| Description | Lenti-EF1α-Luc-T2A-Puro, i.e., Lentivirus Expressing Firefly Luciferase and Puromycin, is a recombinant lentivirus developed by aladdin, which can be used in most mammalian cells (including primary cells and stem cells) to moderately express firefly luciferase and puromycin driven by the EF1&#Lenti-EF1α-Luc-T2A-Puro, i.e., Lentivirus Expressing Firefly Luciferase and Puromycin, is a recombinant lentivirus developed by aladdin, which can be used in most mammalian cells (including primary cells and stem cells) to moderately express firefly luciferase and puromycin driven by the EF1α constitutive promoter. The stable infected cells can be selected with puromycin.This product can be used as a positive control or an internal reference for the renilla luciferase reporter gene, and is often used for the construction of firefly luciferase gene-labeled tumor cell lines and subsequent in vivo bioluminescence imaging to facilitate in vivo tracking of tumor cells.The EF1α (EF1a) promoter is a strong mammalian expression promoter derived from the elongation factor 1 alpha (EF1A) gene, which can stably drive the constitutive expression of its downstream genes in a variety of cells, including stem cells, primary cells, hematopoietic cells, etc.T2A is a 2A peptide derived from Thosea asigna virus (TaV). It encodes a short peptide with self-cleaving ability after translation to produce multiple proteins from a single transcript. T2A is currently considered to have the highest cleaving efficiency, which is close to 100% in many cases. The expression levels of upstream and downstream proteins of T2A are similar, but some residues of the T2A peptide will be added to the C-terminus of upstream proteins, while downstream proteins will have additional prolines at the N-terminus. The functions of firefly luciferase and puromycin resistance protein expressed using this product are not affected by thse extra amino acids introduced by T2A.Firefly luciferase is a 61kDa monomer that catalyzes the oxidation of luciferin into oxyluciferin in the presence of ATP, Mg2+ and oxygen, generating the chemiluminescence that can be measured by a luminometer or a liquid scintillation counter. This bioluminescence system has been widely used for detecting gene expressions sensitively and efficiently. The firefly luciferase encoding region in this Lentivirus has been optimized to ensure better expression in mammalian cells.This product can infect almost all mammalian cells. After cell infection, the lentivirus will randomly integrate the target genes into the genomic DNA to enable a stable expression of target proteins in infected cells, even in non-dividing cells. Therefore, this product has been widely used in cell and animal experiments.Aladdin's Lenti-EF1α-Luc-T2A-Puro is a replication-deficient lentivirus. The enhancer function of its 3' LTR is lost, forming a self-inactivating 3' LTR, and the U3 region in the 5' LRT is replaced with the EF1α promoter, which cannot replicate and proliferate after infecting ordinary cells, thereby effectively reducing the risk of this product in living organisms. The multiplicity of infection (MOI) values recommended by aladdin for lentivirus infection of different types of in vitro cultured cells are shown in the table below. Cell line Tissue Cancer/cell type Species MOI A431 Epithelial Carcinoma Human 5 A549 Lung Carcinoma Human 5 Astrocytes Nervous system Primary Human 1 B16-F10 Epithelial Melanoma, metastatic Mouse 5 BMM Bone Marrow Primary Human 8 BxPC-3 Pancreas, epithelial Adenocarcinoma Human 10 H3255 Lung Carcinoma, NSCLC Human 10 HCT116 Colon Carcinoma Human 5 HeLa Cervix Carcinoma, epithelioid Human 3 HEK293T Kidney Tumor Human 5 Hepa1-6 Liver Carcinoma Mouse 3 HMVEC Endothelial Endothelial, microvascular Human 100 HT-29 Colon Adenocarcinoma Human 3 HUVEC Umbilicus Endothelial cells Human 100 Jurkat Blood Leukemia, Acute T cell Human 10 LLC-1 Lung Carcinoma Mouse 6 LNCaP Prostate Carcinoma Human 5 MM200 Skin Melanoma Human 5 MCF-7 Breast Adenocarcinoma Human 2 MDA-MB-231 Breast Adenocarcinoma Human 1 MM-AN Skin Melanoma, metastatic Human 16 MMC Breast Carcinoma Mouse 4 MRC-5 Lung, embryonic Fibroblasts Human 1 NB4 Blood Leukemia, acute promyelocytic Human 10 PC12 Adrenal gland Pheochromocytoma Rat 20 SKOV-3 Ovary Adenocarcinoma Human 15 U-2 OS Bone Osteosarcoma Human 5 Comparisons among Retrovirus, Lentivirus, adeno-associated virus and Adenovirus commonly used in laboratories are shown in the table below. Some characteristics of special viruses may differ from those in the table below. Characteristics Retrovirus Lentivirus AAV Adenovirus Genome