Collagen IV Antibody - #AF0510
|Product:||Collagen IV Antibody|
|Description:||Rabbit polyclonal antibody to Collagen IV|
|Application:||WB IHC IF/ICC|
|Reactivity:||Human, Mouse, Rat|
|Prediction:||Pig, Bovine, Horse, Sheep, Rabbit, Dog, Chicken|
*The optimal dilutions should be determined by the end user.
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.
Cite Format: Affinity Biosciences Cat# AF0510, RRID:AB_2834130.
Arresten; BSVD; CO4A1_HUMAN; COL4A1; collagen alpha-1(IV) chain; collagen type IV alpha 1 chain; RATOR;
Highly expressed in placenta.
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.
High(score>80) Medium(80>score>50) Low(score<50) No confidence
PTMs - P02462 As Substrate
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.
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.
Secreted>Extracellular space>Extracellular matrix>Basement membrane.
Highly expressed in placenta.
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.
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.
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Application: IHC Species: mouse Sample: renal cortex
Application: IHC Species: mice Sample: Testis
Application: IHC Species: Mice Sample: renal cells
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