You Searched For: trans-4-Fluoro-L-proline

Catalog Number: (10752-128)

Supplier: Prosci

Description: TMIGD2 (transmembrane and immunoglobulin domain containing 1), also known as immunoglobulin-containing and proline-rich receptor 1 (IGPR1), is novel adhesion molecule that is expressed in multiple tissues, primarily in cells of epithelium and endothelium origins. TMIGD2 is thought to be involved in angiogenesis and regulates cellular morphology, homophilic cell aggregation, and cell-cell interaction. TMIGD2 activity also modulates actin stress fiber formation and focal adhesion and reduces cell migration.

Catalog Number: (76083-580)

Supplier: Bioss

Description: Glycogen synthase kinase 3 (GSK3) is a proline directed serine threonine kinase that was initially identified as a phosphorylating and inactivating glycogen synthase. GSK3 has been implicated in fundamental cell processes such as cell fate determination, metabolism, transcriptional control and oncogenesis. Two isoforms, alpha (GSK3A; OMIM 606784) and beta, show a high degree of amino acid homology within their catalytic domains. GSK3B is involved in energy metabolism, neuronal cell development and body pattern formation.

Catalog Number: (89300-818)

Supplier: Genetex

Description: Rabbit polyclonal to SPRR1B (C-term)

Catalog Number: (10751-272)

Supplier: Prosci

Description: ZIMP7 Antibody: ZIMP7, also known as ZMIZ2, is a novel PIAS (protein inhibitor of activated signal transducer and activator of transcription)-like protein and a transcriptional coactivator. ZIMP7 is expressed most abundantly in testis. The C-terminal proline-rich domain possesses a significant intrinsic transcriptional activity and this activity is inhibited by the N-terminus in the full-length ZIMP7. ZIMP7 and the related protein ZIMP10 interact with PIAS3 and enhances Androgen Receptor (AR)- mediated transcription. The interaction between ZIMP7 and SWI/SNF complex suggests a possible role for ZIMP7 in chromatin modification.

Catalog Number: (10749-222)

Supplier: Prosci

Description: Vinculin is a cytoskeletal protein that plays an important role in the regulation of focal adhesions and embryonic development. Three structural vinculin domains include an amino-terminal head, a short flexible proline-rich region and a carboxy-terminal tail. Expression of vinculin were shown to be affected by the level of actin expression. Vinculin deficiencies are associated with a decrease in cell adhesion and an increase in cell motility, suggesting a possible role in metastatic growth. Defects in VCL are the cause of cardiomyopathy dilated type 1W (CMD1W).

Catalog Number: (10346-800)

Supplier: Bioss

Description: Afadin is a cell-cell adherens junction F-actin binding multidomain protein. Two splice variants of afadin have been described: l-afadin, which is ubiquitously expressed, and the smaller s-afadin, which is abundantly expressed in neural tissue. l-Afadin contains one PDZ domain near its middle followed by three proline-rich and one F-actin-binding region at the carboxyl-terminal. l/s-Afadin is localized to cell-cell junctions and binds several cytoplasmic proteins such as the small GTPase Ras, the tight junction protein ZO-1, and the vinculin binding protein ponsin/SH3P12.

Catalog Number: (103006-232)

Supplier: Anaspec Inc

Description: Beta-Casomorphin-7 is a milk opioid peptide derived from fragment 60-66 of bovine beta-Casein. It strongly stimulates mucin secretion in the rat jejunum through a nervous pathway and mu-opioid receptor activation. The presence of the Tyr-Pro aromatic sequence makes the peptide selective for the mu receptor while the high contents of proline residues in the sequence makes the peptide resistant to degradation by gastrointestinal enzymes.
Sequence: YPFPGPI
MW: 789.9 Da
% Peak area by HPLC: 95
Storage condition: -20° C

Catalog Number: (76101-220)

Supplier: Bioss

Description: Catalyzes the calcium-dependent formation of isopeptide cross-links between glutamine and lysine residues in various proteins, as well as the conjugation of polyamines to proteins. Involved in the formation of the cornified envelope (CE), a specialized component consisting of covalent cross-links of proteins beneath the plasma membrane of terminally differentiated keratinocytes. Catalyzes small proline-rich proteins (SPRR1 and SPRR2) and LOR cross-linking to form small interchain oligomers, which are further cross-linked by TGM1 onto the growing CE scaffold (By similarity). In hair follicles, involved in cross-linking structural proteins to hardening the inner root sheath.