ssRNA(+) ssRNA(+) ssDNA dsDNA Coat Enveloped Enveloped Naked Naked Particle size 90-100nm 90-100nm 20-30nm 60-90nm Genome size 7-10kb 9kb 5kb 38-39kb Genome integration Yes Yes No No Packaging capacity 2.5-5kb 2.5-6kb 2.5-4.5kb 3-8kb Infection tropism Dividing cells Dividing and non-dividing cells Dividing and non-dividing cells Dividing and non-dividing cells Relative Transduction Efficiency ND 70% 70% 100% Expression started 48-72h 48-72h 72-96h 24-48h Expression duration ＞ 2 months ＞ 2 months ＞ 6 months 3-4 weeks Expression level Medium Medium Medium High Immune response Low Low Very low High In vivo safety Medium Medium High Low Titer before concentration (IFU/ml) 106 107 1011 107 Titer after concentration (IFU/ml) ND 108 0.5-1×1013 1010 Able to obtain high MOI No (≤ 10 copies integrated) No (≤ 10 copies integrated) Yes Yes Biosafety level BSL-2 BSL-2 BSL-1 BSL-2 The titer of this product is no less than 10^8 transduction unit (TU)/ml, which is suitable for cell or live animal experiments. The TU is determined by the qPCR analysis of genomic DNA extracted from HEK293T cells after 72 hours of infection with this product. Multiplicity of Infection (MOI) is the ratio of the number of viruses to the number of cells when the virus infects cells. When 500,000 cells per well of 6-well plates are infected at 5 MOI, 1 ml of this product can infect 40 wells in total; when 100,000 cells per well of 24-well plates are infected at 5 MOI, 1ml of this product can infect 200 wells. The MOI value can be adjusted and the number of wells that can be infected will change correspondingly.Precautions：Repeated freezing and thawing will reduce the viral titer. If necessary, please store in aliquots after receiving this product. Aliquots must be performed on ice. This product can be stored at 4℃ if it is used within a week, but it should be noted that the viral titer decreases over the time of storage at 4℃. If stored at -80℃ for more than one year, the titer may decrease, and it is recommended to re-titrate this product.Please read Appendix 1 "Safety Specifications for Lentivirus Use" carefully before using this product. The biosafety level of this product is Biosafety Level 2 (BSL-2). Beside following the standard microbiological practices, it is also necessary to pay attention to limiting exposure, biohazard reminders, prominent warning signs, and develop appropriate safety regulations. Effective protections should be taken during virus operation, and any direct skin exposure is not allowed. Please wash your hands immediately after the experiment. It is strictly forbidden to directly contact the virus. In case of accidental contact, please rinse with water immediately, and properly disinfect the skin with 70% ethanol.Any materials, reagents, and samples that have come into contact with the virus should be disinfected by soaking in 1% SDS solution for more than 30 minutes, or sterilized by autoclaving at 121℃ for 30 minutes.This product is for R&D only. Not for drug, household, or other uses.For your safety and health, please wear a lab coat and disposable gloves during the operation.Instructions for Use：1.Determination of infection conditions:MOI (Multiplicity of Infection) definition: the ratio of the number of viruses to the number of cells when the virus infects cells. TU (Transduction Units) Definition: The number of biologically active viral particles. After infecting cells with serial dilutions of the virus, the number of biologically active virus particles is determined based on the number of fluorescent cells or the qPCR assay of extracted cellular genomic DNA. The MOI values required for different types of cells are different, and for the first use of lentivirus, it is necessary to optimize the infection conditions. In theory, the higher the MOI value, the higher the infection efficiency, but with greater cytotoxicity. Therefore, the purpose of the preliminary test is to determine the MOI value that can make the infection efficiency reach a level suitable for observation while ensuring the cell survival rate.The following protocol is provided for HEK293T cells cultured in 24-well plate. For cells cultured in other type of vessels, the following protocol can be adjusted appropriately. a.One day before infection, inoculate 5×104 cells in 0.5ml of complete culture medium per well of a 24-well plate. The cell density should be about 70-80% at the time of virus infection the next day. Note: The specific cell number of inoculations depends on cell type, cell size, cell growth rate and other factors.b.Calculate the required amount of virus to yield the MOI values of 1, 2, 5, 10, and 20, respectively. The calculation formula is as follows:TU = number of cells at infection* × MOIVirus stock solution (µl) = TU / titer (TU/ml) × 1000*Generally, the number of cells on the second day is calculated by doubling the number of inoculated cells, and the cells that proliferate slowly or do not proliferate can be adjusted appropriately.For example: If 20 MOI of virus are needed for infecting 1 × 105 HEK293T cells, the required TU is 2 × 106 TU (1 × 105 × 20)。