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Merck
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ABT257

Sigma-Aldrich

Anti-Pro-Collagen Type I, A1/COL1A1

from rabbit, purified by affinity chromatography

Szinonimák:

Pro-collagen alpha-1(I) chain, Pro-Alpha-1 type I collagen

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

UNSPSC kód:
12352203
eCl@ss:
32160702
NACRES:
NA.41
klón:
polyclonal
application:
FACS
IHC
WB
faj reaktivitás:
mouse, human
technika/technikák:
flow cytometry: suitable
immunohistochemistry: suitable
western blot: suitable
citations:
11

biológiai forrás

rabbit

Minőségi szint

antitest forma

affinity isolated antibody

antitest terméktípus

primary antibodies

klón

polyclonal

tisztítva

affinity chromatography

faj reaktivitás

mouse, human

technika/technikák

flow cytometry: suitable
immunohistochemistry: suitable
western blot: suitable

NCBI elérési szám

UniProt elérési szám

kiszállítva

wet ice

célzott transzláció utáni módosítás

unmodified

Géninformáció

human ... COL1A1(1277)

Általános leírás

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 form 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 an 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.

Egyediség

Cat. No. ABT257 Anti-Pro-Collagen Type I, A1/COL1A1 was raised against a sequence derived from the C-terminal propeptide (not the N-terminal propeptide) region. This polyclonal antibody will detect prepro- and pro-, but not mature collagen alpha-1(I) chain.
Predicted to react with a broad range of species based on high sequence homology, including mammalian, avian, fish, and amphibian species.

Immunogén

Epitope: C-terminal propeptide region
Linear peptide corresponding to sequence derived from human Pro-Collagen Type I, A1/COL1A1 C-terminal propeptide region.

Alkalmazás

Anti-Pro-Collagen Type I Antibody is an antibody against Pro-Collagen Type I for use in Western Blotting, Flow Cytometry, Immunohistochemistry.
Research Category
Cell Structure
Research Sub Category
Adhesion (CAMs)
Western Blotting Analysis: A representative lot detected Pro-Collagen Type I, A1/COL1A1 in mouse lung and skin tissue lysate.
Flow Cytometry Analysis: A representative lot detected Pro-Collagen Type I, A1/COL1A1 in mouse lung tissue.
Immunohistochemistry Analysis: A representative lot detected Pro-Collagen Type I, A1/COL1A1 in mouse lung tissue.

Minőség

Evaluated by Western Blotting in mouse skin tissue lysate.

Western Blotting Analysis: A 1:500 dilution of this antibody detected Pro-Collagen Type I, A1/COL1A1 in 10 µg of mouse skin tissue lysate.

Cél megnevezése

~140 kDa observed

Fizikai forma

Affinity purified
Purified rabbit polyclonal in buffer containing PBS with 0.05% sodium azide.

Tárolás és stabilitás

Stable for 1 year at 2-8°C from date of receipt.

Egyéb megjegyzések

Concentration: Please refer to lot specific datasheet.

Jogi nyilatkozat

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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Tárolási osztály kódja

12 - Non Combustible Liquids

WGK

WGK 2


Analitikai tanúsítványok (COA)

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Dokumentumtár megtekintése

Az ügyfelek ezeket is megtekintették

Timothy Catchpole et al.
PloS one, 15(2), e0229504-e0229504 (2020-02-28)
A subset of neovascular age-related macular degeneration (nvAMD) subjects appears to be refractory to the effects of anti-VEGF treatment and require frequent intravitreal injections. The vascular phenotype of the choroidal neovascular (CNV) lesions may contribute to the resistance. Animal studies
Yu-Chun Chang et al.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 35(10), e21849-e21849 (2021-09-03)
Macrophages are a critical driver of neovessel formation in tissue-engineered vascular grafts (TEVGs), but also contribute to graft stenosis, a leading clinical trial complication. Macrophage depletion via liposomal delivery of clodronate, a first-generation bisphosphonate, mitigates stenosis, but simultaneously leads to
W Grant Stevens et al.
Aesthetic surgery journal, 42(1), 56-67 (2021-05-18)
In addition to body contouring, there is anecdotal and clinical evidence of reduced laxity caused by skin tightening after cryolipolysis. However, it has not been established how cryolipolysis triggers dermal changes. The aim of this study was to investigate the
James W Reinhardt et al.
Regenerative medicine, 14(5), 389-408 (2019-06-11)
Aim: To characterize early events in neotissue formation during the first 2 weeks after vascular scaffold implantation. Materials & methods: Biodegradable polymeric scaffolds were implanted as abdominal inferior vena cava interposition grafts in wild-type mice. Results: All scaffolds explanted at
Maria Giovanna Parisi et al.
International journal of molecular sciences, 22(11) (2021-06-03)
Given the anatomical simplicity and the extraordinary ability to regenerate missing parts of the body, Cnidaria represent an excellent model for the study of the mechanisms regulating regenerative processes. They possess the mesoglea, an amorphous and practically acellular extracellular matrix

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