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AB7533

Native Human Collagen I protein

Native Human Collagen I protein

5

(2 Reviews)

|

(5 Publications)

Native Human Collagen I protein is a Human Full Length protein, expressed in Native, with >95%, suitable for WB, SDS-PAGE.

別名を表示する

Collagen alpha-1(I) chain, Alpha-1 type I collagen, COL1A1

1 Images
Western blot - Native Human Collagen I protein (AB7533)
  • WB

Supplier Data

Western blot - Native Human Collagen I protein (AB7533)

DyLight 649 anti-rabbit secondary antibody at 1 : 20,000 for 30 min at RT.

Blocking Buffer for 30 min at room temperature - proprietary protein formulation in TRIS buffered saline at pH 7.6 with thimerosal added as an antimicrobial agent.

Other Band(s) : Collagen Type I splice variants and isoforms.

All lanes:

Western blot - Anti-Collagen I + Collagen III antibody (<a href='/products/primary-antibodies/collagen-i-collagen-iii-antibody-ab34710'>ab34710</a>) at 1/1000 dilution

All lanes:

Western blot - Native Human Collagen I protein (ab7533) at 0.05 µg

Secondary

All lanes:

DyLight™ 649 anti-rabbit secondary antibody at 1/20000 dilution

Predicted band size: 139 kDa

false

Key facts

精製度

>95%

発現系

Native

タグ

Tag free

アプリケーション

WB, SDS-PAGE

applications

生物活性

No

アクセッション番号

P02452

アニマルフリー

No

キャリアフリー

No

Human

バッファー組成

Preservative: 0.01% Sodium azide Constituents: 3% Acetic acid

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"1/1000", "notes":"<p>This product is not recommended for use under denaturing conditions in WB, IP, and ELISA. We would suggest testing it under native conditions.</p>" }, "SDS-PAGE": { "reactivity":"NO_EXPERIMENTAL_DATA_EXPECTED_TO_REACT", "dilution-info":"", "notes":"<p></p>" } } }

製品の詳細

This product is free from other collagens, human serum proteins and non-collagen extracellular matrix proteins. This product reacts with anti-Collagen Type I. Reaction with anti-Collagen II, III, IV, V or VI is negligible (typically less than 1% cross reactivity was detected by ELISA).

配列情報

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":"139 kDa","actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Native","expressionSystem":null,"accessionNumber":"P02452","tags":[]}]

出荷温度及び保存条件

出荷温度
Blue Ice
短期保存期間
1-2 weeks
短期保存温度
+4°C
長期保存温度
-20°C
分注に関する情報
Upon delivery aliquot
保管に関する情報
Avoid freeze / thaw cycle
False

補足情報

This supplementary information is collated from multiple sources and compiled automatically.

Collagen type I also called collagen I is a structural protein expressed mainly in connective tissues such as skin tendon bone and ligaments. It serves as an important component in providing mechanical strength and integrity to these tissues. Collagen I is a fibrillar collagen known for its triple-helix structure composed of two alpha-1 chains and one alpha-2 chain and has a molecular mass of approximately 300 kDa. Researchers often employ collagen western blot and collagen ELISA techniques for its detection. Collagen suppliers offer various collagen antibodies used in these assays to study its distribution and function.
Biological function summary

Collagen type I plays a central role in maintaining the extracellular matrix and supporting cellular environments. It interacts with other matrix proteins and cells forming complexes that help in tissue development and repair. Type I collagen is especially important in bone matrix working alongside minerals like hydroxyapatite to provide rigidity and support. Anti-collagen antibodies aid in studying its biological functions and interactions which are critical to understanding tissue dynamics.

Pathways

Collagen type I interacts with multiple signaling cascades involved in tissue remodeling and repair. It is a significant player in the TGF-β pathway which regulates fibrosis and wound healing processes. In these pathways proteins such as fibronectin and integrins work in concert with collagen type I to orchestrate cellular responses to damage. Researchers often examine its role in these pathways to uncover therapeutic possibilities for disease interventions.