For a virus stock with a titer of 1×109 TU/ml, the volume of the virus stock will be 2×106 TU / (1×109 TU/ml) × 1000 = 2µl.Note: For a preliminary test of MOI settings for other cell lines, please refer to the table “MOI values recommended by Firefly Luciferase Assay Systeim ( Firefly Luciferase Assay System (RG005) to analyze the expression of firefly luciferase. Appendix: 1.Safety specifications for using of lentivirus:a.As a relatively safe virus, although lentivirus cannot replicate and proliferate in normal cells, the lentivirus genome can integrate into the genome of infected cells, so it still has possible potential biological dangers. We suggest that users should read the specifications carefully before virus operation, and operate in strict accordance with the requirements of the specifications. For more stringent US CDC biosafety levels and their operation and protection requirements, please refer to Appendix 1, or visit the following webpage:https://www.cdc.gov/labs/pdf/CDC-BiosafetyMicrobiologicalBiomedicalLaboratories-2020-P.pdf.b.Biosafety cabinets of corresponding levels should be used for lentivirus operations, and the biosafety levels of different lentiviruses will vary. When using an ordinary laminar hood to operate the virus, please do not turn on the exhaust fan to avoid the dust that may be virus-contaminated being blown to the operator and inhaled.c.Disposable hats, masks, laboratory gloves and special laboratory coats must be worn during the experiments to avoid direct contact with the virus. Virus manipulation is prohibited when there are open wounds on the hands and face.d.Be careful not to produce aerosol or splash when handling the virus. If the laminar hood or other utensils are contaminated by the virus during operation, please clean them with 70% ethanol or 2% SDS solution immediately, or take other appropriate measures.e.If centrifugation is required, use a well-sealed centrifuge tube, or seal it with parafilm and centrifuge, preferably using a centrifuge designated for virus operation.f.The following steps should be followed when observing cell infection with a microscope: Tighten the culture flask or cover the culture plate, clean the outer surface of the culture flask or culture plate with 70% ethanol, and then examine by microscope. After finish examining, clean the microscope bench with 70% ethanol.g.All virus-contaminated pipette tips, centrifuge tubes, culture plates (dishes, bottles), culture solution, gloves, and other consumables should be soaked in disinfectant or 2% SDS overnight before discarding.h.After removing gloves, wash hands with soap or hand sanitizer.i.When virus splashes or virus-containing aerosols contact with eyes, skin or mucous membranes, immediately wash with plenty of water for at least 15 minutes.j.If needles or other sharp instruments containing virus pierce the skin, the wound should be immediately scrubbed with 10% iodophor solution for several minutes, and then rinsed with plenty of water.k.The experimental supplies containing lentiviruses should be kept separately and properly marked.l.Lentivirus safety training or safety warnings must be given to personnel in the same laboratory.2.Biosafety levels and their operation and protection requirements:Summary of Recommended Biosafety Levels for Infectious Agents BSL Agents Practices Primary Barriers and Safety Equipment Facilities (Secondary Barriers) 1 Not known to consistently cause diseases in healthy adults Standard microbiological practices ■ No primary barriers required. ■ PPE: laboratory coats and gloves; eye, face protection, as needed Laboratory bench and sink required 2 ■ Agents associated with human disease ■ Routes of transmission include percutaneous injury, ingestion, mucous membrane exposure SBSL-1 practice plus: ■ Limited access ■ Biohazard warning signs ■ “Sharps” precautions ■ Biosafety manual defining any needed waste decontamination or medical surveillance policies Primary barriers: ■ BSCs or other physical containment devices used for all manipulations of agents that cause splashes or aerosols of infectious materials ■ PPE: Laboratory coats, gloves, face and eye protection, as