Native Human Collagen IV protein (ab7536)
Key features and details
- Expression system: Native
- Purity: > 95% n/a
- Suitable for: WB, IP, ELISA, Blocking
Description
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Product name
Native Human Collagen IV protein
See all Collagen IV proteins and peptides -
Purity
> 95 % n/a.
This product has been prepared from human placenta by pepsin digestion and is chromatographically and immunologically pure. -
Expression system
Native -
Accession
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Protein length
Full length protein -
Animal free
No -
Nature
Native -
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Species
Human -
Predicted molecular weight
161 kDa -
Additional sequence information
Prepared from human placenta and is chromatographically and immunologically pure.
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Specifications
Our Abpromise guarantee covers the use of ab7536 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
Western blot
Immunoprecipitation
ELISA
Blocking
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Form
Liquid -
Additional notes
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).
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Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped at 4°C. Upon delivery aliquot. Store at +4°C. Store undiluted.
Preservative: 0.01% Sodium azide
Constituent: 3% Acetic acid buffer
General Info
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Alternative names
- Arresten
- BSVD
- CO4A1_HUMAN
see all -
Function
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. Inhibits expression of hypoxia-inducible factor 1alpha and ERK1/2 and p38 MAPK activation. Ligand for alpha1/beta1 integrin. -
Tissue specificity
Highly expressed in placenta. -
Involvement in disease
Defects in COL4A1 are a cause of brain small vessel disease with hemorrhage (BSVDH) [MIM:607595]. Brain small vessel diseases underlie 20 to 30 percent of ischemic strokes and a larger proportion of intracerebral hemorrhages. Inheritance is autosomal dominant.
Defects in COL4A1 are the cause of hereditary angiopathy with nephropathy aneurysms and muscle cramps (HANAC) [MIM:611773]. The clinical renal manifestations include hematuria and bilateral large cysts. Histologic analysis revealed complex basement membrane defects in kidney and skin. The systemic angiopathy appears to affect both small vessels and large arteries.
Defects in COL4A1 are a cause of porencephaly familial (PCEPH) [MIM:175780]. Porencephaly is a term used for any cavitation or cerebrospinal fluid-filled cyst in the brain. Porencephaly type 1 is usually unilateral and results from focal destructive lesions such as fetal vascular occlusion or birth trauma. Type 2, or schizencephalic porencephaly, is usually symmetric and represents a primary defect or arrest in the development of the cerebral ventricles. -
Sequence similarities
Belongs to the type IV collagen family.
Contains 1 collagen IV NC1 (C-terminal non-collagenous) domain. -
Domain
Alpha chains of type IV collagen have a non-collagenous domain (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats in the long central triple-helical domain (which may cause flexibility in the triple helix), and a short N-terminal triple-helical 7S domain. -
Post-translational
modificationsLysines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in all cases and bind carbohydrates.
Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 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 between Lys and Met residues.
Proteolytic processing produces the C-terminal NC1 peptide, arresten. -
Cellular localization
Secreted > extracellular space > extracellular matrix > basement membrane. - Information by UniProt
Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
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SDS download
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Datasheet download
References (7)
ab7536 has been referenced in 7 publications.
- Yun J et al. 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. Diabetol Metab Syndr 13:72 (2021). PubMed: 34174955
- Baskaran JP et al. Cell shape, and not 2D migration, predicts extracellular matrix-driven 3D cell invasion in breast cancer. APL Bioeng 4:026105 (2020). PubMed: 32455252
- Long KR et al. Extracellular Matrix Components HAPLN1, Lumican, and Collagen I Cause Hyaluronic Acid-Dependent Folding of the Developing Human Neocortex. Neuron 99:702-719.e6 (2018). PubMed: 30078576
- Xiong Y et al. Precursor N-cadherin mediates glial cell line-derived neurotrophic factor-promoted human malignant glioma. Oncotarget 8:24902-24914 (2017). PubMed: 28212546
- Sand JM et al. MMP mediated degradation of type IV collagen alpha 1 and alpha 3 chains reflects basement membrane remodeling in experimental and clinical fibrosis--validation of two novel biomarker assays. PLoS One 8:e84934 (2013). ELISA . PubMed: 24376856
- Coelho NM et al. Arrangement of type IV collagen and laminin on substrates with controlled density of -OH groups. Tissue Eng Part A 17:2245-57 (2011). PubMed: 21542695
- Coelho NM et al. Different assembly of type IV collagen on hydrophilic and hydrophobic substrata alters endothelial cells interaction. Eur Cell Mater 19:262-72 (2010). Blocking . PubMed: 20533192