Product Name: BMPR1B Antibody
Species Reactivity: Human
Tested Applications: IHC-P, WB
Applications: For WB starting dilution is: 1:1000For IHC-P starting dilution is: 1:50~100
User Note: Optimal dilutions for each application to be determined by the researcher.
Predicted Molecular Weight: 57 kDa
Immunogen: This BMPR1B antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 472-502 amino acids from the C-terminal region of human BMPR1B.
Host Species: Rabbit
Purification: This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis
Physical State: Liquid
CAS NO.: 108963-70-8
Product: D-Lys(Z)-Pro-Arg-pNA (diacetate)
Buffer: Supplied in PBS with 0.09% (W/V) sodium azide.
Concentration:
Storage Conditions: 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.
Clonality: Polyclonal
Conjugate: Unconjugated
Alternate Names: Bone morphogenetic protein receptor type-1B, BMP type-1B receptor, BMPR-1B, CDw293, BMPR1B
Accession NO.: O00238
Protein Ino:
Official Symbol: BMPR1B
Geneid: 658
Background: The bone morphogenetic protein (BMP) receptors are a family of transmembrane serine/threonine kinases that include the type I receptors BMPR1A and BMPR1B and the type II receptor BMPR2. These receptors are also closely related to the activin receptors, ACVR1 and ACVR2. The ligands of these receptors are members of the TGF-beta superfamily. TGF-betas and activins transduce their signals through the formation of heteromeric complexes with 2 different types of serine (threonine) kinase receptors: type I receptors of about 50-55 kD and type II receptors of about 70-80 kD. Type II receptors bind ligands in the absence of type I receptors, but they require their respective type I receptors for signaling, whereas type I receptors require their respective type II receptors for ligand binding.
PubMed ID:http://aac.asm.org/content/42/4/903.abstract
