抗Collagen I alpha 1 (COL-1)抗体 | Anti-Collagen I alpha 1 (COL-1) Antibody

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Image

	Western Blot: Collagen I alpha 1 Antibody (COL-1) [NB600-450] - Analysis of collagen 1. Lane 1: 3 ug Recombinant human collagen 1. Lane 2: 20 ug pig skin whole cell lysate extracted with laemmli buffer.
	Immunohistochemistry-Frozen: Collagen I alpha 1 Antibody (COL-1) [NB600-450] - Staining of acetone-fixed, frozen sections of pig tongue at a dilution of 1:4000
	Immunocytochemistry: Collagen I alpha 1 Antibody (COL-1) [NB600-450] - Collagen I alpha1 labeled pig trabecular meshwork cells indirectly visualized with Alexa488 conjugated secondary antibody. This image was submitted via customer Review.
	Immunohistochemistry: Collagen I alpha 1 Antibody (COL-1) [NB600-450] - Analysis of a formalin/pfa fixed paraffin embedded ligament section. Enzymatic antigen retrieval and blocking using 1% BSA for 30 min at 20C was performed. Sample was incubated for 1 hour with primary antibody at a dilution of 1/400 at 20C.
	Immunohistochemistry-Frozen: Collagen I alpha 1 Antibody (COL-1) [NB600-450] - Staining of acetone-fixed, frozen sections of human tongue at a dilution of 1:2000
	Immunohistochemistry: Collagen I alpha 1 Antibody (COL-1) [NB600-450] - Analysis of formalin fixed frozen porcine skin tissue sections. Blocking: 5% serum for 1 hr at 20C. Sample was incubated for 16 hours at 4C and used at a dilution of 1/500.
	Immunocytochemistry: Collagen I alpha 1 Antibody (COL-1) [NB600-450] - Analysis of Collagen I alpha 1 in 4% PFA fixed equine tenocytes using anti-Collagen I alpha 1 antibody. Image from verified customer review.

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Background

The extracellular matrix is the material found in the extracellular environment of all tissues and organs. It consists of basement membranes and interstitial stroma. The composition of the extracellular framework of all vertebrates is dominated by a class of molecules known as collagens,1 each with unique features suited for its function and location. The collagens are proteins composed of three subunit polypeptides that can vary in length, which interact to form a triple helix. The molecular basis of the triple helix is provided by a repeated unique amino acid sequence (Gly-x-y) and the polypeptides generated are capable of assembly into fibrillar or other types of supramolecular assemblies which are deposited in the extracellular matrix. The number of distinct collagen types presently recognized is more than fourteen.

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