GORASP1 Antibody | 59-584

GORASP1 Antibody | 59-584 | Gentaur UK, US & Europe Distribution

Host: Rabbit

Reactivity: Human

Homology: N/A

Immunogen: This GORASP1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 91-119 amino acids from the Central region of human GORASP1.

Research Area: Cell Cycle

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: 46 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: Golgi reassembly-stacking protein 1, Golgi peripheral membrane protein p65, Golgi phosphoprotein 5, GOLPH5, Golgi reassembly-stacking protein of 65 kDa, GRASP65, GORASP1, GOLPH5, GRASP65

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

BACKGROUND: The Golgi complex plays a key role in the sorting and modification of proteins exported from the endoplasmic reticulum. The protein encoded by this gene is a membrane protein involved in establishing the stacked structure of the Golgi apparatus. It is a caspase-3 substrate, and cleavage of this encoded protein contributes to Golgi fragmentation in apoptosis. This encoded protein can form a complex with the Golgi matrix protein GOLGA2, and this complex binds to the vesicle docking protein p115. Several alternatively spliced transcript variants of this gene have been identified, but their full-length natures have not been determined.