Anti-Collagen Type V (RABBIT) Antibody Peroxidase Conjugated
Collagen Type V Antibody Peroxidase Conjugated
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Host | Rabbit |
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Conjugate | Peroxidase (Horseradish) |
Target Species | Mammalian |
Reactivity | Human, Bovine |
Clonality | Polyclonal |
Application ![]()
| WB, IHC, E, IP, I, LCI |
Application Note | Anti-Collagen V Peroxidase Conjugated Antibody was assayed by immunoblot and found to be reactive against Collagen V at a dilution of 1:5,000 to 1:10,000. This product was also assayed against 1.0 ug of Collagen V in a standard sandwich ELISA using Peroxidase Conjugated Streptavidin #S000-03 and ABTS (2,2’-azino-bis-[3-ethylbenthiazoline-6-sulfonic acid]) code # ABTS-100 as a substrate for 30 minutes at room temperature. A working dilution of 1:4,000 to 1:8,000 of the stock concentration is suggested for this product. For immunohistochemistry on frozen tissue sections dilute the product 1:50 to 1:200. |
Physical State | Lyophilized |
Buffer | 0.01 M Sodium Phosphate, 0.25 M Sodium Chloride, pH 7.2 |
Immunogen | Collagen Type V from human and bovine placenta |
Reconstitution Volume | 50 µL |
Reconstitution Buffer | Restore with deionized water (or equivalent) |
Stabilizer | 10 mg/mL Bovine Serum Albumin (BSA) - Immunoglobulin and Protease free |
Preservative | 0.01% (w/v) Thimerosal |
Gene ID | 50509 |
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Other Names | 50509 |
Purity | Anti-Collagen V has been prepared by immunoaffinity chromatography using immobilized antigens followed by extensive cross-adsorption against other collagens, human serum proteins and non-collagen extracellular matrix proteins to remove any unwanted specificities. Some class specific anti-collagens may be specific for three-dimensional epitopes which may result in diminished reactivity with denatured collagen or formalin-fixed, paraffin embedded tissues. This antibody reacts with most mammalian Type V collagens and has negligible cross-reactivity with Type I, II, III, IV and VI collagens. Non-specific cross reaction of anti-collagen antibodies with other human serum proteins or non-collagen extracellular matrix proteins is negligible. |
Storage Condition | Store vial at 4° C prior to restoration. Restore with 0.05 mL of deionized water (or equivalent). For extended storage aliquot contents and freeze at -20° C or below. Avoid cycles of freezing and thawing. Centrifuge product if not completely clear after standing at room temperature. This product is stable for several weeks at 4° C as an undiluted liquid. Dilute only prior to immediate use. |
Precautions Note | This product is for research use only and is not intended for therapeutic or diagnostic applications. |
Name | COL5A3 |
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Function | Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin. |
Cellular Location | Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. Secreted |
Tissue Location | Detected in fibroblasts (at protein level) (PubMed:36213313). Detected in urine (at protein level) (PubMed:37453717). |

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Provided below are standard protocols that you may find useful for product applications.
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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