P4HA1 Antibody | 58-934

P4HA1 Antibody | 58-934 | Gentaur UK, US & Europe Distribution

Host: Rabbit

Reactivity: Human

Homology: Predicted species reactivity based on immunogen sequence: Bovine

Immunogen: This P4HA1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 414-442 amino acids from the C-terminal region of human P4HA1.

Research Area: Signal Transduction

Tested Application: WB

Application: For WB starting dilution is: 1:1000

Specificiy: N/A

Positive Control 1: N/A

Positive Control 2: N/A

Positive Control 3: N/A

Positive Control 4: N/A

Positive Control 5: N/A

Positive Control 6: N/A

Molecular Weight: 61 kDa

Validation: N/A

Isoform: N/A

Purification: This antibody is purified through a protein A column, followed by peptide affinity purification.

Clonality: Polyclonal

Clone: N/A

Isotype: Rabbit Ig

Conjugate: Unconjugated

Physical State: Liquid

Buffer: Supplied in PBS with 0.09% (W/V) sodium azide.

Concentration: batch dependent

Storage Condition: Store at 4˚C for three months and -20˚C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.

Alternate Name: Prolyl 4-hydroxylase subunit alpha-1, 4-PH alpha-1, Procollagen-proline, 2-oxoglutarate-4-dioxygenase subunit alpha-1, P4HA1, P4HA

User Note: Optimal dilutions for each application to be determined by the researcher.

BACKGROUND: 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 encoding different isoforms have been described.