009;16(18):2261-88.PMID:19519390DOI:10.2174/092986709788453078.

The hyaluronidases (HAases) are a group of less extensively studied glycosidases distributed throughout the animal kingdom and are popularly known as 'spreading factors'. In recent years, HAases received much attention due to their ability to abruptly alter the hyaluronic acid (HA) homeostasis. HAases preferentially degrade HA, which is a megadalton acidic structural polysaccharide found exclusively in the extracellular matrix (ECM) of animals. The HA-HAase system has been suggested to participate in many pathophysiological conditions. The HA degradation in ECM, crack down the structural integrity with an eventual increased tissue permeability that is attributed for the spreading property. The spreading property has been widely accepted in functions including envenomation, acrosomal reaction/ovum fertilization, cancer progression, microbial pathogenesis such as wound infections, pneumonia, and other sepses like, bacteremia and meningitis. HA fragmentation has dual effects; generation of a wide molecular range bioactive oligosaccharides of angiogenic, pro-inflammatory, and immunostimulatory properties; and impairment in the reservoir capacity of ECM that holds metal ions, growth factors, cytokines and various enzymes for signal transduction. Hence, inhibition of HA degradation appears critical and imperative in HAase mediated pathological conditions. HAase inhibitors are thus potent regulators that maintain HA homeostasis and they might serve as anti-inflammatory, anti-aging, anti-microbial, anticancer and anti-venom/toxin and contraceptive agents. In addition, HAase inhibitors may serve as tools to understand several unexplained and complex functions of HAases in HA metabolism. Therefore, this review is expected to provide an integrated update as of 2008 on the HAase inhibitors and their possible role as therapeutics in the management of a wide range of pathological conditions.