Collagen I alpha 1 Antibody [HRP]

Novus Biologicals, part of Bio-Techne | Catalog # NBP1-77457H

Novus Biologicals, part of Bio-Techne

Key Product Details

Species Reactivity

Validated:

Human, Mouse

Predicted:

Bovine (98%), Canine (98%), Primate (100%), Rat (90%), Sheep (98%). Backed by our 100% Guarantee.

Applications

Immunocytochemistry/ Immunofluorescence, Immunohistochemistry, Immunohistochemistry-Paraffin, Western Blot (Negative)

Label

HRP

Antibody Source

Polyclonal Rabbit IgG

Concentration

Please see the vial label for concentration. If unlisted please contact technical services.

View all Collagen I alpha 1 Antibodies »

Product Specifications

Immunogen

This Collagen I alpha 1 antibody was raised against a synthetic peptide made to an internal portion of the human Collagen I protein (between residues 150-200) [UniProt# P02452]

Localization

Secreted to extracellular space and extracellular matrix.

Clonality

Polyclonal

Host

Rabbit

Isotype

IgG

Applications for Collagen I alpha 1 Antibody [HRP]

Application
Recommended Usage

Immunocytochemistry/ Immunofluorescence

Optimal dilutions of this antibody should be experimentally determined.

Immunohistochemistry

Optimal dilutions of this antibody should be experimentally determined.

Immunohistochemistry-Paraffin

Optimal dilutions of this antibody should be experimentally determined.

Western Blot (Negative)

Optimal dilutions of this antibody should be experimentally determined.
Application Notes
Optimal dilution of this antibody should be experimentally determined.

Formulation, Preparation, and Storage

Purification

Immunogen affinity purified

Formulation

PBS

Preservative

No Preservative

Concentration

Please see the vial label for concentration. If unlisted please contact technical services.

Shipping

The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.

Stability & Storage

Store at 4C in the dark.

Background: Collagen I alpha 1

Collagen is an extracellular matrix protein that serves as a scaffold defining the shape and mechanical properties of many tissues and organs including skin, tendon, artery walls, fibrocartilage, bone and teeth. Collagens are highly conserved and are characterized by an uninterrupted "Glycine X Y" triplet repeat that is a necessary part of the triple helical structure. The extensive family of collagens is composed of several chain types, including fibril-forming interstitial collagens (types I, II, III and V) and basement membrane collagens (type IV), each type containing multiple isoforms. Collagen type I (also known as collagen alpha, COL1A1, and alpha-1 type I collagen) is the largest component of fibrillar collagen found in cartilage and connective tissues. It is synthesized by fibroblasts, osteoblasts, and odontoblasts and has a theoretical molecular weight of 138 kDa.

Type I collagen is a fibril-forming collagen found in most connective tissues and is abundant in bone, cornea, dermis and tendon tissue. Collagens are fibrous, extracellular matrix proteins with high tensile strength and are the major components of connective tissue. Several collagens play a role in cell adhesion, responsible for maintaining normal tissue architecture and function. All collagens contain a triple helix domain and frequently show lateral self-association in order to form complex connective tissues. Post-Golgi LH3 trafficking is essential for collagen homeostasis and for the development and function of multiple organs and tissues (1).

The COL1A1 gene encodes the pro-alpha1 chains of type I collagen protein, whose triple helix is comprised of two alpha1 chains and one alpha2 chain. Mutations in the encoding COL1A1 gene are associated with brittle bone disease (Osteogenesis Imperfecta), cortical hyperostosis (Caffey disease) and disorders that affect the connective tissues (Ehlers-Danlos syndrome) (2). Studies have found that HIF-1 transcription regulation of collagen prolyl hydroxylases regulates collagen deposition, promoting cancer cell alignment along collagen fibers, which enhances invasion and metastasis to lymph nodes and lung tissue by breast cancer cells (3).

References

1. Banushi, B., Forneris, F., Straatman-Iwanowska, A., Strange, A., Lyne, A. M., Rogerson, C., . . . Gissen, P. (2016). Regulation of post-Golgi LH3 trafficking is essential for collagen homeostasis. Nat Commun, 7, 12111. doi:10.1038/ncomms12111

2. Lu, Y., Zhang, S., Wang, Y., Ren, X., & Han, J. (2019). Molecular mechanisms and clinical manifestations of rare genetic disorders associated with type I collagen. Intractable Rare Dis Res, 8(2), 98-107. doi:10.5582/irdr.2019.01064

3. Gilkes, D. M., Chaturvedi, P., Bajpai, S., Wong, C. C., Wei, H., Pitcairn, S., . . . Semenza, G. L. (2013). Collagen prolyl hydroxylases are essential for breast cancer metastasis. Cancer Res, 73(11), 3285-3296. doi:10.1158/0008-5472.Can-12-3963

Alternate Names

COL1A1, OI4

Gene Symbol

COL1A1

Additional Collagen I alpha 1 Products

Product Documents for Collagen I alpha 1 Antibody [HRP]

Product Datasheets

Certificate of Analysis

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Product Specific Notices for Collagen I alpha 1 Antibody [HRP]

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

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