Collagen

Collagen is the most abundant mammalian protein and the main component of connective tissues. Typically collagen is first synthesized as individual glycine-rich preprocollagen monomeric strands from the ribosomes in the rough endoplasmic reticulum (RER). After transport to the lumen of the RER signal peptides are cleaved to yield procollagen. Lysine and proline are hydroxylated and glycosylated in the lumen and a helix composed of three peptides is formed. It is then transported to the Golgi and excreted from the cell by exocytosis. Procollagen's propetides are then removed to yield tropocollagen which may join together to form fibrils. The "collagen type" designations of Bornstein and Traub is determined by the peptide composition of the triple helix.

Collagen Type specific diagrams

Collagen Illustration

Collagen Type	Chain Composition	Gene Symbol(s) for Peptide Chains	Localization/Function
Type I			The most abundant collagen type: found in bone, tendon, ligament, blood vessels, intervertebral disks
	Two α1(I), one α2(I)	COL1A1, COL1A2
	Product No.	Sigma Type	Suitability Testing	Form	Species	Source
	C4387	V	Substrate	Powder	Bovine	achilles tendon
	C9879		Substrate	Powder	Bovine	achilles tendon
	C3511	III		Powder	Bovine	calf skin
	C8919			Solution	Bovine	calf skin
	C9791		Cell Culture	Powder	Bovine	calf skin
	C5983			Powder	Human	lung
	C7774	VII		Powder	Human	placenta
	C5483			Powder	Human	skin
	C1809	I	Cell Culture	Powder	Kangaroo	tail
	C8897	VII		Powder	Rat	tail
	C3929			Powder	Kangaroo	tail
	C7661		Cell Culture	Powder	Rat	tail
	C5608			Powder	Rabbit
	C2124		Cell Culture	Solution	Bovine	hide
	C2249		Cell Culture	Solution	Human
Type II			Major protein component of cartilage
	Three α1(II)	COL2A1	Major protein component of cartilage
	Product No.	Sigma Type	Suitability Testing	Form	Species	Source
	C7806			Powder	Bovine	nasal septum
	C9301		Cell Culture	Powder	Chicken	sternal cartilage
	C5733			Powder	Murine	sternum
	C1188			Powder	Bovine	tracheal cartilage
Type III			The second most abundant collagen type: found colocalized with Type I in elastic tissues such as skin and blood vessels
	Three α1(III)	COL3A1
	Product No.	Sigma Type	Suitability Testing	Form	Species	Source
	C4407	X		Powder	Human	placenta
Type IV			Primary protein component of the basal lamina
	Predominantly Two α1(IV) and one α2(IV), heterotrimers may be composed of six different α(IV)chains	COL4A1, COL4A2, COL4A3, COL4A4, COL4A5, COL4A6	Primary protein component of the basal lamina
	Product No.	Sigma Type	Suitability Testing	Form	Species	Source
	C7521	VI		Powder	Human	placenta
	C5533		Cell Culture	Powder	Human	placenta
	C0543		Cell Culture	Powder	Murine	basement membrane
Type V			May be associated with collagen fibril organization and epithelial cell cycle inhibition
	One α1(V), one α2(V), one α3(V)	COL5A1, COL5A2, COL3A3
	Product No.	Sigma Type	Suitability Testing	Form	Species	Source
	C3657	IX		Powder	Human	placenta
Type VI			Found in most interstitial tissue, functions to anchor cells to the ECM framework, binds to the core protein component of decorin
	One α1(VI), one α2(VI), one α3(VI)	COL6A1, COL6A2, COL6A3
Type VII			Anchoring fibrils of the subbasal lamina underlying epithelia
	Three α1(VII)	COL7A1
Type VIII			A nonfibrillar short-chain collagen associated vascular endothelial cells and connective tissue
	Three α1(VIII)	COL8A1, COL8A2
Type IX			Covalently cross-linked to Type II collage in cartilage
	One α1(IX), one α2(IX), one α3(IX)	COL9A1, COL9A2, COL9A3	Covalently cross-linked to Type II collage in cartilage
Type X			Associated with the hypertrophic chondrocytes growth plate during endochondral growth of long bones
	Three α1(X)	COL10A1
Type XI			Closely related to Type V collagen
	One α1(XI), one α2(XI), one α3(XI)	COL11A1, COL11A2	Closely related to Type V collagen
Type XII			Some sequence homology with Type IX. Present in tendons, ligaments, perichondrium, and periosteum, tissues containing Type I collagen
	α1(XII)	COL12A1

(Click image to enlarge.)

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