antibody

Goat Anti-Type I Collagen-FITC

MBS670615

0.2 mg

465 USD

polyclonal

goat

FITC

ELISA, enzyme immunoassay

Antibody

Goat Anti-Type I Collagen-FITC

[Type I Collagen]

[type I collagen, partial; Collagen alpha-2(I) chain; collagen alpha-2(I) chain; collagen type I alpha 2; Alpha-2 type I collagen]

[COL1A2; COL1A2; OI4]

CO1A2_HUMAN

polyclonal

IgG

goat

397

Reacts with conformational determinants on type I collagen

Affinity chromatography on type I collagen covalently linked to agarose

0.4 mg/mL

Store at 2-8 degree C

ELISA (EIA), FLISA

FLISA:. FITC and AF488 conjugates 1:200-1:400. Other Applications: Since applications vary, you should determine the optimum working dilution for product that is appropriate for your specific need.

Testing Data

Source: Pooled antisera from goats hyperimmunized with type I collagen. Cross Adsorption: Collagen types II, III, IV, V, and VI. Buffer Formulation: Supplied in PBS/NaN3

Isotype Control: Goat IgG-FITC

1. Rasmussen LM, Hansen PR, Ledet T. Homocysteine and the production of collagens, proliferation and apoptosis in human arterial smooth muscle cells. APMIS. 2004;112:598-604. (ELISA, Human Reactivity). 2. Kottler UB, Jünemann AG, Aigner T, Zenkel M, Rummelt C, Schlötzer-Schrehardt U. Comparative effects of TGF-beta1 and TGF-beta2 on extracellular matrix production, proliferation, migration, and collagen contraction of human Tenons capsule fibroblasts in pseudoexfoliation and primary open-angle glaucoma. Exp Eye Res. 2005;80:121-34. (ELISA, Human Reactivity). 3. Dooley A, Shi-Wen X, Aden N, Tranah T, Desai N, Denton CP, et al. Modulation of collagen type I, fibronectin and dermal fibroblast function and activity, in systemic sclerosis by the antioxidant epigallocatechin-3-gallate. Rheumatology. 2010;49:2024-36. (ELISA, WB, Human Reactivity). 4. Zhang WW, Ma KC, Andersen O, Sourander P, Tollesson PO, Olsson Y. The microvascular changes in cases of hereditary multi-infarct disease of the brain. Acta Neuropathol. 1994;87:317-24. (IHC-PS, Human Reactivity). 5. Van Deijnen JH, Van Suylichem PT, Wolters GH, Van Schilfgaarde R. Distribution of collagens type I, type III and type V in the pancreas of rat, dog, pig and man. Cell Tissue Res. 1994;277:115-21. (IHC-PS, Canine, Human, Porcine, & Rat Reactivity). 6. Moses MA, Wiederschain D, Wu I, Fernandez CA, Ghazizadeh V, Lane WS, et al. Troponin I is present in human cartilage and inhibits angiogenesis. Proc Natl Acad Sci USA. 1999;96:2645-50. (IHC-PS, Bovine Reactivity). 7. Dorotka R, Bindreiter U, Macfelda K, Windberger U, Nehrer S. Marrow stimulation and chondrocyte transplantation using a collagen matrix for cartilage repair. Osteoarthritis Cartilage. 2005;13:655-64. (IHC-PS, Sheep Reactivity). 8. Weissengruber GE, Egerbacher M, Forstenpointner G. Structure and innervation of the tusk pulp in the African elephant (Loxodonta africana). J Anat. 2005;206:387-93. (IHC-PS, Elephant Reactivity). 9. Walter I, Schönkypl S. Extracellular matrix components and matrix degrading enzymes in the feline placenta during gestation. Placenta. 