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AB7536

Native Human Collagen IV protein

Native Human Collagen IV protein

3

(1 Review)

|

(13 Publications)

Native Human Collagen IV protein is a Human Full Length protein with >95% purity and suitable for western blot, ELISA, IP, Blocking assay and SDS-PAGE. The predicted molecular weight of ab7536 native protein is 161 kDa

- Save time and ensure accurate results - use our Collagen IV (COL4A1) protein as a control
- Cited in over 10 publications

查看别名

Collagen alpha-1(IV) chain, COL4A1

关键信息

纯度

>95%

表达系统

Native

标签

Tag free

应用

SDS-PAGE, WB, BL, ELISA, IP

applications

生物活性

No

访问

P02462

不含动物源

No

不含载体蛋白

No

种属

Human

存储溶液

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

storage-buffer

反应性数据

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"1/10000", "notes":"<p></p>" }, "IP": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "BL": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "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":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

产品详情

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

序列信息

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":"161 kDa","actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Native","expressionSystem":null,"accessionNumber":"P02462","tags":[]}]

性能和储存信息

运输条件
Blue Ice
推荐的短期储存条件
+4°C
推荐的长期储存条件
+4°C
分装信息
Upon delivery aliquot
储存信息
Store undiluted
False

补充信息

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

Collagen IV also known as COL4A1 or collagen type IV is a structural protein essential to the basement membrane in tissues. The molecular weight of collagen type 4 varies but it generally forms a high-molecular-weight complex. This protein expresses prominently in various tissues especially in the kidneys lens capsule of the eye and skin. Collagen IV comprises six different alpha chains where its distinctiveness lies in its non-fibrillar network-forming structure which serves as a supportive scaffold for tissues and contributes to tissue regeneration and cell adhesion.
Biological function summary

The highly organized network of collagen type IV plays a supreme role in maintaining the integrity and functionality of the basement membrane. It exists predominantly as part of a supramolecular complex associating with laminin nidogen and perlecan forming a multifunctional platform. This platform facilitates cellular signaling tissue elasticity and filtration functions. The basement membrane's selective permeability heavily relies on this network structure to regulate the exchange of molecules between tissues like blood vessels and epithelial sheets.

Pathways

Collagen IV contributes to several critical functions within the extracellular matrix organization and cell-matrix adhesion pathways. Specifically it interacts intimately with integrins and matrix metalloproteinases (MMPs) playing roles in angiogenesis and tissue repair. Additionally its interactions with other collagens and integrins within these pathways enhance cellular responses to mechanical stress and contribute to structural resilience in tissues.

Mutations or abnormalities in collagen IV are linked closely with hereditary conditions such as Alport syndrome and Goodpasture syndrome. These conditions often result in compromised structural integrity and function of the basement membrane particularly affecting the kidneys and lungs. Alterations in collagen IV can influence interactions with other proteins like collagen type IV-associated proteins altering normal physiological functions and leading to tissue dysfunction and disease manifestations.

特殊说明

形式

Liquid

附加说明

This product 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.

常规信息

功能

Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.. Arresten, comprising the C-terminal NC1 domain, inhibits angiogenesis and tumor formation. The C-terminal half is found to possess the anti-angiogenic activity. Specifically inhibits endothelial cell proliferation, migration and tube formation.

序列相似性

Belongs to the type IV collagen family.

翻译后修饰

Lysines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated. The modified lysines can be O-glycosylated.. Contains 4-hydroxyproline (Probable). Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains (By similarity).. Contains 3-hydroxyproline. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline.. Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding (PubMed:2844531). 12 of these, located in the NC1 domain, are conserved in all known type IV collagens.. The trimeric structure of the NC1 domains is stabilized by covalent bonds (sulfilimine cross-links) between Lys and Met residues (PubMed:12011424). These cross-links are important for the mechanical stability of the basement membrane (By similarity). Sulfilimine cross-link is catalyzed by PXDN (By similarity).. Proteolytic processing produces the C-terminal NC1 peptide, arresten.

