DNAJB6 Antibody | 56-462

DNAJB6 Antibody | 56-462 | Gentaur UK, US & Europe Distribution

Host: Rabbit

Reactivity: Human

Homology: N/A

Immunogen: This DNAJB6 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 218-247 amino acids from the Central region of human DNAJB6.

Research Area: Neuroscience, Signal Transduction

Tested Application: WB, IHC-P, Flow

Application: For WB starting dilution is: 1:1000
For IHC-P starting dilution is: 1:10~50
For FACS starting dilution is: 1:10~50

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: 36 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: DnaJ homolog subfamily B member 6, HHDJ1, Heat shock protein J2, HSJ-2, MRJ, MSJ-1, DNAJB6, HSJ2, MRJ, MSJ1

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

BACKGROUND: This gene encodes a member of the DNAJ protein family. DNAJ family members are characterized by a highly conserved amino acid stretch called the 'J-domain' and function as one of the two major classes of molecular chaperones involved in a wide range of cellular events, such as protein folding and oligomeric protein complex assembly. This family member may also play a role in polyglutamine aggregation in specific neurons. Alternative splicing of this gene results in multiple transcript variants; however, not all variants have been fully described.