2006;27:291-306. (IHC-PS, Feline Reactivity). 10. Alcazar O, Cousins SW, Striker GE, Marin-Castano ME. (Pro)renin receptor is expressed in human retinal pigment epithelium and participates in extracellular matrix remodeling. Exp Eye Res. 2009;89:638-47. (IHC-PS, WB, Human Reactivity). 11. Chen W, Yu M, Li Y, Chen W, Xia Y. Beneficial effects of astragalus polysaccharides treatment on cardiac chymase activities and cardiomyopathy in diabetic hamsters. Acta Diabetol. 2010;47 Suppl 1:S35-46. (IHC-PS, Hamster Reactivity). 12. Kyller M, Witter K, Tichy F. Gingival stippling in dogs: clinical and structural characteristics. Res Vet Sci. 2010;88:195-202. (IHC-PS, Canine Reactivity). 13. Zhang Y, Edgley AJ, Cox AJ, Powell AK, Wang B, Kompa AR, et al. FT011, a new anti-fibrotic drug, attenuates fibrosis and chronic heart failure in experimental diabetic cardiomyopathy. Eur J Heart Fail. 2012;14:549-62. (IHC-PS, WB, Rat Reactivity). 14. Jiang L, Zhou Y, Xiong M, Fang L, Wen P, Cao H, et al. Sp1 mediates microRNA-29c-regulated type I collagen production in renal tubular epithelial cells. Exp Cell Res. 2013;319:2254-65. (IHC-PS, ICC, WB, Rat Reactivity). 15. Sun S, Zhao T, Zhang H, Huang X, Zhang W, Zhang L, et al. Renoprotective effect of berberine on type 2 diabetic nephropathy in rats. Clin Exp Pharmacol Physiol. 2015;42:662-70. (IHC-PS, WB, Rat Reactivity). 16. Jerdan JA, Michels RG, Glaser BM. Extracellular matrix of newly forming vessels—an immunohistochemical study. Microvasc Res. 1991;42:255-65. (IHC-FS, Guinea Pig & Rabbit Reactivity). 17. Miyaishi O, Sakata K, Matsuyama M, Saga S. Distribution of the collagen binding heat-shock protein in chicken tissues. J Histochem Cytochem. 1992;40:1021-9. (IHC-FS, Chicken Reactivity). 18. Dixon IM, Ju H, Reid NL, Scammell-La Fleur T, Werner JP, Jasmin G. Cardiac collagen remodeling in the cardiomyopathic Syrian hamster and the effect of losartan. J Mol Cell Cardiol. 1997;29:1837-50. (IHC-FS, Hamster Reactivity). 19. Harada T, Juhn SK, Kim Y, Sakakura Y. Immunohistochemical localization of collagen types I, III, and IV, laminin, fibronectin, and keratin in the endolymphatic sac. Ann Otol Rhinol Laryngol. 2000;109:180-6. (IHC-FS, Chinchilla Reactivity). 20. Fraser SA, Crawford A, Frazer A, Dickinson S, Hollander AP, Brook IM, et al. Localization of type VI collagen in tissue-engineered cartilage on polymer scaffolds. Tissue Eng. 2006;12:569-77. (IHC-FS, Bovine & Human Reactivity). 21. Chun SY, Lim GJ, Kwon TG, Kwak EK, Kim BW, Atala A, et al. Identification and characterization of bioactive factors in bladder submucosa matrix. Biomaterials. 2007;28:4251-6. (IHC-FS, Porcine Reactivity). 22. Albon J, Farrant S, Akhtar S, Young R, Boulton ME, Smith G, et al. Connective tissue structure of the tree shrew optic nerve and associated ageing changes. Invest Ophthalmol Vis Sci. 2007;48:2134-44. (IHC-FS, Tree Shrew Reactivity). 23. Behmoaras J, Diaz AG, Venda L, Ko J, Srivastava P, Montoya A, et al. Macrophage epoxygenase determines a profibrotic transcriptome signature. J Immunol. 2015;194:4705-16. (IHC-FS, Rat Reactivity). 