ARG21974

anti-Collagen IV antibody [2F11] (Biotin)

anti-Collagen IV antibody [2F11] (Biotin) for ELISA,FLISA,IHC-Frozen sections,IHC-Formalin-fixed paraffin-embedded sections and Human

Angiogenesis Study antibody; Basement Membrane Marker antibody

Overview

Product Description Biotin-conjugated Mouse Monoclonal antibody [2F11] recognizes Collagen IV
Tested Reactivity Hu
Tested Application ELISA, FLISA, IHC-Fr, IHC-P
Specificity Human type IV collagen
Host Mouse
Clonality Monoclonal
Clone 2F11
Isotype IgG1, kappa
Target Name Collagen IV
Antigen Species Human
Immunogen Native Human type IV collagen
Conjugation Biotin
Alternate Names BSVD; RATOR; Collagen alpha-1(IV) chain

Application Instructions

Application Suggestion
Tested Application Dilution
ELISA1:5000 - 1:20000
FLISAAssay-dependent
IHC-FrAssay-dependent
IHC-PAssay-dependent
Application Note * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist.

Properties

Form Liquid
Buffer PBS and 0.1% Sodium azide.
Preservative 0.1% Sodium azide
Concentration 0.5 mg/ml
Storage Instruction Aliquot and store in the dark at 2-8°C. Keep protected from prolonged exposure to light. 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

GeneID: 1282 Human COL4A1

Swiss-port # P02462 Human Collagen alpha-1(IV) chain

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]
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.