SKU: 45173959204

Biotinylated TGFBR2/TGF-beta RII Fc&Avi Tag Protein, Mouse

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Description

Biotinylated TGFBR2/TGF-beta RII Fc&Avi Tag Protein, MouseProduct Specification Species Mouse Synonyms TGFBR2, TGFR2, TbetaR II, TGFR2 Accession Q62312 1 Amino Acid Sequence Ile24 Asp184, with C terminal hIgG1 Fc and Avitag Expression System HEK293 Molecular Weight 55 70kDa (Reducing) Purity 95% by SDS PAGE Endotoxin <1EU g Physical Appearance Lyophilized Powder Storage Buffer PBS, pH7. 4. Reconstitution Reconstitute at 0. 1 1 mg ml according to the size in ultrapure water after rapid centrifugation.

Product Specification


Species Mouse
Synonyms TGFBR2, TGFR2, TbetaR-II, TGFβR2
Accession Q62312-1
Amino Acid Sequence

Ile24-Asp184, with C-terminal hIgG1 Fc and Avitag

Expression System HEK293
Molecular Weight

55-70kDa (Reducing)

Purity >95% by SDS-PAGE
Endotoxin <1EU/μg
Physical Appearance Lyophilized Powder
Storage Buffer

PBS, pH7.4.

Reconstitution

Reconstitute at 0.1-1 mg/ml according to the size in ultrapure water after rapid centrifugation.

Stability & Storage

· 12 months from date of receipt, lyophilized powder stored at -20 to -80℃.

· 3 months, -20 to -80℃ under sterile conditions after reconstitution.

· 1 week, 2 to 8℃ under sterile conditions after reconstitution.

· Please avoid repeated freeze-thaw cycles.

Reference

1. Biros E, et al. (2011) Meta-analysis of the association between single nucleotide polymorphisms in TGF-β receptor genes and abdominal aortic aneurysm. Atherosclerosis. 219(1):218-23.

Background

TGFBR2 is a member of the Ser/Thr protein kinase family and the TGFB receptor subfamily. It is a transmembrane protein. TGFBR2 is comprised of a C-terminal protein kinase domain and an N-terminal ectodomain. The ectodomain consists of a compact fold containing nine beta-strands and a single helix stabilized by a network of six intra strand disulfide bonds. The folding topology includes a central five-stranded antiparallel beta-sheet, eight-residues long at its centre, covered by a second layer consisting of two segments of two-stranded antiparallel beta-sheets. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and thus regulates a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and activation of TGFBR1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways.Mutations in TGFBR2 gene have been associated with Marfan syndrome, Loeys-Deitz Aortic Aneurysm Syndrome, and the development of various types of tumors.

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SKU: 45173959204

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Big Pumpkin
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While this book raises some thought-provoking points, it ultimately reads like a product of self-righteous elites disconnected from reality and from the American public. 1. Ignores public opinion. The author never acknowledges that polls consistently show Americans oppose racial preferences in college admissions. Proposition 16—which would have allowed such preferences—was defeated by a wide margin in 2020 in California, one of the nation’s most liberal states. A Brookings poll found that virtually all racial groups, including Black respondents, supported the Supreme Court’s Students for Fair Admissions (SFFA) decision. 2. Starts with a strange premise. The first chapter claims conservatives will “regret” the SFFA ruling because universities will continue racial preferences covertly. But that sidesteps the real question: why shouldn’t colleges comply with the ruling’s letter and spirit? 3. Offers dubious legal advice. In Chapter Three, the author—himself a law professor—floats risky ideas for “working around” the Supreme Court’s decision. Many of these suggestions rest on shaky legal ground, as anyone familiar with the Second Circuit’s CACAGNY v. Adams, 116 F.4th 161 (2d Cir. 2024), would recognize. 4. Ignores proportionality and real-world outcomes. The book argues for “diversity” preferences without asking how much preference is justified. In reality, Asian American applicants face steep penalties. e.g. Stanley Zhong was rejected by five University of California campuses’ Computer Science programs as an in-state applicant—shortly before Google hired him for a full-time, Ph.D.-level software engineering position. Meanwhile, UC San Diego’s own freshman math-placement data show a surge of students—mostly “underrepresented minorities” favored by UC—placed into remedial courses, some testing at a 4th-grade level. It is hard to see how admitting these students is helping them other than allowing some elites to make themselves feel good or get a promotion. If this book represents what passes for legal scholarship at Yale, the state of American legal education should worry us all.
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