Product: Collagen IV Antibody
Catalog: AF0510
Description: Rabbit polyclonal antibody to Collagen IV
Application: WB IHC IF/ICC
Reactivity: Human, Mouse, Rat
Prediction: Pig, Bovine, Horse, Sheep, Rabbit, Dog, Chicken
Mol.Wt.: 160kDa,300kDa; 161kD(Calculated).
Uniprot: P02462
RRID: AB_2834130

View similar products>>

   Size Price Inventory
 100ul $280 In stock
 200ul $350 In stock

Lead Time: Same day delivery

For pricing and ordering contact:
Local distributors

Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:100-1:500
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Rat
Prediction:
Pig(100%), Bovine(100%), Horse(88%), Sheep(88%), Rabbit(100%), Dog(100%), Chicken(100%)
Clonality:
Polyclonal
Specificity:
Collagen IV Antibody detects endogenous levels of total Collagen IV.
RRID:
AB_2834130
Cite Format: Affinity Biosciences Cat# AF0510, RRID:AB_2834130.
Conjugate:
Unconjugated.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

Arresten; BSVD; CO4A1_HUMAN; COL4A1; collagen alpha-1(IV) chain; collagen type IV alpha 1 chain; RATOR;

Immunogens

Immunogen:
Uniprot:
Gene(ID):
Expression:
P02462 CO4A1_HUMAN:

Highly expressed in placenta.

Description:
COL4A1 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. Belongs to the type IV collagen family. There are six type IV collagen isoforms, alpha 1(IV)- alpha 6(IV), each of which can form a triple helix structure with 2 other chains to generate type IV collagen network. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Sequence:
MGPRLSVWLLLLPAALLLHEEHSRAAAKGGCAGSGCGKCDCHGVKGQKGERGLPGLQGVIGFPGMQGPEGPQGPPGQKGDTGEPGLPGTKGTRGPPGASGYPGNPGLPGIPGQDGPPGPPGIPGCNGTKGERGPLGPPGLPGFAGNPGPPGLPGMKGDPGEILGHVPGMLLKGERGFPGIPGTPGPPGLPGLQGPVGPPGFTGPPGPPGPPGPPGEKGQMGLSFQGPKGDKGDQGVSGPPGVPGQAQVQEKGDFATKGEKGQKGEPGFQGMPGVGEKGEPGKPGPRGKPGKDGDKGEKGSPGFPGEPGYPGLIGRQGPQGEKGEAGPPGPPGIVIGTGPLGEKGERGYPGTPGPRGEPGPKGFPGLPGQPGPPGLPVPGQAGAPGFPGERGEKGDRGFPGTSLPGPSGRDGLPGPPGSPGPPGQPGYTNGIVECQPGPPGDQGPPGIPGQPGFIGEIGEKGQKGESCLICDIDGYRGPPGPQGPPGEIGFPGQPGAKGDRGLPGRDGVAGVPGPQGTPGLIGQPGAKGEPGEFYFDLRLKGDKGDPGFPGQPGMPGRAGSPGRDGHPGLPGPKGSPGSVGLKGERGPPGGVGFPGSRGDTGPPGPPGYGPAGPIGDKGQAGFPGGPGSPGLPGPKGEPGKIVPLPGPPGAEGLPGSPGFPGPQGDRGFPGTPGRPGLPGEKGAVGQPGIGFPGPPGPKGVDGLPGDMGPPGTPGRPGFNGLPGNPGVQGQKGEPGVGLPGLKGLPGLPGIPGTPGEKGSIGVPGVPGEHGAIGPPGLQGIRGEPGPPGLPGSVGSPGVPGIGPPGARGPPGGQGPPGLSGPPGIKGEKGFPGFPGLDMPGPKGDKGAQGLPGITGQSGLPGLPGQQGAPGIPGFPGSKGEMGVMGTPGQPGSPGPVGAPGLPGEKGDHGFPGSSGPRGDPGLKGDKGDVGLPGKPGSMDKVDMGSMKGQKGDQGEKGQIGPIGEKGSRGDPGTPGVPGKDGQAGQPGQPGPKGDPGISGTPGAPGLPGPKGSVGGMGLPGTPGEKGVPGIPGPQGSPGLPGDKGAKGEKGQAGPPGIGIPGLRGEKGDQGIAGFPGSPGEKGEKGSIGIPGMPGSPGLKGSPGSVGYPGSPGLPGEKGDKGLPGLDGIPGVKGEAGLPGTPGPTGPAGQKGEPGSDGIPGSAGEKGEPGLPGRGFPGFPGAKGDKGSKGEVGFPGLAGSPGIPGSKGEQGFMGPPGPQGQPGLPGSPGHATEGPKGDRGPQGQPGLPGLPGPMGPPGLPGIDGVKGDKGNPGWPGAPGVPGPKGDPGFQGMPGIGGSPGITGSKGDMGPPGVPGFQGPKGLPGLQGIKGDQGDQGVPGAKGLPGPPGPPGPYDIIKGEPGLPGPEGPPGLKGLQGLPGPKGQQGVTGLVGIPGPPGIPGFDGAPGQKGEMGPAGPTGPRGFPGPPGPDGLPGSMGPPGTPSVDHGFLVTRHSQTIDDPQCPSGTKILYHGYSLLYVQGNERAHGQDLGTAGSCLRKFSTMPFLFCNINNVCNFASRNDYSYWLSTPEPMPMSMAPITGENIRPFISRCAVCEAPAMVMAVHSQTIQIPPCPSGWSSLWIGYSFVMHTSAGAEGSGQALASPGSCLEEFRSAPFIECHGRGTCNYYANAYSFWLATIERSEMFKKPTPSTLKAGELRTHVSRCQVCMRRT

