bmp-2

BMP-2 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 16.9 kDa and the accession number is P12643.

BMP-2 Protein, Human, Mouse, Rat, Rhesus, Canine, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 13 kDa and the accession number is C8C060.

BMP-2 Protein, Human, Mouse, Rat, Rhesus, Canine, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 39.5 kDa and the accession number is C8C060.

BMP-2 Protein, Danio rerio (zebrafish), Recombinant is expressed in E. coli expression system. The predicted molecular weight is 13.2 kDa and the accession number is B3DI86.

Enhances bone morphogenetic protein (BMP) signaling in a paracrine manner. In contrast, it inhibits both the activin-A and TGFB1-mediated signaling pathways. KCP Protein, Mouse, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 44.7 kDa and the accession number is Q3U492.

TWSG1 belongs to the twisted gastrulation protein family. TWSG1 from different species are functionally equivalent. In contrast to Drosophila where TWSG1 expression is limited to early embryos, expression of TWSG1 is found throughout mouse and human development. Mutations in the TWSG1 gene cause at least some of the cells on the dorsal half of the embryo to adopt more ventral cell fates. This is thought to involve gradients of the signaling molecule decapentaplegic. TWSG1 may function as a bone morphogenetic protein signalling agonist or antagonize these activities. It can dislodge latent bone morphogenetic proteins and thus provides a permissive signal that allows high BMP signaling in the embryo. TWSG1 is a cofactor in the antagonism of chordin to BMP signaling. It also binds both the vertebrate Decapentaplegic ortholog BMP4 and chordin and forms ternary complexes. Meanwhile, TWSG1 increases binding of chordin to BMP4, potentiates the ability of chordin to induce secondary axes in Xenopus embryos, and enhances chordin cleavage by vertebrate proteases related to tolloid at a site poorly used in the absence of TWSG1. The presence of TWSG1 enhances the secondary axis-inducing activity of 2 products of chordin cleavage.

Brorin, also known as brain-specific chordin-like protein, von Willebrand factor C domain-containing protein 2 and VWC2, is a secreted protein that contains two VWFC domains. VWC2 Brorin is a BMP antagonist that may play a role in neural development. It promotes cell adhesion. VWC2 Brorin is a unique member of the chordin family. It inhibited the activity of bone morphogenetic protein 2 (BMP2) and BMP6 in mouse preosteoblastic MC3T3-E1 cells. Mouse Brorin was predominantly expressed in neural tissues in embryos and also predominantly expressed in the adult brain. In the brain, the expression was detected in neurons, but not glial cells. The neural tissue-specific expression profile of Brorin is quite distinct from that of any other member of the Chordin family. VWC2 Brorin protein promoted neurogenesis, but not astrogenesis, in mouse neural precursor cells. VWC2 Brorin is a novel secreted BMP antagonist that potentially plays roles in neural development and functions.

SMAD2 is a member of the SMAD family. Members of this family mediate signal transduction by the TGF-beta activin BMP-2 4 cytokine superfamily from receptor Ser Thr protein kinases at the cell surface to the nucleus. SMAD2 mediates the signal of the TGF-beta, and therefore regulates multiple cellular processes, such as cell proliferation, apoptosis, and differentiation. SMAD2 is recruited to the TGF-beta receptors through its interaction with the SMAD anchor for receptor activation (SARA) protein. SMAD2 is the downstream signal transducers of TGF-beta-1 in human dental pulp cells. In response to TGF-beta signal, this protein is phosphorylated by the TGF-beta receptors. Phosphorylated SMAD2 is able to form a complex with SMAD4 or SARA. These complexes accumulate in the cell nucleus, where they are directly participating in the regulation of gene expression.

Dermatopontin is a widely expressed noncollagenous protein component of the extracellular matrix. It is a 22 kDa molecule that is tyrosine sulfated but not glycosylated. Dermatopontin is down regulated in fibrotic growths such as leiomyoma and scar tissue, inhibits cell proliferation, accelerates collagen fibril formation, and stabilizes collagen fibrils against low-temperature dissociation, Dermatopontin deficient mice exhibit altered collagen matrix deposition and organization. Dermatopontin seems to mediate adhesion by cell surface integrin binding, may serve as a communication link between the dermal fibroblast cell surface and its extracellular matrix environment, and enhances TGFB1 activity (By similarity). Dermatopontin promotes bone mineralization under the control of the vitamin D receptor and inhibits BMP-2 effects on osteoblast precursors.

