Technical Data
Bone Morphogenetic Protein 5, Recombinant, Human, Western Blot Positive Control (BMP5)
Molecular Biology Storage: -20CShipping: Blue Ice
The BMPs belong to the TGF- Beta superfamily, whose members are widely represented throughout the animal kingdom. The BMPs are important regulators of key events in the processes of bone formation during embryogenesis, postnatal growth, remodeling and regeneration of the skeleton. The BMPs function by binding to a receptor complex that is found on all normal cells and is composed of type-I and II receptors. The primary unit of bone formation is osteoblast, the bone-forming cell. These osteoblast cells respond to physical loading by transducing signals that alter gene expression patterns, and Cbfa (core binding factor), the osteoblast specific transcription factor plays an important role in osteoblast differentiation and function.
Localization studies in both human and mouse tissues have demonstrated high levels of mRNA expression and protein synthesis for various BMPs in kidney, heart, lung, small intestine, limb bud and teeth. Several BMPs have been implicated in early skeletal development, including BMP-2, -4, -5, -7, -14 (CDMP-1 / GDF-5), other members, such as BMP-3, -6, -7 and 13 (CDMP-2 / GDF-6) may be involved in later stages of skeletal formation. BMP5, a 454aa protein mainly expressed in lungs and liver. (Chr 6). The Bmp5 gene is expressed at the earliest stages of skeletaldevelopment in small, local patterns that prefigure the shapesof future skeletal elements. Based upon a high degree of amino acid sequence homology, BMP5, BMP6, and BMP7 constitute a subfamily within the BMPs.

Recombinant Human BMP-5 protein

BMP-5 Protein: The DNA sequence encoding a chimeric protein containing the human BMP-2 signal peptide and propeptides (aa1-282 of human BMP-2) fused to the human BMP-5 mature chain (aa323-454 of human BMP-5) was expressed in a mouse myeloma cell line, NSO. As a result of cleavage at an alternate dibasic cleavage site within the human BMP-2 propeptide, the majority of the protein in the recombinant human BMP-5 preparation contains the carboxy terminal 35aa residues from the human BMP-2 propeptide. The recombinant BMP-5 is a disulfide-linked homodimeric protein consisting of two 167aa residue subunits with a MW of ~18kD. Due to glycosylation the rhBMP-5 migrates as an ~36kD protein under non-reducing conditions and as doublet of 20kD and 25kD protein under reducing conditions in SDS-PAGE.

Suitable for use in Western Blot. Other applications not tested.

Recommended Dilution:
Western Blot: Load 10ul/lane for good visibility with antibodies.
Optimal dilutions to be determined by the researcher.

Note: SDS may crystallize in cold conditions. It should redissolve by warming before taking it from the stock. It should be heated once prior to loading on gels. If the product has been stored for several weeks, then it may be preferable to add 5ul of fresh 2X sample buffer per 10ul of solution prior to heating and loading on gels. This preparation is not biologically inactive. It is not suitable for ELISA or other applications where native protein is required. This preparation is intended for qualitative purpose and not to serve as standard of known concentration. Do not freeze, thaw, or heat repeatedly.

Storage and Stability:
Lyophilized powder may be stored at -20C. Stable for 12 months at -20C. Reconstitute with sterile buffer or ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20C. Reconstituted product is stable for 6 months at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Purity: Purified
Concentration: As reported
Form: Supplied as a lyophilized powder from PBS, 0.05% sodium azide.

Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.
1.) Kawabata, M et al (1998) Cytokine and Growth Factor Reviews 9: 49-61,
2.) Ebendal, T et al (1998), J. Neurosci. Res. 51: 139-146;
3.) Reddi, A. H (1998), Nature Biotechnology 16: 247-252.

Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.