You searched for: Proteins and Peptides

Supplier: Shenandoah Biotechnology

Interleukin 17AF (IL-17AF) is a heterodimer that is composed of the interleukin 17A (IL-17A) and interleukin 17F (IL-17F) members of the IL-17 family of cytokines. IL-17AF is produced by T helper 17 cells (Th17) following interleukin 23 (IL-23) stimulation. IL-17AF signals through the IL-17RA/IL-17RC receptor complex and functions to regulate inflammatory responses. IL-17AF induces chemokine and airway neutrophilia production, similar in function to IL-17A and IL-17F homodimers. In regard to these functions, IL-17AF is less active than the IL-17A homodimer and shows greater activity than the IL-17F homodimer. Human and rat IL-17AF are active on mouse cells.

Supplier: Prosci

ANGPTL4 (Angiopoietin-like protein 4) mainly expressed in endothelial cells (hypoxia-induced). Regulates angiogenesis and modulates tumorigenesis and directly regulates lipid, glucose, and energy metabolism. Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. ANGPTL4 is a protein consisting of an N-terminal coiled-coil domain and a C-terminal fibrinogen-like domain (FLD). Both domains have distinct biological functions. The coiled-coil domain is responsible for the inhibitory effects on lipoprotein lipase (LPL) converting the active form of LPL into an inactive form, and the FLD domain mediates its antiangiogenic functions. The coiled coil and the FLD domains are separated by a short linker that can be cleaved after secretion. ANGPTL4 appears on the cell surface as the full-length form, where it can be released by heparin treatment. ANGPTL4 protein is then proteolytically cleaved by proprotein convertases (PCs), including furin, PC5/6, paired basic amino acid-cleaving enzyme 4, and PC7.

Supplier: Prosci

RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic-cell-membrane protein, which by interacting with RANKL augments the ability of dendritic cells to stimulate naïve T cell proliferation and to promote the survival of RANK + T cells. RANK is also expressed in a variety of tissues including skeletal muscle, thymus, liver, colon, small intestine and adrenal gland. The RANK/RANKL interaction is important in the regulation of osteoclastogenesis and in dendritic-cell-mediated T cell immune responses. Impairments in RANK signaling have been implicated in the induction of expansile osteolysis and Paget disease of bone (PDB2). Recombinant human sRANK receptor is a 19.3 kDa polypeptide containing the TNFR homologous cysteine rich portion of the extracellular domain of RANK receptor (175 amino acid residues).

Supplier: Thermo Scientific Chemicals

CAS No.: 98824-26-1
Molecular Formula: C162H267N51O48S3
Formula Weight: 3793.35
Storage Temperature: -30°C to -10°C
Physical Form: Solid
Appearance: White to off-white
MDL No.: MFCD00130617

Supplier: Prosci

Tumor necrosis factor receptor superfamily member 1B (TNFRSF1B) is a member of the tumor necrosis factor receptor superfamily. Human TNF RII contains four cysteinerich repeats in its ECD, which shares 58% and 56% amino acid sequence identity with the mouse and rat orthologs, respectively.TNF RII is expressed predominantly on cells of the hematopoietic lineage, such as T and natural killer cells, as well as on endothelial cells, microglia, astrocytes,neurons, oligodendrocytes, cardiac myocytes, thymocytes, and mesenchymal stem cells.TNF RII binds to the membranebound forms of TNF alpha and Lymphotoxin alpha/TNF beta ;soluble TNF is thought to signal predominately through TNF RI.Soluble TNF RII is believed to inhibit TNF biological activity by binding TNF thereby preventing it from activating membrane TNF receptors.

Supplier: Prosci

The prolactin receptor (PRLR) is a member of the class I cytokine/lactogen receptor family which mediates the diverse cellular actions of prolactin in several tissues. PRLRs are expressed in normal and neoplastic human breast tissue, and in most breast cancer cells. PRLR contains an extracellular region that binds prolactin, a transmembrane region, and a cytoplasmatic region required for the activation of the Jak2–Stat5 signal transduction pathway by Prl which is essential for transcriptional activation of all known prolactin regulated genes. PRLRs have also been observed in ovarian follicular cells of mice, pigs, sheep, deer, and humans, as well as in luteal tissue in cow and horse ovaries. Furthermore, PRLR knockout mice exhibit failure of embryonic implantation, reduced number of mature oocytes, and low fertilization rates. Knockout females also display a reduced number of primary follicles.

