Hyaluronic Acid, Bovine [9067-32-7]

Cat# H7980-11-10mg

Size : 10mg

Brand : US Biological

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H7980-11 Hyaluronic Acid, Bovine

Grade
Molecular Biology Grade
Shipping Temp
Blue Ice
Storage Temp
4°C Do Not Freeze

Suitable as a substrate for hyaluronidase assays. The hyaluronic acids (HA) are a class of macromolecular proteoglycans characterized by a highly polymerized chain of glucuronic acid and N-acetylglucosamine units bonded to protein. They exist in nature as a hydrated gel, usually closely associated with other tissue components such as chrondroitin sulfate. Hyaluronic acid (HA) preparations have variable molecular weights depending on purification procedures, the extent of degradation, as well as the source. The range of molecular weight is 70kD to 2,000-4,000kD in a highly polymerized preparation. Bovine vitreous humor HA has a lower molecular weight than most other sources. The hyaluronic acids are a class of macromolecular proteoglycans characterized by a highly polymerized chain of the repeating disaccharide glucuronic acid β-(1-3) N-acetylglucosamine (β1-4).

The molecular weight of HA preparations varies with purification procedures, i.e., the extent of degradation as well as the source. According to Bettelheim (1958) when the protein is completely removed a molecular weight on the order of 70,000 is obtainable as compared with 2-4 million in a highly polymerized preparation (Laurent and Gergely 1955). It has been reported (Laurent et al. 1960) that bovine vitreous humor hyaluronic acid has a lower molecular weight than most other sources and that from human umbilical cord has the largest molecular weight (Jensen and Carlsen 1954). Pigman et al. (1961) report that HA is degraded in the presence of oxygen and reducing agents and by merthiolate, often used in its preparation. Ascorbic acid likewise has this effect (Swann 1967). The carbohydrate polymer is negatively charged. When it is mixed with a cationic protein such as albumin at low pH, a precipitate is formed. If the glycosidic bonds have been split, i.e., the chain depolymerized, this precipitation no longer occurs. This phenomenon is the basis for the turbidimetric assay of hyaluronidase.

Synonyms:
Poly(b-glucuronic acid-[1→3]-b-N-acetylglucosamine-[1→4]); Arthrease; Artz; Artz Dispo; Artzal; Bio Hyaluro 12; Bio Sodium Hyaluronate HA 20; Chlamyhyaluronic acid sodium salt; Cystistat; Euflexxa; FCH 121-S; FCH 150; FCH 200; FCH 248; FCH 60; FCH 80; FCH 80LE; FCH-SU; Fermatron; HA-F; HA-Q; HA-Q 1; HA-QA; HE-QSE; Healon; Healon (polysaccharide); Healon GV; Healon V; Hyalart; Hyalein; Hyalein Mini; Hyalgan; Hyaluronsan HA-LQ; Hyaluronsan HA-LQ1; Hyaluronsan HA-LQH; Hyaluronsan HA-Q; Hyaluronsan HA-QSS; Hyaluronsan M 5070; Hyasol; Hyasol BT; Hyladerm; Hylo Comod; Jointex; Khionat; NRD 101; Nidelon; Opegan; Orthovisc; Ostenil; Provisc; SI 4402; SL 1010; SLM 10; SPH; Sinovial; Sodium hyaluronate; Suvenyl; Tear Balance; Vismed

CAS No:
9067-32-7

Molecular Formula:
(C₁₄H₂₀NaNO₁₂)n

Molecular Weight:
80-120kD

Purity:
Purified

Form:
White to off-white lyophilized powder

Specificity:
Suitable as a substrate for hyaluronidase assays

Storage and Stability:
Lyophilized and reconstituted products are stable for 6 months after receipt at 4°C. Do not freeze. Reconstitute with sterile buffer or ddH2O. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Applications
Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological. Toxicity and Hazards: All products should be handled by qualified personnel only, trained in laboratory procedures.
Form
White to off-white lyophilized powder
References
1. Atkins, E., and Sheehan, J., Nature New Biol 235:253, 1972. 2. Barrett, T., Biochim Biophys Acta 385:157, 1975. 3. Bettelheim, F., Nature 182:1301, 1958. 4. Bettelheim, F., and Philpott, D., Biochim Biophys Acta 34:124, 1959. 5. Block, A., and Bettelheim, F., Biochim Biophys Acta 201:69, 1970. 6. Blumberg, B., Oster, G., and Meyer, K., J Clin Invest 34:1454, 1955. 7. Cowman, M., Cozart, D., Nakanishi, K., and Balazs, E., Arch Biochem Biophys 230:203, 1984. 8. Frost, S., and Weigel, P., Biochim Biophys Acta 1034:39, 1990. 9. Hardingham, T., and Muir, H., Biochem Soc Trans 1:282, 1973. 10. Jacoboni, I., Mori, V., Quaglino Jr., D., and Pasquali-Ronchetti, I., J Struct Biol 126:52, 1999. 11. Jensen, C., and Carlsen, F.: Acta Chem Scand 8:1357, 1954