Catalog Number: (10752-064)

Supplier: Prosci

Description: Vinculin is a cytoskeletal protein that plays an important role in the regulation of focal adhesions and embryonic development. Three structural vinculin domains include an amino-terminal head, a short flexible proline-rich region and a carboxy-terminal tail. Expression of vinculin were shown to be affected by the level of actin expression. Vinculin deficiencies are associated with a decrease in cell adhesion and an increase in cell motility, suggesting a possible role in metastatic growth. Defects in VCL are the cause of cardiomyopathy dilated type 1W (CMD1W).

Catalog Number: (10668-728)

Supplier: Bioss

Description: Belongs to the PROCA1 family.

Catalog Number: (77437-458)

Supplier: Bioss

Description: Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2. Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vibronectin, tenascin, laminin, fibronectin, fibrin or casein. Have also dipeptidyl peptidase activity, exhibiting the ability to hydrolyze the prolyl bond two residues from the N-terminus of synthetic dipeptide substrates provided that the penultimate residue is proline, with a preference for Ala-Pro, Ile-Pro, Gly-Pro, Arg-Pro and Pro-Pro. Natural neuropeptide hormones for dipeptidyl peptidase are the neuropeptide Y (NPY), peptide YY (PYY), substance P (TAC1) and brain natriuretic peptide 32 (NPPB) (PubMed:21314817). The plasma membrane form, in association with either DPP4, PLAUR or integrins, is involved in the pericellular proteolysis of the extracellular matrix (ECM), and hence promotes cell adhesion, migration and invasion through the ECM. Plays a role in tissue remodeling during development and wound healing. Participates in the cell invasiveness towards the ECM in malignant melanoma cancers. Enhances tumor growth progression by increasing angiogenesis, collagen fiber degradation and apoptosis and by reducing antitumor response of the immune system. Promotes glioma cell invasion through the brain parenchyma by degrading the proteoglycan brevican. Acts as a tumor suppressor in melanocytic cells through regulation of cell proliferation and survival in a serine protease activity-independent manner.

Catalog Number: (10375-634)

Supplier: Bioss

Description: Vasodilator-stimulated phosphoprotein (VASP) is a member of the Ena-VASP protein family. Ena-VASP family members contain an EHV1 N-terminal domain that binds proteins containing E/DFPPPPXD/E motifs and targets Ena-VASP proteins to focal adhesions. In the mid-region of the protein, family members have a proline-rich domain that binds SH3 and WW domain-containing proteins. Their C-terminal EVH2 domain mediates tetramerization and binds both G and F actin. VASP is associated with filamentous actin formation and likely plays a widespread role in cell adhesion and motility. VASP may also be involved in the intracellular signaling pathways that regulate integrin-extracellular matrix interactions. VASP is regulated by the cyclic nucleotide-dependent kinases PKA and PKG. [provided by RefSeq].

Catalog Number: (10751-534)

Supplier: Prosci

Description: CASKIN2 Antibody: Calcium/calmodulin-dependent serine protein kinase (CASK) is a conserved multi-domain scaffolding protein involved in brain development, synapse formation, and establishment of cell polarity. CASKINs (CASK interacting protein ) interact with CASK and is thought to play a role in CASK function, specifically by coupling CASK to distinct downstream effectors. CASKIN2 is a multidomain protein containing six N-terminal ankyrin repeats, one SH3 domain, and two sterile alpha motif domains followed by a long proline-rich sequence and a short conserved C-terminal domain. It is expressed ubiquitously with highest levels present in fetal and adult liver tissue.

Catalog Number: (89335-892)

Supplier: Genetex

Description: Purity: Purified by antigen-affinity chromatography. Species Reactivity: Human, Mouse Tested Applications: IHC-P, WB Pkg Size: 100 ul

Catalog Number: (10487-612)

Supplier: Bioss

Description: This gene encodes a large protein that contains six ankyrin repeats, as well as a Src homology 3 (SH3) domain and two sterile alpha motif (SAM) domains, which may be involved in protein-protein interactions. The C-terminal portion of this protein is proline-rich and contains a conserved region. A related protein interacts with calcium/calmodulin-dependent serine protein kinase (CASK). Alternative splicing results in multiple transcript variants.

Catalog Number: (10093-004)

Supplier: Proteintech

Description: PSTPIP1 (proline-serine-threonine phosphatase interacting protein 1), also known as CD2BP1, is a cytoskeleton-associated adaptor protein that links PEST-type phosphatases to their substrates . It is involved in regulation of the actin cytoskeleton. Preferentially expressed in hematopoetic tissues, PSTPIP1 binds to the cytoplasmic tail of CD2, negatively affecting CD2-triggered T cell activation . It has also been shown to interact with ABL1, PTPN18, WAS, CD2AP, PTPN12 and MEFV/pyrin. Mutations in the gene of PSTPIP1 cause PAPA syndrome (Pyogenic sterile Arthritis, Pyoderma gangrenosum, and Acne), an autoinflammatory disease .