Supplier: Prosci

Mouse Sonic Hedgehog Homolog (SHH) belongs to a three-protein family called Hedgehog. The other two family members are Indian Hedgehog (IHH) and Desert Hedgehog (DHH). Hedgehog proteins are key signaling molecules in embryonic development. SHH is expressed in various embryonic tissues and plays critical roles in regulating the patterning of many systems, such as limbs and brain. SHH also plays an important role in adult, including the division of adult stem cells and the development of certain cancers and other diseases.Mouse Shh is synthesized as a 437 aa precursor that contains a 24 aa signal sequence and a 413 aa mature region. The mature region is autocatalytically processed into a nonglycosylated, 20 kDa, 174 aa N­terminal fragment (Shh­N), and a catalytic­processing,glycosylated, 34 kDa, 239 aa C­terminal fragment. The 20 kDa Shh­N fragment is the core of the active hedgehog molecule. Mouse Shh­N is 99%, 98%, and 100% aa identical to human, rat and gerbil Shh­N, respectively.

Supplier: Prosci

Triggering receptor expressed on myeloid cells-2 (TREM-2) is a cell surface receptor primarily expressed on macrophages, osteoclasts, microglia and dendritic cells. TREM-2 is one member of the TREM family, inhibiting the releasing of inflammatory mediators, so it is an important in vivo anti-inflammatory receptor. TREM-2 consists of an 18 aa signal sequence, a 153 aa extracellular domain (ECD) with one V-type Ig-like domain, a 21 aa transmembrane (TM) domain, and a 35 aa cytoplasmic tail. A soluble form of TREM-2 (TREM-2b) created by alternate splicing diverges at aa 161. TREM-2 transduces intracellular signals through the adaptor DAP12. After binding of TREM-2 with ligand, the TREM-2/DAP12 (dead-cell-activated-receptor-associated protein)-mediated signal transduction pathway causes a series of intracellular protein tyrosine phosphorylation reactions and enzymatic reactions, which then activate the myeloid cells and participate T cell responses.

Supplier: Prosci

Human Brain-Specific Angiogenesis Inhibitor 3 (BAI3) is a 177 kDa seven-span transmembrane (TM) protein, which is thought to be a member of the secretin receptor family. It is synthesized by neurons of the CNS and likely is a negative regulator of angiogenesis. BAI3 is 1498 amino acids in size. It contains three distinct regions: an N-terminal extracellular domain (ECD) (aa25-883), a 7-TM segment, and a C-terminal cytoplasmic region. The ECD contains four antiangiogenic TSP type 1 repeat (aa296-508), and one GSP domain (aa 816-867) that is likely used to cleave the ECD from the membrane-bound receptor. There is one altermate splice form that shows a deletion of aa 643-665. Over aa 25-880, human BAI3 shares 98% aa identity with mouse BAI3. BAI3 has been reported primarily in the brain, but is also localized to lung, testis, and pancreas. It might be involved in angiogenesis inhibition and suppression of glioblastoma.

Supplier: Thermo Scientific

Supplier: Prosci

Activin Receptor Type-2A is a protein that in humans is encoded by the ACVR2A gene. ACVR2A is an activin type 2 receptor. This gene encodes activin A type II receptor. Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF-beta) superfamily of structurally related signaling proteins. Activins signal through a heteromeric complex of receptor serine kinases which include at least two type I (I and IB) and two type II (II and IIB) receptors. These receptors are all transmembrane proteins, composed of a ligand-binding extracellular domain with cysteine-rich region, a transmembrane domain, and a cytoplasmic domain with predicted serine/threonine specificity. Type I receptors are essential for signaling; and type II receptors are required for binding ligands and for expression of type I receptors. Type I and II receptors form a stable complex after ligand binding, resulting in phosphorylation of type I receptors by type II receptors. Type II receptors are considered to be constitutively active kinases.

