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AB7533

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.

View Alternative Names

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='/en-us/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

Purity

>95%

Expression system

Native

Tags

Tag free

Applications

WB, SDS-PAGE

applications

Biologically active

No

Accession

P02452

Animal free

No

Carrier free

No

Species

Human

Storage buffer

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>" } } }

Product details

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).

Sequence info

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

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

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.

Specifications

Form

Liquid

Additional notes

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.

General info

Function

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

Sequence similarities

Belongs to the fibrillar collagen family.

Post-translational modifications

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.

Product protocols

Target data

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

Publications (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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