24. Kothapalli D, Liu S, Bae YH, Monslow J, Xu T, Hawthrone EA, et al. Cardiovascular protection by ApoE and ApoE-HDL linked to suppression of ECM gene expression and arterial stiffening. Cell Rep. 2012;2:1259-71. (IHC-FS, ICC, Mouse Reactivity). 25. Lundquist P, Ritchie HH, Moore K, Lundgren T, Linde A. Phosphate and calcium uptake by rat odontoblast-like MRPC-1 cells concomitant with mineralization. J Bone Miner Res. 2002;17:1801-13. (ICC, Rat Reactivity). 26. via c-Abl and Egr-1: selective modulation by imatinib mesylate. Oncogene. 2009;28:1285-97. (ICC, WB, Human Reactivity)?Bhattacharyya S, Ishida W, Wu M, Wilkes M, Mori Y, Hinchcliff M, et al. A non-Smad mechanism of fibroblast activation by transforming growth factor-. 27. Wang J, Chu ES, Chen H, Man K, Go MY, Huang XR, et al. microRNA-29b prevents liver fibrosis by attenuating hepatic stellate cell activation and inducing apoptosis through targeting PI3K/AKT pathway. Oncotarget. 2015;6:7325-38. (ICC, WB, Human, Mouse, & Rat Reactivity). 28. Marangoni RG, Korman BD, Wei J, Wood TA, Graham LV, Whitfield ML, et al. Myofibroblasts in murine cutaneous fibrosis originate from adiponectin-positive intradermal progenitors. Arthritis Rheumatol. 2015;67:1062-73. (ICC, WB, Mouse Reactivity). 29. Dingemans KP, Teeling P, Lagendikj JH, Becker AE. Extracellular matrix of the human aortic media: an ultrastructural histochemical and immunohistochemical study of the adult aortic media. Anat Rec. 2000;258:1-14. (EM, Human Reactivity). 30. Sharawy M, Ali AM, Choi W. Experimental induction of anterior disk displacement of the rabbit craniomandibular joint: an immuno-electron microscopic study of collagen and proteoglycan occurrence in the condylar cartilage. J Oral Pathol Med. 2003;32:176-84. (EM, Rabbit Reactivity). 31. Rodrigues MT, Lee SJ, Gomes ME, Reis RL, Atala A, Yoo JJ. Amniotic fluid-derived stem cells as a cell source for bone tissue engineering. Tissue Eng Part A. 2012;18:2518-27. (EM, Human Reactivity). 32. Xu S, Vancheeswaran R, Bou-Gharios G, O'Hare MJ, Olsen I, Abraham D, et al. Scleroderma-derived human fibroblasts retain abnormal phenotypic and functional characteristics following retroviral transduction with the SV40 tsT antigen. Exp Cell Res. 1995;220:407-14. (FC, Human Reactivity). 33. Mendoza FA, Piera-Velazquez S, Farber JL, Feghali-Bostwick C, Jiménez SA. Endothelial cells expressing endothelial and mesenchymal cell gene products in lung tissue from patients with systemic sclerosis-associated interstitial lung disease. Arthritis Rheumatol. 2016;68:210-7. (WB, Human Reactivity). 34. Sato M, Shegogue D, Hatamochi A, Yamazaki S, Trojanowska M. Lysophosphatidic acid inhibits TGF-beta-mediated stimulation of type I collagen mRNA stability via an ERK-dependent pathway in dermal fibroblasts. Matrix Biol. 2004;23:353-61. (IP, Human Reactivity). 35. Reynaert H, Rombouts K, Jia Y, Urbain D, Chatterjee N, Uyama N, et al. Somatostatin at nanomolar concentration reduces collagen I and III synthesis by, but not proliferation of activated rat hepatic stellate cells. Br J Pharmacol. 2005;146:77-88. (IP, Rat Reactivity)

