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Rabbit Polyclonal Collagen IV antibody (STJ98598)
Supplier: St John’s Laboratory Ltd.
Recommended applications: WB, ELISA
Recommended dilution: WB 1:500-2000; ELISA 1:10000-20000
Recommended protocols: check protocols
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Check alternative names for the antibodyExpand
COL4A1 antibody,|Alpha-1 type I collagen antibody|CO1A1_HUMAN antibody|COL1A1 antibody|COL2A1 antibody|COL3A1 antibody|COL4A1 antibody|COL5A1 antibody|Collagen alpha 1 chain antibody|Collagen alpha 1(I) chain antibody|Collagen alpha 1(II) chain antibody|Collagen alpha 1(III) chain antibody|Collagen alpha 1(IV) chain antibody|Collagen alpha 1(V) chain antibody|Collagen alpha-1(I) chain antibody|Collagen I alpha 1 polypeptide antibody|Collagen II alpha 1 polypeptide antibody|Collagen IV alpha 1 polypeptide antibody|Collagen type I alpha 1 antibody|Collagen type II alpha 1 antibody|Collagen type III alpha 1 antibody|Collagen type IV alpha 1 antibody|Collagen type V alpha 1 antibody|EDS4A antibody|Anti-Collagen I + II + III + IV + V antibody (ab24117)
SCBT cat No: sc-166194|sc-166155|sc-166154|sc-133162|sc-20648|
Collagen IV Polyclonal Antibody
|Catalogue No.|| |
Human, Mouse, Rat
Collagen IV Polyclonal Antibody detects endogenous levels of Collagen IV
Synthesized peptide derived from Collagen IV at AA range 1620-1670
|Recommended dilution|| |
WB 1:500-2000; ELISA 1:10000-20000
Collagen IV Antibody was tube-contained. Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Collagen IV Antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
-20 Celsius degree. Avoid repeated freeze/thaw cycles.
|Alternative antibody names|| |
Collagen alpha-1antibody, IV antibody, chain antibody
|Protein names|| |
Collagen alpha-1, IV , chain
|Protein 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.
|Protein tissue specificity|| |
Highly expressed in placenta.
|Involvement in disease|| |
Brain small vessel disease with or without ocular anomalies (BSVD) [MIM:607595]: An autosomal dominant disease characterized by weakening of the blood vessels in the brain and retinal arteriolar tortuosity. In affected individuals, stroke is often the first symptom and is usually caused by bleeding in the brain (hemorrhagic stroke) rather than a lack of blood flow in the brain (ischemic stroke). Patients also have leukoencephalopathy and may experience seizures and migraine headaches accompanied by visual sensations known as auras. . Note: The disease is caused by mutations affecting the gene represented in this entry.; 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. . Note: The disease is caused by mutations affecting the gene represented in this entry.; Porencephaly 1 (POREN1) [MIM:175780]: A neurologic disorder characterized by a fluid-filled cysts or cavities within the cerebral hemispheres, neurologic manifestations, facial paresis, and visual defects. Affected individuals typically have hemiplegia, seizures, and intellectual disability. Porencephaly type 1 is usually unilateral and results from focal destructive lesions such as fetal vascular occlusion or birth trauma. . Note: The disease is caused by mutations affecting the gene represented in this entry.; Intracerebral hemorrhage (ICH) [MIM:614519]: A pathological condition characterized by bleeding into one or both cerebral hemispheres including the basal ganglia and the cerebral cortex. It is often associated with hypertension and craniocerebral trauma. Intracerebral bleeding is a common cause of stroke. . Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.; Tortuosity of retinal arteries (RATOR) [MIM:180000]: A disease characterized by marked tortuosity of second- and third-order retinal arteries with normal first-order arteries and venous system. Most patients manifest variable degrees of symptomatic transient vision loss due to retinal hemorrhage following minor stress or trauma. . Note: The disease is caused by mutations affecting the gene represented in this entry.; Schizencephaly (SCHZC) [MIM:269160]: Extremely rare human congenital disorder characterized by a full-thickness cleft within the cerebral hemispheres. These clefts are lined with gray matter and most commonly involve the parasylvian regions. Large portions of the cerebral hemispheres may be absent and replaced by cerebro-spinal fluid. . Note: The disease is caused by mutations affecting the gene represented in this entry.
|Protein sequence and 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. / Belongs to the type IV collagen family. / Contains 1 collagen IV NC1 (C-terminal non-collagenous) domain.
|Protein post-translational modifications|| |
Lysines 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.
|Protein cellular localization|| |
Secreted > extracellular space > extracellular matrix > basement membrane
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St John’s Laboratory Ltd.
|Product type|| |
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