Collagen type I has strong connections to conditions like osteogenesis imperfecta and fibrosis. Mutations or irregularities in collagen I production can lead to osteogenesis imperfecta a genetic disorder characterized by brittle bones. In fibrosis excessive collagen deposition disrupts normal tissue architecture contributing to organ dysfunction. In both conditions type I collagen interacts with other proteins like matrix metalloproteinases which modulate its breakdown and remodeling highlighting its importance in disease pathology.

製品の性状

製品の状態

Liquid

補足情報

Human Collagen type I has been prepared from human placenta and is chromatographically and immunologically pure. This product is free from other collagens, human serum proteins and non-collagen extracellular matrix proteins.

一般的な情報

機能

Type I collagen is a member of group I collagen (fibrillar forming collagen).

配列の類似性

Belongs to the fibrillar collagen family.

翻訳後修飾

Contains mostly 4-hydroxyproline. Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.. Contains 3-hydroxyproline at a few sites. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline.. Lysine residues at the third position of the tripeptide repeating unit (G-X-Y) are 5-hydroxylated in some or all of the chains.. O-glycosylated on hydroxylated lysine residues. The O-linked glycan consists of a Glc-Gal disaccharide.

製品プロトコール

ターゲットの情報

Type I collagen is a member of group I collagen (fibrillar forming collagen).
See full target information COL1A1

文献 (5)

Recent publications for all applications. Explore the full list and refine your search

Acta biomaterialia 99:269-283 PubMed31525537

2019

Donor age significantly influences the Raman spectroscopic biomolecular fingerprint of human pancreatic extracellular matrix proteins following collagenase-based digestion.

Applications

Unspecified application

Species

Unspecified reactive species

Rebecca M Spiers,Julia Marzi,Eva M Brauchle,Sarah E Cross,Rebecca H Vaughan,Paul A Bateman,Stephen J Hughes,Katja Schenke-Layland,Paul R V Johnson

Neuron 99:702-719.e6 PubMed30078576

2018

Extracellular Matrix Components HAPLN1, Lumican, and Collagen I Cause Hyaluronic Acid-Dependent Folding of the Developing Human Neocortex.

Applications

Unspecified application

Species

Unspecified reactive species

Katherine R Long,Ben Newland,Marta Florio,Nereo Kalebic,Barbara Langen,Anna Kolterer,Pauline Wimberger,Wieland B Huttner

Cancer biology & therapy 19:904-912 PubMed30067436

2018

A fragment of SPARC reflecting increased collagen affinity shows pathological relevance in lung cancer - implications of a new collagen chaperone function of SPARC.

Applications

Unspecified application

Species

Unspecified reactive species

S N Kehlet,T Manon-Jensen,S Sun,S Brix,D J Leeming,M A Karsdal,N Willumsen

American journal of physiology. Heart and circulat 309:H1883-93 PubMed26453333

2015

Calpastatin overexpression impairs postinfarct scar healing in mice by compromising reparative immune cell recruitment and activation.

Applications

Unspecified application

Species

Unspecified reactive species

Feng Wan,Emmanuel Letavernier,Claude Jourdan Le Saux,Amal Houssaini,Shariq Abid,Gabor Czibik,Daigo Sawaki,Elisabeth Marcos,Jean-Luc Dubois-Rande,Laurent Baud,Serge Adnot,Geneviève Derumeaux,Barnabas Gellen

The British journal of dermatology 164:83-96 PubMed20849516

2010

Fibroblasts from the growing margin of keloid scars produce higher levels of collagen I and III compared with intralesional and extralesional sites: clinical implications for lesional site-directed therapy.

Applications

Unspecified application

Species

Unspecified reactive species

F Syed,E Ahmadi,S A Iqbal,S Singh,D A McGrouther,A Bayat
View all publications

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