Prolyl-4-Hydroxylase Alpha Polypeptide III (P4HA3) Antibody

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Description
This gene encodes a component of prolyl 4-hydroxylase, a key enzyme in collagen synthesis composed of two identical alpha subunits and two beta subunits. The encoded protein is one of several different types of alpha subunits and provides the major part of the catalytic site of the active enzyme. In collagen and related proteins, prolyl 4-hydroxylase catalyzes the formation of 4-hydroxyproline that is essential to the proper three-dimensional folding of newly synthesized procollagen chains. Alternatively spliced transcript variants have been observed, but their full-length nature has not been determined.
Documents del producto
Product specifications
Category | Primary Antibodies |
Immunogen Target | Prolyl-4-Hydroxylase Alpha Polypeptide III (P4HA3) |
Host | Rabbit |
Reactivity | Human |
Recommended Dilution | WB: 1/1000. Optimal dilutions/concentrations should be determined by the end user. |
Clonality | Polyclonal |
Conjugation | Unconjugated |
Isotype | IgG |
Purification | Purified through a protein A column, followed by peptide affinity purification. |
Size 1 | 80 µl |
Size 2 | 400 µl |
Form | Liquid |
Tested Applications | ELISA, WB |
Buffer | PBS containing 0.09% sodium azide. |
Availability | Shipped within 5-10 working days. |
Storage | Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles. |
Dry Ice | No |
UniProt ID | Q7Z4N8 |
Background | Antibody anti-P4HA3 |
Status | RUO |
Descripción
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Catalyzes the post-translational formation of 4-hydroxyproline in-Xaa-Pro-Gly-sequences in collagens and other proteins.
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Prolyl-4-Hydroxylase Alpha Polypeptide III (P4HA3) Antibody
This gene encodes a component of prolyl 4-hydroxylase, a key enzyme in collagen synthesis composed of two identical alpha subunits and two beta subunits. The encoded protein is one of several different types of alpha subunits and provides the major part of the catalytic site of the active enzyme. In collagen and related proteins, prolyl 4-hydroxylase catalyzes the formation of 4-hydroxyproline that is essential to the proper three-dimensional folding of newly synthesized procollagen chains. Alternatively spliced transcript variants have been observed, but their full-length nature has not been determined.
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