Supplier: Prosci

Vascular Endothelial Growth Factor (VEGF)-C is a member of the VEGF family, a group of polypeptide growth factors which play key roles in the physiology and pathology of many aspects of the cardiovascular system, including vasculogenesis, hematopoiesis, angiogenesis and vascular permeability. While VEGFC is homologous to other members of the VEGF/PDGF family, it contains the C-terminal propeptide which has an unusual structure with tandemly repeated cysteine-rich motifs. Upon biosynthesis, VEGFC is secreted as a non-covalent momodimer in an anti-parellel fashion. VEGF signalling in endothelial cells occurs through three tyrosine kinase receptors (VEGFRs) expressed by endothelial cells and hematopoietic precursors, and VEGF-C is a ligand for two receptors, VEGFR-3 (Flt4), and VEGFR-2. It is indicated that VEGFC undergoes a complex proteolytic maturation generating a variety of processed secreted forms with increased activity toward VEGFR-3, but only the fully processed form could activate VEGFR-2. VEGFC may function in angiogenesis of the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentiated lymphatic endothelium in adults. Knockout of the VEGF-C gene is embryonic lethal late in development, and although cells differentiate into the lymphatic lineage, they fail to sprout and form lymphatic vessels. Inactivation of a single VEGF-C allele results in the development of cutaneous lymphatic hypoplasia and lymphedema.

Supplier: MilliporeSigma

Active in cell adhesion and cell-surface receptor binding and in stimulating cell migration.

Supplier: Thermo Scientific Chemicals

Selective and irreversible cysteine proteas

Supplier: Prosci

Fibroblast growth factor 21 (FGF-21) is a member of the fibroblast growth factor family and has been identified as an important regulator of energy metabolism connecting nutrition, growth, reproduction and longevity. FGF-21 lacks the heparin-binding domain of most FGF proteins, allowing its secretion. FGF-21 is abundantly expressed in adipose tissues, liver and pancreas. In adipose tissue, FGF-21 promotes glucose uptake and oxidation and in liver it replenishes on fasting the tissues with fuel on low nutritional supply. It also induces lipolysis and ketogenesis. FGF-21 acts through FGF receptors (FGFR) associated with the auxiliary protein beta-Klotho. Recently, FGF-21 has been reported to interact directly with the brain circadian clock to coordinate activity and reproduction as part of the adaptation to fasting. Due to its multiple functions of normalizing glucose, lipid and energy homeostasis, FGF-21 represents an attractive novel therapy for type 2 diabetes mellitus and obesity.

Supplier: Thermo Scientific Chemicals

Powder

Supplier: Prosci

Interleukin-1 receptor type 2 (IL1R2) is also known as CD121 antigen-like family member B (CDw121b), IL-1 type II receptor, Interleukin-1 receptor type II, belongs to the interleukin-1 receptor family. Two distinct types of IL1 receptors which are able to bind IL1 specifically have been identified, designated as IL1RI (IL1RA) and IL1RII (IL1RB). IL1R2 is non-signaling receptor for IL1A, IL1B and IL1RN, reduces IL1B activities. Serves as a decoy receptor by competetive binding to IL1B and preventing its binding to IL1R1. IL1R2 modulates cellular response through non-signaling association with IL1RAP after binding to IL1B. IL1R2 (membrane and secreted forms) preferentially binds IL1B and poorly IL1A and IL1RN. The secreted IL1R2 recruits secreted IL1RAP with high affinity; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors.

Supplier: Thermo Scientific

Thermo Scientific PageRuler Prestained NIR Protein Ladder is a mixture of 10 proteins (11 to 250KDa) that are blue-stained and fluor-labeled for near-IR fluorescent visualization and protein sizing following electrophoresis.

Supplier: Thermo Scientific Chemicals

Powder

Supplier: Rockland Immunochemical

0.5mg. Protein Concentration: 1 mg/mL. Buffer: 0.1M sodium acetate, pH 4.5. Stabilizer: None. For research. Sterile filtered liquid.

Supplier: Rockland Immunochemical

0.5mg. Protein Concentration: 1 mg/mL. Buffer: 0.1M sodium acetate, pH 4.5. Stabilizer: None. For research. Sterile filtered liquid.

Supplier: Prosci

Epithelial Cell Adhesion Molecule (EpCAM) is a signal type I transmembrane glycoprotein that belongs to the EPCAM family. EpCAM is composed of an extracellular domain with one thyroglobulin type-1 domain, a transmembrane domain and a cytoplasmic domain. EpCAM is found on the surface of adenocarcinoma, but not on mesodermal or neural cell membranes. The EpCAM molecule has been shown to function as a homophilic Ca2+ independent adhesion molecule. It may act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium as an immunological barrier providing the first line of defense against infection. Defects in EPCAM are a cause of hereditary non-polyposis colorectal cancer type 8 (HNPCC8) and diarrhea type 5 (DIAR5). EpCAM plays a role in embryonic stem cells proliferation and differentiation; it up-regulates the expression of FABP5, MYC and Cyclin A and Cyclin E. It is highly and selectively expressed by undifferentiated embryonic stem cells.