Activin RIA, also known as ALK-2, TSK-7L, SKR1, TSR-I, and ACTR-I, is a glycosylated 65 kDa type I receptor in the TGF-beta serine threonine kinase receptor family. Binding of TGF-beta superfamily ligands induces formation of a heterotetrameric complex that contains two chains each of a type I and a type II receptor in multiple combinations. The type II receptors phosphorylate the type I receptors which then phosphorylate and activate Smad signal transduction proteins. Activin RIA functions in a wide variety of growth and differentiation processes including gastrulation, skeletal system development, and cardiac morphogenesis. BMP signaling through Activin RIA is enhanced by the direct interaction between Activin RIA and RGM-B DRAGON, a BMP coreceptor that also associates with other type I and type II receptors. Activin RIA can additionally phosphorylate the coreceptor Endoglin and is required for the inhibitory effect of Endoglin on prostate cancer cell motility.

Mouse Chordin-Like 2, also known as CHL2, is a novel chordin family member with structural homology to CHL1 which is implicated in tumor angiogenesis. The mouse CHL2 gene encodes a 426 amino acids (aa) protein with a 25 aa signal peptide. The mature chain of CHL2 protein contains two potential N-linked glycosylation sites, one putative NLS and three 63 aa cysteine-rich von Willebrand type C repeats (CRs). CHL2 gene is weakly expressed in the liver and kidney, partly expressed in the connective tissues of reproductive organs such as ligaments of the ovary and oviduct in females, and of testis, epididymis and certain male accessory sex glands in males. Recombinant mCHL2 protein interacted directly with five BMPs and one GDF thereby inhibiting, in vitro, several BMP GDF-dependent processes including, osteogenic differentiation of C2C12 mesenchymal progenitor cells by several BMPs, ATDC5 embryonal carcinoma cells by GDF5 and BMP4-dependent lymphohematopoietic (CD34+CD31hi and CD34+CD31lo) progenitor cell development from ES cells. CHL2 may inhibits BMPs activity by blocking their interaction with their receptors, and has a negative regulator effect on the cartilage formation regeneration from immature mesenchymal cells, by preventing or reducing the rate of matrix accumulation. Also, it may play a role during myoblast and osteoblast differentiation, and maturation.

SMAD3 belongs to the SMAD family. Members of this family mediate signal transduction by the TGF-beta activin BMP-2 4 cytokine superfamily from receptor Ser Thr protein kinases at the cell surface to the nucleus. SMAD3 is involved in cell signalling. It modulates signals of activin and TGFβ's. Binding of SMAD3 with SMAD4 enables its transmigration into the nucleus where it forms complexes with other proteins and acts as a transcription factor. SMAD3 is a receptor-regulated SMAD (R-SMAD). In mice, mutation of SMAD3 has been linked to colorectal adenocarcinoma, increased systemic inflammation, and accelerated wound healing. Increased SMAD3 activity has been implicated in the pathogenesis of scleroderma. Smad3 is also a multifaceted regulator in adipose physiology and the pathogenesis of obesity and type 2 diabetes.

Sclerostin (SOST) is a member of the cerberus DAN family, a group of secreted glycoproteins characterized by a cysteine-knot motif. Cerberus DAN family members are putative BMP antagonists, and include Dan, Cerberus, Gremlin, PRDC, and Caronte. While the overall sequence identity between members of the family is low, they have conserved spacing of six cysteine residues. Cerberus and Dan have an additional cysteine residue used for dimerization; however, SOST does not and is secreted as a monomer. SOST was originally identified as an important regulator of bone homeostasis. SOST is expressed by osteoclasts in developing bones of mouse embryos, including both intramembranously forming skull bones and endochondrally forming long bones. SOST plays a physiological role as a negative regulator of bone formation by repressing BMP-induced osteogenesis. SOST has been shown to have unique ligand specificity, binding BMP-5, -6, and -7 with high affinity and BMP-2 and -4 with low affinity.

CALCB, also known as CGPR and calcitonin 2, belongs to the calcitonin family. CALCB is a calcitonin (CT) peptide which may play a role in the mediation of human inflammatory diseases. It is highly expressed in the skin, blood, and cerebrospinal fluid. CGRP immunolabeling (IL) was detected in epidermal keratinocytes at levels that were especially high and widespread in the skin of humans from locations afflicted with postherpetic neuralgia (PHN) and complex region pain syndrome type 1 (CRPS), of monkeys infected with simian immunodeficiency virus, and of rats subjected to L5 L6 spinal nerve ligation, sciatic nerve chronic constriction, and subcutaneous injection of complete Freund's adjuvant. Increased CGRP-IL was also detected in epidermal keratinocytes of transgenic mice with keratin-14 promoter driven overexpression of noggin, an antagonist to BMP-4 signaling. CGPR dilates a variety of vessels including the coronary, cerebral and systemic vasculature.