needed BSL-1 plus: ■ Autoclave available 3 Indigenous or exotic agents that may cause serious or potentially lethal disease through the inhalation route of exposure BSL-2 practice plus: ■ Controlled access ■ Decontamination of all waste ■ Decontamination of laboratory clothing before laundering Primary barriers: ■ BSCs or other physical containment devices used for all open manipulations of agents ■ PPE: Protective laboratory clothing, gloves, face, eye and respiratory protection, as needed BSL-2 plus: ■ Physical separation from access corridors ■ Self-closing, double-door access ■ Exhausted air not recirculated ■ Negative airflow into laboratory ■ Entry through airlock or anteroom ■ Hand washing sink near laboratory exit 4 ■ Dangerous/exotic agents which post high individual risk of aerosol-transmitted laboratory infections that are frequently fatal, for which there are no vaccines or treatments ■ Agents with a close or identical antigenic relationship to an agent requiring BSL-4 until data are available to redesignate the level ■ Related agents with unknown risk of transmission BSL-3 practices plus: ■ Clothing change before entering ■ Shower on exit ■ All material decontaminated on exit from facility Primary barriers: ■ All procedures conducted in Class III BSCs or Class I or II BSCs in combination with full-body, air-supplied, positive pressure suit BSL-3 plus: ■ Separate building or isolated zone ■ Dedicated supply and exhaust, vacuum, and decontamination systems ■ Other requirements outlined in the text BSL, biosafety level; PPE, personal protective equipment... Read More | Protein Purity≥85% by SDS PAGEExtinction CoeffA280 nm = 10.16 at 1.0 mg/ml for pure C3Molecular Weight187,000 Da (2 chains)General DescriptionRat C3 is purified from pooled normal rat serum. C3 is central to the activation of all three pathways of complement activation (Law, S.K.A. and Reid, KProtein Purity≥85% by SDS PAGEExtinction CoeffA280 nm = 10.16 at 1.0 mg/ml for pure C3Molecular Weight187,000 Da (2 chains)General DescriptionRat C3 is purified from pooled normal rat serum. C3 is central to the activation of all three pathways of complement activation (Law, S.K.A. and Reid, K.B.M. (1995)). Initiation of each pathway generates proteolytic enzyme complexes (C3 convertases) which are bound to the target surface. These enzymes cleave a peptide bond in C3 releasing the anaphylatoxin C3a and activating C3b. For a brief time (~60 µs) this nascent C3b is capable of reacting with and covalently coupling to hydroxyl groups on the target surface. Carbohydrates are the favored target, but protein hydroxyls and amino groups also react. This process of tagging the target surface with C3b is called opsonization. The reactive site in nascent C3b is a thioester (Tack B.J., et al. (1980); Pangburn M.K. and MüllerEberhard H.J. (1980)) and C3b is linked to the target through a covalent ester bond (an amide bond is formed if C3b is attached to amino groups). Most of the C3 activated during complement activation never attaches to the surface because its thioester reacts with water forming fluid phase C3b which is rapidly inactivated by factors H and I forming iC3b. Surface-bound C3b is necessary in all three pathways for efficient activation of C5 and formation of C5b-9 complexes that lyse the target cell membrane. Surface-bound C3b and its breakdown products iC3b and C3d are recognized by numerous receptors on lymphoid and phagocytic cells which use the C3b ligand to stimulate antigen presentation to cells of the adaptive immune system. The end result is an expansion of target-specific B-cell and T-cell populations.Physical Characteristics & StructureThe calculated molecular weight of rat C3 based on its amino acid sequence is 184,111daltons (without the signal peptide) and is similar to that of human C3 (185,000 daltons).The molecular weight of rat C3 as determined by SDS/polyacrylamide gel electrophoresis has been reported by Daha, M.R. et al., (1979) to be 187,000 daltons composed of two disulfide linked chains, alpha chain (123,000 daltons) and beta chain (76,000 daltons). The extinction coefficient of rat C3 (E1%/280nm = 10.16) is calculated based on its amino acid sequence using ProtParam and assumes all pairs of Cys residues form cystines (i.e. a pair of cysteine molecules are joined by a disulfide bond). The theoretical pI of rat C3 is 6.12. The normal plasma concentration of C3 inWistar rats has been reported to be 0.581mg/ml (Daha, M.R. et al., (1979)).FunctionThe biological functions of C3 are described above in the General Description section.GeneticsRat C3 chromosome location 9. The NCBI Gene