Description
SELK Antibody | 6975 | Gentaur UK, US & Europe Distribution
Host: Rabbit
Reactivity: Human, Mouse, Rat
Homology: Predicted species reactivity based on immunogen sequence: Bovine: (100%) , Pig: (100%)
Immunogen: SELK antibody was raised against an 18 amino acid synthetic peptide near the carboxy terminus of human SELK.
The immunogen is located within the last 50 amino acids of SELK.
Research Area: Innate Immunity
Tested Application: E, WB, IF
Application: SELK antibody can be used for detection of SELK by Western blot at 1 - 2 μg/mL. For immunofluorescence start at 20 μg/mL.
Antibody validated: Western Blot in mouse samples and Immunofluorescence in human samples. All other applications and species not yet tested.
Specificiy: N/A
Positive Control 1: Cat. No. 1288 - A20 Cell Lysate
Positive Control 2: Cat. No. 10-501 - Human Heart Tissue Slide
Positive Control 3: N/A
Positive Control 4: N/A
Positive Control 5: N/A
Positive Control 6: N/A
Molecular Weight: 10 kDa
Validation: N/A
Isoform: N/A
Purification: SELK Antibody is affinity chromatography purified via peptide column.
Clonality: Polyclonal
Clone: N/A
Isotype: IgG
Conjugate: Unconjugated
Physical State: Liquid
Buffer: SELK Antibody is supplied in PBS containing 0.02% sodium azide.
Concentration: 1 mg/mL
Storage Condition: SELK antibody can be stored 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: SELK Antibody: SelK, HSPC030, HSPC297, Selenoprotein K, SelK
User Note: Optimal dilutions for each application to be determined by the researcher.
BACKGROUND: SELK Antibody: SELK is a selenoprotein, containing a selenocysteine residue at its active site. SELK is localized to the endoplasmic reticulum and is highly expressed in the heart, where it may function as an antioxidant. SELK can bind to proteins such as the ER-associated degradation (ERAD) components p97 ATPase, Derlin-1 and -2, and SelS as well as proteins in the oligosaccharyltransferase complex, suggesting that SELK may be involved in the Derlin-dependent ERAD of glycosylated misfolded proteins. SELK is also thought to be important in Ca2+ flux in immune cells, and is cleaved by m-calpain in resting macrophages. When these macrophages are activated through different Toll-like receptors, this cleavage is inhibited