For research use only.
| Verified Samples | Verified Samples in WB: Rat colon |
| Dilution | WB 1:500-1:1000 |
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Rat |
| Applications | WB |
| Clonality | Polyclonal |
| Immunogen | Recombinant Mouse MCSF protein expressed by E.coli |
| Abbre | MCSF |
| Synonyms | Macrophage colony-stimulating factor, TNFSF, Ath, Ath1, Ath-1, CD134, CD134L, CSF-1, gp3, gp34, Macrophage colony-stimulating factor 1, MCSF, M-CSF, OX4, OX-40L, TNFSF4, Tnlg2b, Txgp, TXGP1, Txgp1l, Csfm, Csf1, Ath-, Txgp |
| Swissprot | |
| Calculated MW | 61 kDa |
| Observed MW | 43 kDa The actual band is not consistent with the expectation. Western blotting is a method for detecting a certain protein in a complex sample based on the specific binding of antigen and antibody. Different proteins can be divided into bands based on different mobility rates. The mobility is affected by many factors, which may cause the observed band size to be inconsistent with the expected size. The common factors include: 1. Post-translational modifications: For example, modifications such as glycosylation, phosphorylation, methylation, and acetylation will increase the molecular weight of the protein. 2. Splicing variants: Different expression patterns of various mRNA splicing bodies may produce proteins of different sizes. 3. Post-translational cleavage: Many proteins are first synthesized into precursor proteins and then cleaved to form active forms, such as COL1A1. 4. Relative charge: the composition of amino acids (the proportion of charged amino acids and uncharged amino acids). 5. Formation of multimers: For example, in protein dimer, strong interactions between proteins can cause the bands to be larger. However, the use of reducing conditions can usually avoid the formation of multimers. If a protein in a sample has different modified forms at the same time, multiple bands may be detected on the membrane. |
| Cellular Localization | Cell membrane |
| Concentration | 1 mg/mL |
| Buffer | PBS with 0.05% proclin 300, 1% protective protein and 50% glycerol,pH7.4 |
| Purification Method | Antigen Affinity Purification |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | The product is shipped with ice pack, upon receipt, store it immediately at the temperature recommended. |
| background | M-CSF, also known as CSF-1, is a four-alpha -helical-bundle cytokine that is the primary regulator of macrophage survival, proliferation and differentiation. M-CSF protein is also essential for the survival and proliferation of osteoclast progenitors. M-CSF also primes and enhances macrophage killing of tumor cells and microorganisms, regulates the release of cytokines and other inflammatory modulators from macrophages, and stimulates pinocytosis. M-CSF increases during pregnancy to support implantation and growth of the decidua and placenta. Sources of M-CSF include fibroblasts, activated macrophages, endometrial secretory epithelium, bone marrow stromal cells and activated endothelial cells. The M-CSF receptor (c-fms) transduces its pleotropic effects and mediates its endocytosis. M-CSF mRNAs of various sizes occur. Full length mouse M-CSF transcripts encode a 520 amino acid (aa) type I transmembrane (TM) protein with a 462 aa extracellular region, a 21 aa TM domain, and a 37 aa cytoplasmic tail that forms a 140 kDa covalent dimer. Differential processing produces two proteolytically cleaved, secreted dimers. One is an N- and O- glycosylated 86 kDa dimer, while the other is modified by both glycosylation and chondroitin-sulfate proteoglycan (PG) to generate a 200 kDa subunit. Although PG-modified M-CSF protein can circulate, it may be immobilized by attachment to type V collagen. Shorter transcripts encode M‑CSF that lacks cleavage and PG sites and produces an N-glycosylated 68 kDa TM dimer and a slowly produced 44 kDa secreted dimer. Although forms may vary in activity and half-life, all contain the N-terminal 150 aa portion that is necessary and sufficient for interaction with the M-CSF receptor. The first 229 aa of mature mouse M-CSF shares 87%, 83%, 82% and 81% aa identity with corresponding regions of rat, dog, cow and human M-CSF, respectively. Human M‑CSF is active in the mouse, but mouse M-CSF is reported to be species-specific. |
Other Clones
1 Results
Other Formats
1 Results
Unconjugated