产品实验方案

靶点信息

Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.. Arresten, comprising the C-terminal NC1 domain, inhibits angiogenesis and tumor formation. The C-terminal half is found to possess the anti-angiogenic activity. Specifically inhibits endothelial cell proliferation, migration and tube formation.
See full target information COL4A1

文献 (13)

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

Bioactive materials 38:399-410 PubMed38774457

2024

HtrA3 paves the way for MSC migration and promotes osteogenesis.

Applications

Unspecified application

Species

Unspecified reactive species

Yaru Guo,Siqin Ma,Dandan Wang,Feng Mei,Yusi Guo,Boon Chin Heng,Shihan Zhang,Ying Huang,Yan Wei,Ying He,Wenwen Liu,Mingming Xu,Xuehui Zhang,Lili Chen,Xuliang Deng

ACS biomaterials science & engineering 8:3819-3830 PubMed35994527

2022

Role of Extracellular Matrix Biomolecules on Endometrial Epithelial Cell Attachment and Cytokeratin 18 Expression on Gelatin Hydrogels.

Applications

Unspecified application

Species

Unspecified reactive species

Samantha G Zambuto,Ishita Jain,Kathryn B H Clancy,Gregory H Underhill,Brendan A C Harley

BMC immunology 23:29 PubMed35668375

2022

Lack of autoantibodies against collagen and related proteins in collagenous colitis.

Applications

Unspecified application

Species

Unspecified reactive species

Larsson Jk,Roth B,Ohlsson B,Sjöberg K

Cancer research 82:2031-2044 PubMed35260882

2022

Chemotherapy-Induced Collagen IV Drives Cancer Cell Motility through Activation of Src and Focal Adhesion Kinase.

Applications

Unspecified application

Species

Unspecified reactive species

Jackson P Fatherree,Justinne R Guarin,Rachel A McGinn,Stephen P Naber,Madeleine J Oudin

International journal of molecular sciences 22: PubMed34948383

2021

Screening of Self-Assembling of Collagen IV Fragments into Stable Structures Potentially Useful in Regenerative Medicine.

Applications

Unspecified application

Species

Unspecified reactive species

Marcin Kolasa,Grzegorz Galita,Ireneusz Majsterek,Ewa Kucharska,Katarzyna Czerczak,Joanna Wasko,Angelika Becht,Justyna Fraczyk,Anna Gajda,Lukasz Pietrzak,Lukasz Szymanski,Agnieszka Krakowiak,Zbigniew Draczynski,Beata Kolesinska

Diabetology & metabolic syndrome 13:72 PubMed34174955

2021

Circ-ACTR2 aggravates the high glucose-induced cell dysfunction of human renal mesangial cells through mediating the miR-205-5p/HMGA2 axis in diabetic nephropathy.

Applications

Unspecified application

Species

Unspecified reactive species

Jie Yun,Jinyu Ren,Yufei Liu,Lijuan Dai,Liqun Song,Xiaopeng Ma,Shan Luo,Yexu Song

Nephrology (Carlton, Vic.) 26:623-631 PubMed33811432

2021

MiR-1297 attenuates high glucose-induced injury in HK-2 cells via targeting COL1A2.

Applications

Unspecified application

Species

Unspecified reactive species

Shujuan Wang,Kun Sun,Honglei Hu,Xingqian Jin,Zhenzhen Wang,Hongmei Zhang,Xiaodong Zhao

APL bioengineering 4:026105 PubMed32455252

2020

Cell shape, and not 2D migration, predicts extracellular matrix-driven 3D cell invasion in breast cancer.

Applications

Unspecified application

Species

Unspecified reactive species

Janani P Baskaran,Anna Weldy,Justinne Guarin,Gabrielle Munoz,Polina H Shpilker,Michael Kotlik,Nandita Subbiah,Andrew Wishart,Yifan Peng,Miles A Miller,Lenore Cowen,Madeleine J Oudin

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

Oncotarget 8:24902-24914 PubMed28212546

2017

Precursor N-cadherin mediates glial cell line-derived neurotrophic factor-promoted human malignant glioma.

Applications

Unspecified application

Species

Unspecified reactive species

Ye Xiong,Liyun Liu,Shuang Zhu,Baole Zhang,Yuxia Qin,Ruiqin Yao,Hao Zhou,Dian Shuai Gao
View all publications

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