Supplier: Prosci

CD3e molecule, epsilon is also known as CD3E, is a T-cell surface single-pass type I membrane glycoprotein. CD3E contains 1 Ig-like (immunoglobulin-like) domain and 1 ITAM domain. CD3E, together with CD3-gamma, CD3-delta and CD3-zeta, and the T-cell receptor alpha/beta and gamma/delta heterodimers, forms the T cell receptor-CD3 complex. This complex plays an important role in coupling antigen recognition to several intracellular signal-transduction pathways. The genes encoding the epsilon, gamma and delta polypeptides are located in the same cluster on chromosome 11. The epsilon polypeptide plays an essential role in T-cell development. CD3E plays an essential role in T-cell development, and defects in CD3E gene cause severe immunodeficiency. CD3E gene has also been linked to a susceptibility to type I diabetes in women. CD3E has been shown to interact with TOP2B, CD3EAP and NCK2.

Supplier: Prosci

CD3e molecule, epsilon is also known as CD3E, is a T-cell surface single-pass type I membrane glycoprotein. CD3E contains 1 Ig-like (immunoglobulin-like) domain and 1 ITAM domain. CD3E, together with CD3-gamma, CD3-delta and CD3-zeta, and the T-cell receptor alpha/beta and gamma/delta heterodimers, forms the T cell receptor-CD3 complex. This complex plays an important role in coupling antigen recognition to several intracellular signal-transduction pathways. The genes encoding the epsilon, gamma and delta polypeptides are located in the same cluster on chromosome 11. The epsilon polypeptide plays an essential role in T-cell development. CD3E plays an essential role in T-cell development, and defects in CD3E gene cause severe immunodeficiency. CD3E gene has also been linked to a susceptibility to type I diabetes in women. CD3E has been shown to interact with TOP2B, CD3EAP and NCK2.

Supplier: Thermo Scientific Chemicals

Protease inhibitor that acts on pepsin, renin and cathepsin D

Supplier: Prosci

CD30 ligand (CD30L) is a type-II membrane-associated glycoprotein protein belonging to the TNF superfamily and is expressed primarily on certain B cells, T cells, and monocytes. CD30L binds specifically to CD30 (receptor), which is expressed on activated, but not resting, B and T cells, in lymphomas and various chronically inflamed tissues. CD30L/CD30 interactions initiate a signaling cascade that can ultimately lead to the activation of NF-KappaB. CD30L/CD30 signaling exerts pleiotropic effects on normal cells, including cell death, differentiation, or cell division. Certain diseases, including Hodgkins’s lymphoma, allergic inflammation, diabetes (in NOD mice), and mycobacterial infection can also be affected by CD30L/CD30 signaling. The CD30L gene encodes for a 234 amino acid type II transmembrane protein, which contains a 37 amino acid cytoplasmic sequence, a 25 amino acid transmembrane domain and a 172 amino acid extracellular domain. Recombinant human soluble CD30L (sCD30L) is a 188 amino acid polypeptide corresponding to the extracellular domain, and contains an 8 residue N-terminal His -Tag.

Supplier: MilliporeSigma

Pepstatin A is a reversible inhibitor of aspartic proteases and inhibits cathepsin D, pepsin, and renin.

Supplier: Thermo Scientific Chemicals

a, human

Supplier: Rockland Immunochemical

0.5mg. Protein Concentration: 1 mg/mL. Buffer: 0.5M acetic acid. Stabilizer: None. Preservative: 0.01% (w/v) sodium azide. For research. Sterile filtered liquid.

Supplier: New England Biolabs (NEB)

E. coli RecA is necessary for genetic recombination, reactions involving DNA repair and UV-induced mutagenesis. RecA promotes the autodigestion of the lexA repressor, umuD protein and lambda repressor. Cleavage of LexA derepresses more than 20 genes. In vitro studies indicate that in the presence of ATP, RecA promotes the strand exchange of single-strand DNA fragments with homologous duplex DNA. The reaction has three distinct steps: (i) RecA polymerizes on the single-strand DNA, (ii) the nucleoprotein filament binds the duplex DNA and searches for a homologous region, (iii) the strands are exchanged.