Bovine Collagen Type V
$50.00 to US & $70.00 to Canada for most products. Final costs are calculated at checkout.
Background
In muscle tissue, collagen serves as a major component of the endomysium. Collagen constitutes one to two percent of muscle tissue, and accounts for 6% of the weight of strong, tendinous muscles. A collagen may be defined as a protein containing sizable domain(s) of triple-helical conformation. Type IV collagen is a major macromolecular constituent of basement membranes and can be readily isolated from basement-membrane-rich tissues or highly vascularized tissues such as the placental villi. This collagen appears to be largely restricted to structures identifiable as basement membranes. In contrast, type VI collagen appears to be prevalent in several tissues even though it has been isolated largely from placental villi preparations. The extent to which type VII and VIII collagens are distributed is not known.
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What is the source of the collagen proteins?
Collagen proteins are purified from bovine or human placenta and the purity of the protein is analyzed by SDS-PAGE.
How are the collagen proteins purified?
The proteins were purified by a proprietary method that includes mechanical separation and salt precipitation. Due to the nature and close association of certain collagen proteins, it is difficult to fully separate each collagen.
In what format are the collagen proteins provided?
Collagen proteins are provided in liquid format at a concentration of around 1 mg/mL. The collagen proteins are solubilized, maintaining their native structure. No enzymatic treatment is performed. The low pH of the buffer is essential in maintaining the solubility of the collagen protein.
In what buffer are the collagen proteins provided?
0.5 M Acetic Acid, pH 2.5 with 0.01% (w/v) Sodium Azide.
What are the recommended SDS-PAGE conditions for collagen proteins?
The recommended buffer for SDS-PAGE is 2X SDS buffer with 8 M Urea. The low pH of the buffer maintains the solubility of the collagen proteins. Also, low-density gels such as 3-8% Tris Acetate should be used. Collagen proteins can be reduced with DTT.
What are the recommended storage conditions for collagen proteins?
Collagen proteins should always be stored at 4°C. It is important to never let the collagen proteins freeze because this will degrade the protein. Please be sure to maintain 4°C temperature during assays such as SDS-PAGE.
How was the concentration determined?
The concentration of the collagen proteins was measured by absorbance via nanodrop at 205 nm. When measuring concentration, please be sure to blank with the same buffer as the protein product (0.5 M Acetic Acid).
Are collagen proteins suitable for cell culture?
Since no testing for endotoxin or other contaminants was performed, we do not recommend the use of this product for cell culture.
This product is for research use only and is not intended for therapeutic or diagnostic applications. Please contact a technical service representative for more information. All products of animal origin manufactured by Rockland Immunochemicals are derived from starting materials of North American origin. Collection was performed in United States Department of Agriculture (USDA) inspected facilities and all materials have been inspected and certified to be free of disease and suitable for exportation. All properties listed are typical characteristics and are not specifications. All suggestions and data are offered in good faith but without guarantee as conditions and methods of use of our products are beyond our control. All claims must be made within 30 days following the date of delivery. The prospective user must determine the suitability of our materials before adopting them on a commercial scale. Suggested uses of our products are not recommendations to use our products in violation of any patent or as a license under any patent of Rockland Immunochemicals, Inc. If you require a commercial license to use this material and do not have one, then return this material, unopened to: Rockland Inc., P.O. BOX 5199, Limerick, Pennsylvania, USA.
