CREBL1 Antibody | 61-792

CREBL1 Antibody | 61-792 | Gentaur UK, US & Europe Distribution

Host: Rabbit

Reactivity: Human, Mouse, Hamster

Homology: N/A

Immunogen: This CREBL1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 560-589 amino acids from the C-terminal region of human CREBL1.

Research Area: Other

Tested Application: WB, IHC-P

Application: For IHC-P starting dilution is: 1:25
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: 77 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: Cyclic AMP-dependent transcription factor ATF-6 beta, cAMP-dependent transcription factor ATF-6 beta, Activating transcription factor 6 beta, ATF6-beta, Protein G13, cAMP response element-binding protein-related protein, Creb-rp, cAMP-responsive element-binding protein-like 1, Processed cyclic AMP-dependent transcription factor ATF-6 beta, ATF6B, CREBL1, G13

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

BACKGROUND: CREBL1 is a transcription factor in the unfolded protein response (UPR) pathway during ER stress. Either as a homodimer or as a heterodimer with ATF6-alpha, the encoded protein binds to the ER stress response element, interacting with nuclear transcription factor Y to activate UPR target genes. The protein is normally found in the membrane of the endoplasmic reticulum; however, under ER stress, the N-terminal cytoplasmic domain is cleaved from the rest of the protein and translocates to the nucleus.