30102

CAA39142.1

P08123

129,314 Da

AGE-RAGE Signaling Pathway In Diabetic Complications (1319988); AGE-RAGE Signaling Pathway In Diabetic Complications (1319775); Amoebiasis Pathway (167324); Amoebiasis Pathway (167191); Assembly Of Collagen Fibrils And Other Multimeric Structures Pathway (1270247); Binding And Uptake Of Ligands By Scavenger Receptors Pathway (1269897); C-MYB Transcription Factor Network Pathway (138073); Collagen Biosynthesis And Modifying Enzymes Pathway (1270246); Collagen Formation Pathway (1270245); ECM-receptor Interaction Pathway (83068)

This gene encodes the pro-alpha2 chain of type I collagen whose triple helix comprises two alpha1 chains and one alpha2 chain. Type I is a fibril-forming collagen found in most connective tissues and is abundant in bone, cornea, dermis and tendon. Mutations in this gene are associated with osteogenesis imperfecta types I-IV, Ehlers-Danlos syndrome type VIIB, recessive Ehlers-Danlos syndrome Classical type, idiopathic osteoporosis, and atypical Marfan syndrome. Symptoms associated with mutations in this gene, however, tend to be less severe than mutations in the gene for the alpha1 chain of type I collagen (COL1A1) reflecting the different role of alpha2 chains in matrix integrity. Three transcripts, resulting from the use of alternate polyadenylation signals, have been identified for this gene. [provided by R. Dalgleish, Feb 2008]

COL1A2: Type I collagen is a member of group I collagen (fibrillar forming collagen). Defects in COL1A2 are the cause of Ehlers-Danlos syndrome type 7B (EDS7B). EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS7B is marked by bilateral congenital hip dislocation, hyperlaxity of the joints, and recurrent partial dislocations. Defects in COL1A2 are a cause of osteogenesis imperfecta type 1 (OI1). A dominantly inherited connective tissue disorder characterized by bone fragility and blue sclerae. Osteogenesis imperfecta type 1 is non-deforming with normal height or mild short stature, and no dentinogenesis imperfecta. Defects in COL1A2 are a cause of osteogenesis imperfecta type 2 (OI2); also known as osteogenesis imperfecta congenita (OIC) or lethal perinatal. A connective tissue disorder characterized by bone fragility, with many perinatal fractures, severe bowing of long bones, undermineralization, and death in the perinatal period due to respiratory insufficiency. Defects in COL1A2 are the cause of Ehlers-Danlos syndrome autosomal recessive cardiac valvular form (EDSCV). A connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. In addition to joint laxity, skin hyperextensibility and friability, and abnormal scar formation, patients have mitral valve prolapse and insufficiency, mitral regurgitation, and aortic insufficiency. Defects in COL1A2 are a cause of osteogenesis imperfecta type 3 (OI3). A connective tissue disorder characterized by progressively deforming bones, very short stature, a triangular face, severe scoliosis, grayish sclera, and dentinogenesis imperfecta. Defects in COL1A2 are a cause of osteogenesis imperfecta type 4 (OI4); also known as osteogenesis imperfecta with normal sclerae. A connective tissue disorder characterized by moderately short stature, mild to moderate scoliosis, grayish or white sclera and dentinogenesis imperfecta. A chromosomal aberration involving COL1A2 may be a cause of lipoblastomas, which are benign tumors resulting from transformation of adipocytes, usually diagnosed in children. Translocation t(7;8)(p22;q13) with PLAG1. Belongs to the fibrillar collagen family. Protein type: Secreted; Secreted, signal peptide. Chromosomal Location of Human Ortholog: 7q22.1. Cellular Component: collagen type I; endoplasmic reticulum lumen; extracellular matrix; extracellular region; extracellular space. Molecular Function: extracellular matrix structural constituent; identical protein binding; metal ion binding; platelet-derived growth factor binding; protein binding; protein binding, bridging; SMAD binding. Biological Process: blood coagulation; blood vessel development; collagen catabolic process; collagen fibril organization; extracellular matrix organization and biogenesis; leukocyte migration; odontogenesis; platelet activation; regulation of blood pressure; regulation of immune response; Rho protein signal transduction; skeletal development; skin morphogenesis; transforming growth factor beta receptor signaling pathway. Disease: Ehlers-danlos Syndrome, Autosomal Recessive, Cardiac Valvular Form; Ehlers-danlos Syndrome, Type Vii, Autosomal Dominant; Osteogenesis Imperfecta, Type Ii; Osteogenesis Imperfecta, Type Iii; Osteogenesis Imperfecta, Type Iv; Osteoporosis

0.2 mg

465 USD