Predictions

Predictions:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species
Results
Score
Pig
100
Bovine
100
Dog
100
Chicken
100
Rabbit
100
Horse
88
Sheep
88
Xenopus
0
Zebrafish
0
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P02462 As Substrate

Site PTM Type Enzyme
S6 Phosphorylation
S23 Phosphorylation
Y348 Phosphorylation
S892 Phosphorylation
S1012 Phosphorylation
S1077 Phosphorylation
S1226 Phosphorylation
T1231 Phosphorylation

Research Backgrounds

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.

PTMs:

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. 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. These cross-links are important for the mechanical stability of the basement membrane (By similarity).

Proteolytic processing produces the C-terminal NC1 peptide, arresten.

Subcellular Location:

Secreted>Extracellular space>Extracellular matrix>Basement membrane.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Highly expressed in placenta.

Subunit Structure:

There are six type IV collagen isoforms, alpha 1(IV)-alpha 6(IV), each of which can form a triple helix structure with 2 other chains to generate type IV collagen network.

Family&Domains:

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.

Belongs to the type IV collagen family.

Research Fields

· Cellular Processes > Cellular community - eukaryotes > Focal adhesion.   (View pathway)

· Environmental Information Processing > Signal transduction > PI3K-Akt signaling pathway.   (View pathway)

· Environmental Information Processing > Signaling molecules and interaction > ECM-receptor interaction.   (View pathway)

· Human Diseases > Infectious diseases: Parasitic > Amoebiasis.

· Human Diseases > Infectious diseases: Viral > Human papillomavirus infection.

· Human Diseases > Cancers: Overview > Pathways in cancer.   (View pathway)

· Human Diseases > Cancers: Specific types > Small cell lung cancer.   (View pathway)

· Organismal Systems > Endocrine system > Relaxin signaling pathway.

· Organismal Systems > Digestive system > Protein digestion and absorption.

References

1). Quercetin inhibited mesangial cell proliferation of early diabetic nephropathy through the Hippo pathway. PHARMACOLOGICAL RESEARCH (PubMed: 31220559) [IF=9.3]

Application: IHC    Species: mouse    Sample: renal cortex

Fig. 4. | Effects of quercetin on renal interstitial fibrosis in diabetic mice. (A) PAS, Sirius red and Masson staining of renal cortex sections of diabetic mice. (B)Expression of laminin and type IV collagen in renal cortex of diabetic mice through immunohistochemistry. (C) Statistical analysis of laminin protein expression. (D)Statistical analysis of collagen IV protein expression. Data were expressed as mean ± SD, n = 6.

