ARG21968
anti-Collagen IV antibody, pre-adsorbed
anti-Collagen IV antibody, pre-adsorbed for Electron microscopy,ELISA,FLISA,Flow cytometry,ICC/IF,IHC-Formalin-fixed paraffin-embedded sections,IHC-Frozen sections,Immunoprecipitation,Western blot and Bovine,Human,Mouse,Rat
Angiogenesis Study antibody; Basement Membrane Marker antibody
Overview
Product Description | Goat Polyclonal antibody recognizes Collagen IV |
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Tested Reactivity | Hu, Ms, Rat, Bov |
Tested Application | ELISA, EM, FACS, FLISA, ICC/IF, IHC-Fr, IHC-P, IP, WB |
Specificity | The antibody reacts with conformational determinants on type IV collagen. The antibody is pre-adsorbed with Collagen types I, II, III, V and VI, so the antibody may not react with Collagen types I, II, III, V and VI. |
Host | Goat |
Clonality | Polyclonal |
Isotype | IgG |
Target Name | Collagen IV |
Antigen Species | Human |
Immunogen | Human type IV collagen |
Conjugation | Un-conjugated |
Alternate Names | BSVD; RATOR; Collagen alpha-1(IV) chain |
Application Instructions
Pre Adsorbed | Collagen types I, II, III, V and VI. | ||||||||||||||||||||
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Application Suggestion |
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Application Note | * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. |
Properties
Form | Liquid |
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Purification | Affinity purification with immunogen. |
Buffer | BBS (pH 8.2) |
Concentration | 0.4 mg/ml |
Storage Instruction | For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use. |
Note | For laboratory research only, not for drug, diagnostic or other use. |
Bioinformation
Database Links | |
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Gene Symbol | COL4A1 |
Gene Full Name | collagen, type IV, alpha 1 |
Background | Collagen IV proteins are integral components of basement membranes. This gene shares a bidirectional promoter with a paralogous gene on the opposite strand. The protein consists of an amino-terminal 7S domain, a triple-helix forming collagenous domain, and a carboxy-terminal non-collagenous domain. It functions as part of a heterotrimer and interacts with other extracellular matrix components such as perlecans, proteoglycans, and laminins. In addition, proteolytic cleavage of the non-collagenous carboxy-terminal domain results in a biologically active fragment known as arresten, which has anti-angiogenic and tumor suppressor properties. Mutations in this gene cause porencephaly, cerebrovascular disease, and renal and muscular defects. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2014] |
Function | Collagen IV 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. [UniProt] |
Highlight | Related Antibody Duos and Panels: ARG30328 Angiogenesis Antibody Panel Related products: Collagen IV antibodies; Collagen IV Duos / Panels; Anti-Goat IgG secondary antibodies; Related news: Gene therapy for retinitis pigmentosa (RP) |
Research Area | Angiogenesis Study antibody; Basement Membrane Marker antibody |
Calculated MW | 161 kDa |
PTM | 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. |