ID number for rat C3 is 24232 and UniProt accession number is P01026.Precautions/Toxicity/HazardsThis protein is purified from animal plasma/serum and therefore precautions appropriate for handling any animal blood-derived product must be used.ReferencesLaw, S.K.A. and Reid, K.B.M. (1995) Complement 2nd Edition (ISBN 0199633568) Oxford University Press, Oxford.Tack BF, Harrison RA, Janatova J, Thomas ML, Prahl JW. (1980) Evidence for presence of an internal thiolester bond in third component of human complement. Proc Natl Acad Sci U S A. 77:5764-8.Pangburn M.K. and Müller-Eberhard H.J. (1980) Relation of putative thioester bond in C3 to activation of the alternative pathway and the binding of C3b to biological targets of complement. J Exp Med. 152:1102-14.Daha MR, Stuffers-Heiman M, Kijlstra A and Van ES LA. (1979) Isolation and characterization of the third component of rat complement. Immunology 36:63-70... Read More | Protein Purity>95% by SDS-PAGEExtinction Coeff.A276 nm = 0.456 at 1.0 mg/mLMolecular Weight8,759 Da (single chain)General DescriptionNatural human C4a is prepared by cleavage of human C4 protein by human C1s. It is produced during activation of both the classical and lectin pathways of complementProtein Purity>95% by SDS-PAGEExtinction Coeff.A276 nm = 0.456 at 1.0 mg/mLMolecular Weight8,759 Da (single chain)General DescriptionNatural human C4a is prepared by cleavage of human C4 protein by human C1s. It is produced during activation of both the classical and lectin pathways of complement. C4a is a member of the anaphylatoxin family of three proteins (C3a, C4a and C5a) produced by the activation of complement (Hugli, T.E. et al. (1981)). It is an unglycosylated polypeptidecontaining 77 amino acids with a molecular mass of 8,759 daltons. Many of the biological functions of C4a are similar to those of C3a, but the specific activities are far below those of C3a. C4a activity is so low, in fact, that it was initially thought to be inactive. These measured activities include inducing muscle contraction in the guinea pig ileum test (spasmogenic activity), desensitization of muscle to C3a stimulation suggesting that the same receptor for both C3a and C4a is involved (tachyphylactic activity) and inducing vascular permeability in human skin (Gorski J.P. et al. (1979)). C4a does not show tachyphylactic activity against C5a or chemotactic activity. Removal of the C-terminal arginine by serum carboxypeptidase N destroys all these activities (Meuller-Ortiz, S.L., et al. (2009)). C4a appears to act through the C3a receptor (C3aR) which is a G-protein coupled receptor found widely distributed on peripheral tissues, lymphoid cells (neutrohphils, monocyes, and eosinophils) and in the central nervous system (astrocytes, neurons and glial cells) (Law, S.K.A. and Reid, K.B.M. (1995)). Physical Characteristics & StructureMolecular weight: 8,759 calculated molecular mass. Observed mass (MALDI-TOF) is 8,762 + 9 mass units. pI = 9.0 to 9.5 (Gorski, J.P. et al. (1981))Amino acid sequence (77 amino acids): NVNFQKAINE KLGQYASPTA KRCCQDGVTR LPMMRSCEQR AARVQQPDCR EPFLSCCQFA ESLRKKSRDK GQAGLQRC4a is thought to be structurally very similar to C3a and C5a to which it is homologous. Thus its 3D structure is probably similar to the X-ray-derived crystal structureof C3a (Huber, R. et al. (1980)) and the NMR derived structure of C3a: Nettesheim, D.G. et al. (1988); Murray, I. et al. (1999).FunctionSee General Description above. C4a exhibits much weaker biological activities than C3a and C5a. Its activity in inducing erythema and edema in human skin is 25,000-fold weaker than that of C5a and 100-fold weaker than C3a per nanomole. The spasmogenic activity of C4a is 2000-fold weaker than C5a and 100-fold weaker than that of C3a. Due to these differences the role of C4a in these responses in vivo is thought to be negligible.AssaysTwo well established assays for C4a and C3a functional activities include induction of contraction in the guinea pig ileum and the permeation of a dye such as trypan blue from the vasculature into skin. The anaphylatoxins also induce mast cell degranulation, (measured as histamine release), platelet aggregation, IL-1 release from monocytes and the release of prostaglandins and leukotrienes from many cells and tissues. The other assays used for C3a (Dodds, A.W. and Sim, R.B. (1997)) should also respond to C4a, but few reports have described utilizing these assays with C4a. ELISA kits for the assay of C4a levels (or more correctly C4a desArg levels) in blood and other fluids are sold by several companies. These measurements are useful for detecting complement