Recombinant Human TGFBR2 Protein, His-tagged
Cat.No. : | TGFBR2-2765H |
Product Overview : | Recombinant Human TGFBR2 Protein (Thr23-Gln166) with a N-His tag was expressed in E. coli. |
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Description : | The protein encoded by this gene is a transmembrane protein that has a protein kinase domain, forms a heterodimeric complex with TGF-beta receptor type-1, and binds TGF-beta. This receptor/ligand complex phosphorylates proteins, which then enter the nucleus and regulate the transcription of genes related to cell proliferation, cell cycle arrest, wound healing, immunosuppression, and tumorigenesis. Mutations in this gene have been associated with Marfan Syndrome, Loeys-Deitz Aortic Aneurysm Syndrome, and the development of various types of tumors. Alternatively spliced transcript variants encoding different isoforms have been characterized. |
Source : | E. coli |
Species : | Human |
Tag : | His |
Form : | Freeze-dried powder |
Molecular Mass : | Predicted Molecular Mass: 16.3 kDa Accurate Molecular Mass: 22 kDa |
Protein length : | Thr23-Gln166 |
Endotoxin : | <1.0 EU per 1µg (determined by the LAL method). |
Purity : | > 97% |
Applications : | Positive Control; Immunogen; SDS-PAGE; WB. |
Stability : | The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37 centigrade for 48h, and no obvious degradation and precipitation were observed. The loss rate is less than 5% within the expiration date under appropriate storage condition. |
Storage : | Avoid repeated freeze/thaw cycles. Store at 2-8 centigrade for one month. Aliquot and store at -80 centigrade for 12 months. |
Storage Buffer : | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
Reconstitution : | Reconstitute in 20mM Tris, 150mM NaCl (pH8.0) to a concentration of 0.1-1.0 mg/mL. Do not vortex. |
Gene Name : | TGFBR2 transforming growth factor, beta receptor II (70/80kDa) [ Homo sapiens (human) ] |
Official Symbol : | TGFBR2 |
Synonyms : | TGFBR2; transforming growth factor, beta receptor II (70/80kDa); MFS2, transforming growth factor, beta receptor II (70 80kD); TGF-beta receptor type-2; tbetaR-II; TGF-beta receptor type II; TGF-beta type II receptor; TGF-beta receptor type IIB; transforming growth factor-beta receptor type II; transforming growth factor beta receptor type IIC; transforming growth factor, beta receptor II (70/80kDa) isoform 1; transforming growth factor, beta receptor II (70/80kDa) isoform 2; AAT3; FAA3; MFS2; RIIC; LDS1B; LDS2B; TAAD2; TGFR-2; TGFbeta-RII; |
Gene ID : | 7048 |
mRNA Refseq : | NM_001024847 |
Protein Refseq : | NP_001020018 |
MIM : | 190182 |
UniProt ID : | P37173 |
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Related Gene
Not For Human Consumption!
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Customer Reviews (3)
Write a reviewTGFBR2 protein's remarkable performance in ELISA and protein electron microscopy structure analysis positions it as a valuable tool in various fields, including cardiovascular research, developmental biology, and molecular medicine.
TGFBR2 protein's utility extends to protein electron microscopy structure analysis, where it plays a crucial role in investigating the detailed architecture and conformational changes of proteins.
TGFBR2 protein is highly recommended for use in various research applications, including ELISA and protein electron microscopy structure analysis.
Q&As (5)
Ask a questionDysregulation of TGF-beta signaling, including TGFBR2, has been associated with autoimmune diseases. Understanding these pathways may provide insights into developing targeted therapies.
Yes, there are ongoing clinical trials exploring the modulation of TGFBR2 for various conditions, including cancer and fibrotic diseases.
TGFBR2 is involved in cardiovascular development and homeostasis. Dysregulation can contribute to conditions like aortic aneurysms and other cardiovascular diseases.
Some studies suggest a potential link between TGFBR2 and neurological disorders. Further research is ongoing to understand its role in conditions like Alzheimer's and Parkinson's disease.
Yes, TGFBR2 is implicated in fibrosis, and targeting it may offer therapeutic options for diseases characterized by excessive tissue scarring.
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