2). YY1 was indispensable for the alleviation of quercetin on diabetic nephropathy-associated tubulointerstitial inflammation. Phytomedicine (PubMed: 36641979) [IF=7.9]

3). GYY4137, a H2S donor, ameliorates kidney injuries in diabetic mice by modifying renal ROS-associated enzymes. Biomedicine & Pharmacotherapy (PubMed: 37054540) [IF=7.5]

Application: WB    Species: Mouse    Sample: kidney tissues

Fig. 2. Effects of GYY4137 on oxidative stress, kidney injury and early fibrosis in the DN mice. A-B: Western blots (A) and levels of renal nitrotyrosine (NT), 8-hydroxy-2′-deoxyguanosine (8-OHdG), kidney-injury-molecule-1 (KIM1) corrected by actin (B). GYY4137 suppressed NT (81.7 ± 8.6 % of DN, p 

4). Connexin32 Promotes the Activation of Foxo3a to Ameliorate Diabetic Nephropathy via Inhibiting the Polyubiquitination and Degradation of Sirt1. Antioxidants & Redox Signaling (PubMed: 36601735) [IF=6.6]

5). Sodium butyrate ameliorated diabetic nephropathy-associated tubulointerstitial inflammation by modulating tight junction of renal tubular epithelial cells. Food & Function [IF=6.1]

6). YY1 inactivated transcription co-regulator PGC-1α to promote mitochondrial dysfunction of early diabetic nephropathy-associated tubulointerstitial fibrosis. Cell Biology and Toxicology (PubMed: 35445903) [IF=6.1]

7). A Testis-Derived Hydrogel as an Efficient Feeder-Free Culture Platform to Promote Mouse Spermatogonial Stem Cell Proliferation and Differentiation. Frontiers in Cell and Developmental Biology (PubMed: 32509769) [IF=5.5]

Application: IHC    Species: mice    Sample: Testis

FIGURE 2 | Immunohistochemical staining of native testis and decellularized testicular matrix (DTM). (A) Immunohistochemical validation of the essential extracellular matrix proteins of the native testis (laminin, collagen type I, collagen type IV, and fibronectin) in the DTM. Scale bar, 200 µm. (B–E) Relative quantity of collagen I, collagen IV, fibronectin, and laminin. ImageJ software was used to determine the average optical density (AOD). Data were shown as mean ± SD, n = 8. Differences were considered statistically significant at *p < 0.05, **p < 0.01.

8). Fraxin represses NF-κB pathway via inhibiting the activation of epidermal growth factor receptor to ameliorate diabetic renal tubulointerstitial fibrosis. European Journal of Pharmacology (PubMed: 37467841) [IF=5.0]

9). Porphyran-derived oligosaccharides alleviate NAFLD and related cecal microbiota dysbiosis in mice. The FASEB Journal (PubMed: 33948987) [IF=4.8]

10). Network pharmacology analysis of ZiShenWan for diabetic nephropathy and experimental verification of its anti-inflammatory mechanism. Drug Design, Development and Therapy (PubMed: 33883881) [IF=4.8]

Application: IHC    Species: Mice    Sample: renal cells

Figure 8 ZSW treatment regulates the major biomarkers of renal injuries in db/db mice. (A) Nephrin, α-SMA and IV-C expression detected by IHC analysis (400 ×); (B) The positive rate of the IHC results. Data are presented as mean ± SD (n = 3). **P < 0.01, vs db/m group; #P < 0.05, ##P < 0.01, vs NC group.

Load more

Restrictive clause

 

Affinity Biosciences tests all products strictly. Citations are provided as a resource for additional applications that have not been validated by Affinity Biosciences. Please choose the appropriate format for each application and consult Materials and Methods sections for additional details about the use of any product in these publications.

For Research Use Only.
Not for use in diagnostic or therapeutic procedures. Not for resale. Not for distribution without written consent. Affinity Biosciences will not be held responsible for patent infringement or other violations that may occur with the use of our products. Affinity Biosciences, Affinity Biosciences Logo and all other trademarks are the property of Affinity Biosciences LTD.