Recombinant Human Activin A (INHBA)
| CAT.NO | UNIT | PRICE |
|---|---|---|
| Z101665 | 10 µg | $165.00 |
| Description | Part of the TGF-β family, inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic, pituitary and gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development and bone growth depending on their subunit composition. Activin A is a disulfide linked homodimer (two beta-A chains) that binds to the two forms of activin receptor type I (Act RI-A and Act RI-B) and two forms of activin receptor type II (Act RII-A and Act RII-B). The biological activities of Activin A can be neutralized by inhibins and by the diffusible TGF-β antagonist, follistatin. Recombinant Human Activin A is a homodimeric, non-glycosylated protein that has a molecular weight of 26 kDa. |
|---|---|
| SKU | Z101665 |
| Growth Factor Size | 10 µg |
| Unit quantity | 10 µg |
| Family | TGF-beta Super-family |
| Aliases | Activin beta-A chain, Inhibin beta-A chain, Erythroid differentiation protein, INHBA, FSH releasing protein |
| Gene Symbol | INHBA |
| Gene ID | 3624 |
| Accession Number | P08476 |
| Source | E. coli |
| Species | Human (H. sapiens) |
| Appearance | Lyophilized Powder |
| Molecular Weight | 13 kDa |
| Endotoxin Level | <1.0 EU/µg of recombinant protein as determined by the LAL method |
| Purity | >95% as determined by SDS-PAGE |
| Formulation | Lyophilized from a concentrated protein solution containing 0.02% TFA |
| Function | The ED(50) as determined by the ability to induce cytotoxicity of MPC-11 cells was found to be 1-1.5 ng/ml |
| Reconstitution | A quick spin of the vial followed by reconstitution in sterile distilled water to a concentration not less than 0.1 mg/mL. This solution can then be diluted into other buffers. |
| Storage | The lyophilized protein is stable for at least one year from date of receipt at -70°C. Upon reconstitution, this cytokine can be stored in working aliquots at 2° - 8°C for one month, or at -20°C for six months, with a carrier protein without detectable loss of activity. Avoid repeated freeze/thaw cycles. |
| Usage | For research use only. Not for diagnostic or therapeutic use. |
Supporting Protocol
MSDS
QC
Other
- Growth Factor eFlyer
- Growth Factor and Cytokine Brochure
- Active Kinases Brochure
- Growth Factors and Cytokines Catalogue
- Growth Factors and Cytokines FAQ
- Role of Growth Factors in Cell Differentiation (Poster)
| How are endotoxin levels measured? | |
1. For estimating the endotoxin levels; we use the LAL (Limulus Amebocyte Lysate) method: The lysate from horseshoe crab amebocytes clots in the presence of very low endotoxin. This reaction is the basis of the Limulus amebocyte lysate (LAL) assay which was approved by the FDA in 1970.
· Endotoxin is generally measured in Endotoxin Units per milliliter (EU/mL).
· For recombinant proteins: EU is reported per microgram of protein.
· One EU = 0.1-0.2 ng endotoxin/µg of protein.
· At abm, we do the LAL chromogenic assays that can detect down to 0.01 EU/ml. | |
| With regard to the BSA levels in some Growth Factors and Cytokines, can you please provide an explanation as to why they are so high? | |
The amount of BSA, as part of the formulation of a protein, can vary considerably depending on how much BSA was deemed optimum/necessary for protein stability in combination with /in-lieu of - other possible additives. The aforementioned formulations are somewhat analogous to the “carrier” versions of many formulations from “R and D systems” that have as high as 50 µg of BSA per µg of the recombinant protein product. If, needed or desired, abm scientists can substitute BSA for other stabilizing additives for most formulations. | |
| Are your Escherichia coli sourced growth factors: 1) Human derived materials free? 2) Recombinant proteins free? | |
Yes, all of abm's growth factors made in Escherichia coli using recombinant technology contain no human derived-products or other recombinant proteins. In the rare cases of BSA presence, this will be mentioned in the product's formulation. | |
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