Rabbit Polyclonal CO5A1 antibody. Suitable for IHC-P and reacts with Human samples. Cited in 1 publication.
pH: 8
Preservative: 0.01% Sodium azide
Constituents: 4.77% Sodium borate, 0.43% Sodium chloride, 0.15% EDTA
IHC-P | |
---|---|
Human | Tested |
Cow | Predicted |
Mammals | Predicted |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 5 µg/mL | Notes Perform heat-mediated antigen retrieval before commencing with IHC staining protocol. |
Species | Dilution info | Notes |
---|---|---|
Species Cow, Mammals | Dilution info - | Notes - |
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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.
Collagen alpha-1(V) chain, COL5A1
Rabbit Polyclonal CO5A1 antibody. Suitable for IHC-P and reacts with Human samples. Cited in 1 publication.
pH: 8
Preservative: 0.01% Sodium azide
Constituents: 4.77% Sodium borate, 0.43% Sodium chloride, 0.15% EDTA
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Collagen V also known as collagen type V is a fibrillar collagen integral to the formation and structure of the extracellular matrix. It plays a mechanical role by regulating the assembly of other fibrillar collagens such as type I. Collagen V is a heterotrimer composed of three alpha chains—two α1(V) and one α2(V)—and demonstrates a molecular weight that typically ranges between 180-200 kDa. Expression of collagen type 5 is prominent in connective tissues especially those found in skin tendon and cornea where it ensures proper collagen fibril formation and tissue stability.
Collagen V coordinates with other collagen types to control fibrillogenesis the process by which collagen molecules assemble into fibrils. It exists as part of a complex within the extracellular matrix often found interacting with collagen type I influencing its diameter and the organization of fibrils. This involvement is important for maintaining the structural integrity and mechanical properties of tissues that require a well-organized fibrillar network like the sclera and the dermis.
Collagen V participates in the regulation of the collagen biosynthesis and degradation pathway as well as the TGF-β signaling pathway. It modulates the biosynthesis pathway by ensuring a controlled assembly and deposition of collagen fibrils which is essential for tissue repair and maintenance. Through its influence on the TGF-β signaling pathway collagen type V interacts with proteins such as decorin and biglycan which are also associated with modulating collagen fibril formation and tissue morphogenesis.
Collagen V defects or imbalances can lead to conditions such as Ehlers-Danlos syndrome (EDS) and fibrosis. EDS is associated with mutations in the COL5A1 or COL5A2 genes leading to abnormal collagen V production which affects skin elasticity and joint integrity. Fibrosis involves excessive collagen deposition including collagen type V resulting in tissue stiffening and impaired function. In these disorders surrounding collagens and matrix proteins like decorin may be altered further exacerbating tissue dysfunction.
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Immunohistochemical analysis of formalin-fixed, paraffin-embedded Human skin, dermal collagen labelling Collagen V with ab134800 at 5 µg/ml, after heat-induced antigen retrieval.
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