activation in vivo, but the interpretation of their meaning is complicated by the fact that clearance of the anaphylatoxins is rapid. In vivoFreshly drawn normal human serum contains significant levels of all three anaphylatoxins. Although these may represent the resting concentration in vivo it is difficult to draw or store blood without some complement activation so a true in vivo concentration is difficult to determine. The presence of EDTA and Futhan in the collection tubes can minimize this background (Pfeifer, P.H. et al. (1999)). Full activation of all C4 in blood (600µg/mL) would result in ~3,400 nM C4a (~30 µg/mL). Due to the low biological activity of C4a it could require activation of most of the C4 in a small region to achieve the micromolar C4a concentrations necessary to elicit a response.RegulationC4a levels are regulated by three processes: formation, inactivation and clearance. There are two enzymes that cleave C4 and release C4a: C1s and MASP-2. C4a is “inactivated” by removal of its C-terminal arginine amino acid. The product C4a desArg (or C4a without the C-terminal arginine) is produced by the action of the plasma enzyme carboxypeptidase N (Mueller-Ortiz S.L. et al. (2009)). The inactivation is rapid and most C4a is converted to C4a desArg within minutes of its formation. Inactivated C4a lack measurable biological activity. Because of the large number of cells bearing C3a/C4areceptors (endothelial, immune, smooth muscle, neuronal, etc.) the capture, internalization and digestion of C4a and C4a desArg probably results in its removal from circulation.DeficienciesA deficiency of C4 or a deficiency of all of the enzymes that cleave C4 to generate C4a could result in the absence of C4a. There are no known complete deficiencies of all ofthe C4 cleaving enzymes. Examples of C4 deficient humans and mice exist (Wessels, M.R. et al. (1995)), but the degree to which pathologies associated with C4 deficiency are due to the lack of C4 or the absence of C4a is unclear. DiseasesThere are no known diseases connected to C4a or C4a desArg. Precautions/Toxicity/HazardsThe source of C4a is human serum, therefore appropriate precautions must be observed even though the source was shown by certified tests to be negative for HBsAg, HTLV-I/II, STS, and for antibodies to HCV, HIV-1 and HIV-II.Injection can cause anaphylatic shock which is a generalized circulatory collapse similar to that caused by an allergic reaction.Hazard Code: B WGK Germany 3... Read More | Purity> 95% by SDS-PAGE and HPLC analyses.FunctionGrowth factor that controls proliferation and cellular differentiation in the retina and bone formation. Plays a key role in regulating apoptosis during retinal development. Establishes dorsal-ventral positional information in the retina and Purity> 95% by SDS-PAGE and HPLC analyses.FunctionGrowth factor that controls proliferation and cellular differentiation in the retina and bone formation. Plays a key role in regulating apoptosis during retinal development. Establishes dorsal-ventral positional information in the retina and controls the formation of the retinotectal map (PubMed:23307924). Required for normal formation of bones and joints in the limbs, skull, digits and axial skeleton. Plays a key role in establishing boundaries between skeletal elements during development. Regulation of GDF6 expression seems to be a mechanism for evolving species-specific changes in skeletal strucutres. Seems to positively regulates differentiation of chondrogenic tissue through the growth factor receptors subunits BMPR1A, BMPR1B, BMPR2 and ACVR2A, leading to the activation of SMAD1-SMAD5-SMAD8 complex. The regulation of chondrogenic differentiation is inhibited by NOG (PubMed:26643732). Also involved in the induction of adipogenesis from mesenchymal stem cells. This mechanism acts through the growth factor receptors subunits BMPR1A, BMPR2 and ACVR2A and the activation of SMAD1-SMAD5-SMAD8 complex and MAPK14/p38... Read More | Purity>95% SDS-PAGE.Additional sequence informationFull length mature chain without signal peptide.FunctionLineage-specific cytokine affecting the proliferation and maturation of megakaryocytes from their committed progenitor cells. It acts at a late stage of megakaryocyte development. It may be Purity>95% SDS-PAGE.Additional sequence informationFull length mature chain without signal peptide.FunctionLineage-specific cytokine affecting the proliferation and maturation of megakaryocytes from their committed progenitor cells. It acts at a late stage of megakaryocyte development. It may be the major physiological regulator of circulating platelets... Read More |