Note: You clicked on an external link, which has been disabled in order to keep your shopping session open.
|Tested species reactivity||Rat|
|Published species reactivity||Rat, Hamster, Bovine, Human|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Recombinant MLN64 protein.|
|Purification||Antigen affinity chromatography|
|Storage buffer||PBS with 1mg/ml BSA|
|Contains||0.05% sodium azide|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Western Blot (WB)||1 µg/ml|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
PA1-562 detects MLN64 from rat tissues.
PA1-562 has been successfully used in Western blot procedures. By Western blot, this antibody detects an ~53 kDa protein representing MLN64 from rat adrenal gland tissue extracts. This antibody also detects an ~25 kDa protein from rat adrenal gland which may correspond to degradation product.
PA1-562 antigen is recombinant MLN64 protein.
The steroidogenic acute regulatory (StAR) protein facilitates the movement of cholesterol from the outer to inner mitochondrial membrane in adrenal and gonadal cells, fostering steroid biosynthesis. MLN64 is a 445-amino acid protein of unknown function. When 218 amino-terminal residues of MLN64 are deleted, the resulting N-218 MLN64 has 37% amino acid identity with StAR and 50% of StAR's steroidogenic activity in transfected cells. Bacterially expressed N-218 MLN64 exerts StAR-like activity to promote the transfer of cholesterol from the outer to inner mitochondrial membrane in vitro. The presence of a protease-resistant domain and a protease-sensitive carboxy-terminal domain in N-218 MLN64 is similar to the organization of StAR. However, as MLN64 never enters the mitochondria, the protease-resistant domain of MLN64 cannot be a mitochondrial pause-transfer sequence, as has been proposed for StAR.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Niemann-Pick Type C2 protein contributes to the transport of endosomal cholesterol to mitochondria without interacting with NPC1.
PA1-562 was used in western blot to study the NPC1-independent transport of endosomal cholesterol to mitochondria by Niemann-Pick type C2 protein
|Kennedy BE,Charman M,Karten B||Journal of lipid research (53:2632)||2012|
Effects of interleukin-8 on estradiol and progesterone production by bovine granulosa cells from large follicles and progesterone production by luteinizing granulosa cells in culture.
PA1-562 was used in western blot to study the role of interleukin-8 in steroid synthesis in granulosa cells
|Shimizu T,Kaji A,Murayama C,Magata F,Shirasuna K,Wakamiya K,Okuda K,Miyamoto A||Cytokine (57:175)||2012|
MLN64 mediates egress of cholesterol from endosomes to mitochondria in the absence of functional Niemann-Pick Type C1 protein.
PA1-562 was used in western blot to investigate the role of endosomal metastatic lymph node protein 64 MLN64 in cholesterol mitochondrial transport
|Charman M,Kennedy BE,Osborne N,Karten B||Journal of lipid research (51:1023)||2010|
N-218 MLN64, a protein with StAR-like steroidogenic activity, is folded and cleaved similarly to StAR.
PA1-562 was used in western blot to investigate the functional properties of N-218 MLN64 in comparison with StAR
|Bose HS,Whittal RM,Huang MC,Baldwin MA,Miller WL||Biochemistry (39:11722)||2000|
BMP-4 suppresses progesterone production by inhibiting histone H3 acetylation of StAR in bovine granulosa cells in vitro.
PA1-562 was used in immunocytochemistry to study the mechanism by which BMP-4 inhibits the production of progesterone and the expression of steroidogenic genes.
|Yamashita H,Murayama C,Takasugi R,Miyamoto A,Shimizu T||Molecular and cellular biochemistry (348:183)||2011|
Trafficking from CD63-positive late endocytic multivesicular bodies is essential for intracellular development of Chlamydia trachomatis.
PA1-562 was used in immunocytochemistry to study the intracellular mechanism for chlamydiae infection.
|Beatty WL||Journal of cell science (119:350)||2006|
stAR-related lipid transfer protein 3; StARD3; START domain containing 3