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MAB1913-C

Sigma-Aldrich

Anti-Procollagen Type I Antibody, CT, clone PCIDG10 (Ascites Free)

clone PCIDG10, from mouse

Sinônimo(s):

Collagen alpha-1(I) chain, Procollagen Type I, CT, Alpha-1 type I collagen

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About This Item

Código UNSPSC:
12352203
eCl@ss:
32160702
NACRES:
NA.43

fonte biológica

mouse

Nível de qualidade

forma do anticorpo

purified immunoglobulin

tipo de produto de anticorpo

primary antibodies

clone

PCIDG10, monoclonal

reatividade de espécies

mouse, human, rat, guinea pig

reatividade da espécie (prevista por homologia)

bovine (based on 100% sequence homology)

técnica(s)

ELISA: suitable
flow cytometry: suitable
immunocytochemistry: suitable
immunohistochemistry: suitable (paraffin)

Isotipo

IgG1κ

nº de adesão NCBI

nº de adesão UniProt

Condições de expedição

dry ice

modificação pós-traducional do alvo

unmodified

Informações sobre genes

human ... COL1A1(1277)

Descrição geral

Collagen alpha-1(I) chain (UniProt P02452; also known as Alpha-1 type I collagen) is encoded by the COL1A1 gene (Gene ID 1277) in human. Collagen is the major component of the extracellular matrix (ECM) and forms the fibrils of tendons, ligaments, and bones. Type I collagen consists of two alpha I chains and one alpha 2 chain. Alpha-1 type I collagen is initially produced as a 1464-amino acid prepro-form with a signal peptide sequence (a.a. 1-22) and two propeptide sequences (a.a. 23-161 and a.a. 1219 –1464), the removal of which yields the mature alpha-1(I) chain. The mature alpha-1(I) chain is composed mostly of a large triple-helical region (a.a. 179-1192) sandwiched between two nonhelical segments known as the N-terminal telopeptide (a.a. 162-178; numbering based on the prepro-form) and the C-terminal telopeptide (a.a. 1193-1218; numbering based on the prepro-form). Collagen can be extracted from tissue via either enzymatic or non-enzymatic means. Collagen extracted using the proteolytic enzyme pepsin corresponds to the large triple-helical region, referred to as atelocollagen because both the N- and C-terminal telopeptides have been cleaved off by pepsin. On the other hand, collagen preparations obtained with non-enzymatic means (e.g. by acid extraction) have the intact telopeptides at both ends.

Especificidade

Labels carboxy-terminal pro-peptide of collagen type I. Does not stain mature collagen fibers in tissue, but rather is localized intracellularly in cells producing pro-collagen I.

Imunogênio

Epitope: C-terminal propeptide region
Human pro-collagen I.

Aplicação

Immunohistochemistry Analysis: A 1:50 dilution from a representative lot detected Procollagen Type I in mouse skin, rat skin, and rat skeletal muscle tissue.
Immunocytochemistry Analysis: A representative lot detected type I procollagen immunoreactivity in human semitendinosus and gracilis tendon fibroblasts from patients undergoing reconstruction surgery after anterior cruciate ligament (ACL) rupture by fluorescent immunocytochemistry (Bayer, M.L., et al. (2012). Mech Ageing Dev. 133(5):246-254).
Flow Cytometry Analysis: A representative lot detected PICP+/CD45+ fibrocytes in lung cells from bleomycin-treated mice (Yeager, M.E., et al. (2012). Eur Respir J. 39(1):104-111).
Flow Cytometry Analysis: A representative lot detected higher numbers and percentages of circulating PICP+/CD45+ fibrocytes in peripheral blood samples from children/yound adults with pulmonary hypertension (PH) than in samples from healthy individuals (Reese, C., et al. (2014). Front Pharmacol. 5:141).
Immunohistochemistry Analysis: A representative lot detected cytoplasmic type I procollagen immunoreactivity in stromal cells from the lysed functionalis of frozen human menstrual endometria sections (Gaide Chevronnay, H.P., et al. (2009). Endocrinology. 150(11):5094-5105).
ELISA Analysis: A representative lot detected different age-dependency of procollagen type I C-terminal propeptide (PICP) immunoreactivity in the cruciate ligaments of osteoarthritis-/OA-prone Dunkin-Hartley (DH) guinea pigs and in age-matched Bristol strain 2 (BS2) control guinea pigs (Quasnichka, H.L., et al. (2005). Arthritis Rheum. 52(10):3100-3109).
Research Category
Cell Structure
Research Sub Category
Adhesion (CAMs)
This Anti-Procollagen Type I Antibody, CT, clone PCIDG10 (Ascites Free) is validated for use in Immunohistochemistry (Paraffin), Immunocytochemistry, Flow Cytometry and ELISA for the detection of Procollagen Type I.

Qualidade

Evaluated by Immunohistochemistry in human bone tissue.

Immunohistochemistry Analysis: A 1:50 dilution of this antibody detected Procollagen Type I in human bone tissue.

Descrição-alvo

140 kDa calculated

forma física

Format: Purified
Protein G Purified
Purified mouse monoclonal IgG1κ antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl without preservatives.

Armazenamento e estabilidade

Stable for 1 year at -20°C from date of receipt.
Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.

Outras notas

Concentration: Please refer to lot specific datasheet.

Exoneração de responsabilidade

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Código de classe de armazenamento

12 - Non Combustible Liquids

Classe de risco de água (WGK)

WGK 1

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


Certificados de análise (COA)

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Héloïse P Gaide Chevronnay et al.
Endocrinology, 150(11), 5094-5105 (2009-10-13)
Coupling of focal degradation and renewal of the functional layer of menstrual endometrium is a key event of the female reproductive biology. The precise mechanisms by which the various endometrial cell populations control extracellular matrix (ECM) degradation in the functionalis
Helen L Quasnichka et al.
Arthritis and rheumatism, 52(10), 3100-3109 (2005-10-04)
The influence of the cruciate ligaments in spontaneous osteoarthritis (OA) is not understood, although ligament rupture is known to cause secondary OA. Additionally, femoral notch narrowing at the anterior cruciate ligament (ACL) insertion site is associated with disease severity, but
Monika L Bayer et al.
Mechanisms of ageing and development, 133(5), 246-254 (2012-03-08)
The aging process of tendon tissue is associated with decreased collagen content and increased risk for injuries. An essential factor in tendon physiology is transforming growth factor-β1 (TGF-β1), which is presumed to be reduced systemically with advanced age. The aim
J A McDonald et al.
The Journal of clinical investigation, 78(5), 1237-1244 (1986-11-01)
Excessive collagen deposition plays a critical role in the development of fibrosis, and early or active fibrosis may be more susceptible to therapeutic intervention than later stages of scarring. However, at present there is no simple method for assessing the
M E Yeager et al.
The European respiratory journal, 39(1), 104-111 (2011-06-28)
Chronic inflammation is an important component of the fibroproliferative changes that characterise pulmonary hypertensive vasculopathy. Fibrocytes contribute to tissue remodelling in settings of chronic inflammation, including animal models of pulmonary hypertension (PH). We sought to determine whether circulating fibrocytes were

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